RESEARCH PRODUCTS

Cambridge Isotope Laboratories, Inc.
isotope.com

Stable Isotope-Labeled
Peptide and Protein
Reagents /Kits
Build Your Dream Standard or
Choose from off the Shelf!
Mass spectrometry (MS) and nuclear magnetic resonance (NMR)
spectroscopy have benefitted greatly from the use of isotopeenriched peptides and proteins. Within the MS field, isotope
dilution mass spectrometry (IDMS) is largely considered thegold standard for quantitative analysis of peptides and proteins.
In contrast, biomolecular NMR spectroscopy typically requires
isotopic enrichment of protein and nucleic acids for determinationof molecular structure and dynamics. Regardless if MS or NMR isused, labeled proteins are produced in vivo using recombinant
cells grown in isotopic cell culture media or in situ using cell-freesynthesis. Cambridge Isotope Laboratories, Inc. (CIL) is pleased
to offer stable isotope-labeled peptide and protein reagentsand kits to aid researchers in the scientific community.

Overview• Peptide synthesis– Protected amino acids and preloaded resins• Protein expression starting materials– Cell growth media– Cell-free protein expression kits
• Isotope-labeled peptides and proteins• QC and quantitation kits for peptide/protein analysis

Peptide Reagents and Kits
Protected Amino Acids
CIL offers more than 130 isotope-enriched protected amino acids
for the solid-phase synthesis of stable isotope-labeled peptides.
Each compound has undergone extensive quality control testingfor identity, chemical purity, and isotopic enrichment. The chemical
purities are ≥98%, unless otherwise specified, while the “H” in the
catalog number denotes a highly enriched amino acid of ≥99%.
Package sizes range from 50 mg to 1 g; however, alternate sizes
may be available. Please inquire or visit isotope.com for pricing
and delivery.

Mass Shift from
Unlabeled (Da)

Catalog No.

Description

CLM-818

L-Alanine-N-FMOC (1-13C, 99%)+1

CLM-3638

L-Alanine-N-FMOC (2-13C, 99%)+1

CLM-1142

L-Alanine-N-FMOC (3-13C, 99%)

+1

NLM-614

L-Alanine-N-FMOC (15N, 98%)

+1

CLM-7785

L-Alanine-N-FMOC (13C3, 97-99%)+3

DLM-7316

L-Alanine-N-FMOC (3,3,3-D3, 98%)

+3

DLM-8168

L-Alanine-N-FMOC (2,3,3,3-D4, 98%)

+4

CNLM-4355-H

L-Alanine-N-FMOC (13C3, 99%; 15N, 99%)

+4

CDNLM-7852

L-Alanine-N-FMOC(13C3, 97-99%; D4, 97-99%; 15N, 97-99%)+8

CLM-2150

L-Alanine-N-t-BOC (1-13C, 99%)+1

CLM-2011

L-Alanine-N-t-BOC (2-13C, 98-99%)+1

CLM-2151

L-Alanine-N-t-BOC (3-13C, 99%)

+1

DLM-649

L-Alanine-N-t-BOC (2-D, 98%)

+1

NLM-1903

L-Alanine-N-t-BOC (15N, 98%)

+1

CNLM-6014

L-Alanine-N-t-BOC (2-13C, 99%; 15N, 96-99%)+2

CLM-3589

L-Alanine-N-t-BOC (13C3, 97-99%)+3

DLM-2793

L-Alanine-N-t-BOC (3,3,3-D3, 99%)

+3

CNLM-2394

L-Alanine-N-t-BOC (13C3, 97-99%; 15N, 97-99%)+4

NLM-8841

L-Arginine-N-FMOC, PBF-OH (15N4, 98%)
contains solvent+4

CLM-8475-H

L-Arginine-N-FMOC, PBF-OH (13C6, 99%)
contains solvent+6

CNLM-8474-H

L-Arginine-N-FMOC, PBF-OH(13C6, 99%; 15N4, 99%) contains solvent+10

NLM-4204

L-Asparagine-N-FMOC, N-b-trityl (15N2, 98%)

+2

CNLM-4354

L-Asparagine-N-FMOC(13C4, 97-99%; 15N2, 97-99%)+6

Note: If equipped to perform FMOC or BOC protection, pleaserefer to our offering of free amino acids in our “Stable Isotope
Standards for Mass Spectrometry” catalog.

Continued ➤Cambridge Isotope Laboratories, Inc.
North America: 1.800.322.1174 cilsales@isotope.com | International: +1.978.749.8000 intlsales@isotope.com | fax: 1.978.749.2768 | isotope.com

| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

Cambridge Isotope Laboratories, Inc.

Protected Amino Acids (continued)
Mass Shift from
Unlabeled (Da)

Catalog No.

Description

L-Asparagine-N-FMOC, N-b-trityl(13C4, 99%; 15N2, 99%)+6

CLM-8043

L-Isoleucine-N-FMOC (1-13C, 99%)

+1

NLM-391

L-Isoleucine-N-FMOC (15N, 98%)

+1

CLM-4249

L-Aspartic acid-N-a-CBZ (13C4, 97-99%)+4

CLM-7794+6

CNLM-4788

L-Aspartic acid-N-FMOC(13C4, 97-99%; 15N, 97-99%)+5

L-Isoleucine-N-FMOC (13C6, 97-99%)

CNLM-4346-H

L-Isoleucine-N-FMOC (13C6, 99%; 15N, 99%)

+7

L-Aspartic acid-N-FMOC, b-O-t-butyl ester(15N, 98%)

+1

NLM-2167

L-Isoleucine-N-t-BOC (15N, 98%)+1

CLM-3691

L-Leucine-N-FMOC (1-13C, 99%)

+1

L-Aspartic acid-N-FMOC, b-O-t-butyl ester(13C4, 99%; 15N, 99%)

+5

NLM-2397

L-Leucine-N-FMOC (15N, 98%)

+1

CLM-7546

L-Leucine-N-FMOC (1,2-13C2, 99%)

+2

NLM-3493

L-Aspartic acid-N-t-BOC(15N, 98%)

+1

DLM-7202

L-Leucine-N-FMOC (5,5,5-D3, 98%)

+3

NLM-1908

L-Aspartic acid-N-t-BOC, b-benzyl ester(15N, 98%)+1

CLM-3683

L-Leucine-N-FMOC (13C6, 97-99%)+6

L-Aspartic acid-N-t-BOC, b-benzyl ester(13C4, 97-99%; 15N, 97-99%)

CNLM-4345-H+7+5

L-Leucine-N-FMOC (13C6, 99%; 15N, 99%)

DLM-7575

L-Leucine-N-FMOC (D10, 98%)

+10

CLM-404

DL-Cysteine, S-benzyl (1-13C, 99%)

+1

CDNLM-7854+17

CNLM-7579

L-Cysteine, N-acetyl (cysteine-13C3, 97-99%;
15
N, 97-99%) CP 95%+4

L-Leucine-N-FMOC(13C6, 97-99%; D10, 97-99%; 15N, 97-99%)

CLM-2155

L-Leucine-N-t-BOC·H2O (1-13C, 99%)

+1

DLM-4721

L-Cysteine-N-FMOC, S-trityl (3,3-D2, 98%)+2

CLM-2010

L-Leucine-N-t-BOC·H2O (2-13C, 99%)

+1

CNLM-4722-H

L-Cysteine-N-FMOC, S-trityl(13C3, 99%; 15N, 99%)

+4

NLM-1904

L-Leucine-N-t-BOC·H2O (15N, 98%)

+1

DLM-2736

L-Leucine-N-t-BOC·H2O (5,5,5-D3, 98%)

+3

CLM-1901

L-Cysteine-N-t-BOC, S-benzyl (3-13C, 99%)

+1

CNLM-2396+7

NLM-3874

L-Cysteine-N-t-BOC, S-p-Mebz (15N, 98%)

+1

L-Leucine-N-t-BOC·H2O(13C6, 97-99%; 15N, 97-99%)

CLM-2182

L-Cysteine, S-benzyl (3-13C, 99%)

+1

DLM-3650

L-Leucine-N-t-BOC·H2O (D10, 98%)

+10

NLM-8960

L-Glutamic acid-N-FMOC, g-t-butyl ester(15N, 98%)

+1

CLM-6194

L-Lysine-a-N-FMOC, e-N-t-BOC (1-13C, 99%)

+1

NLM-4631

L-Lysine-a-N-FMOC, e-N-t-BOC (15N2, 96-98%)+2

CNLM-4753-H

L-Glutamic acid-N-FMOC, g-t-butyl ester(13C5, 99%; 15N, 99%) CP 96%+6

DLM-4731

L-Lysine, N-e-carboxymethyl(4,4,5,5-D4, 96-98%)+4

NLM-1907

L-Glutamic acid-N-t-BOC, g-benzyl ester(15N, 98%)

+1

CLM-7865-H

L-Lysine-a-N-FMOC, e-N-t-BOC (13C6, 99%)

+6

CNLM-4754-H+8

CLM-2008

L-Glutamic acid-N-t-BOC, g-benzyl ester(1,2-13C2, 99%)+2

L-Lysine-a-N-FMOC, e-N-t-BOC(13C6, 99%; 15N2, 99%)

CLM-8166

L-Methionine-N-FMOC (1-13C, 99%)

+1

CNLM-4356-H

L-Glutamine-N-FMOC (13C5, 99%; 15N2, 99%)

+7

NLM-4632

L-Methionine-N-FMOC (15N, 98%) CP 95%+1

CNLM-7252-H

L-Glutamine-N-FMOC, N-g-trityl(13C5, 99%; 15N2, 99%)

+7

CLM-1141

L-Methionine-N-FMOC (methyl-13C, 99%)

+1

CNLM-4358-H

L-Methionine-N-FMOC (13C5, 99%; 15N, 99%)

+6

NLM-3419

L-Glutamine-N-t-BOC (a-15N, 98%)+1

CLM-2156

L-Methionine-N-t-BOC (methyl-13C, 98%)+1

CLM-1902

L-Glutamine-N-t-BOC (1,2-13C2, 99%)+2

CLM-4824

L-Phenylalanine-N-FMOC (1-13C, 99%)+1

CLM-3777

Glycine, N-acetyl (2-13C, 99%)

+1

NLM-1265

L-Phenylalanine-N-FMOC (15N, 98%)

+1

NLM-2377

Glycine, N-benzoyl (15N, 98%)

+1

DLM-7786

L-Phenylalanine-N-FMOC (ring-D5, 98%)

+5

DLM-7703

Glycine, N-benzoyl (benzoyl-D5, 98%)

+5

CLM-3684

L-Phenylalanine-N-FMOC (ring-13C6, 99%)+6

CLM-3639

Glycine-N-FMOC (1-13C, 99%)

+1

DLM-8752

L-Phenylalanine-N-FMOC (D8, 98%)

+8

CLM-2387

Glycine-N-FMOC (2-13C, 99%)

+1

CNLM-4362-H

L-Phenylalanine-N-FMOC (13C9, 99%; 15N, 99%)

+10

NLM-694

Glycine-N-FMOC (15N, 98%)+1

CLM-2170

L-Phenylalanine-N-t-BOC (1-13C, 99%)+1

CLM-7547

Glycine-N-FMOC (13C2, 97-99%)+2

CLM-2009

L-Phenylalanine-N-t-BOC (2-13C, 99%)

+1

DLM-7339

Glycine-N-FMOC (2,2-D2, 98%)

+2

NLM-1905

L-Phenylalanine-N-t-BOC (15N, 98%)

+1

CNLM-7697

Glycine-N-FMOC (1-13C, 99%; 15N, 98%)

+2

DLM-2157

L-Phenylalanine-N-t-BOC (ring-D5, 98%)

+5

CNLM-7698

Glycine-N-FMOC (2-13C, 99%; 15N, 98%)+2

CLM-2061

L-Phenylalanine-N-t-BOC (ring-13C6, 99%)

+6

CNLM-4357-H

Glycine-N-FMOC (13C2, 99%; 15N, 99%)+3

CLM-7859

L-Phenylalanine-N-t-BOC (13C9, 97-99%)+9

CDNLM-7853

Glycine-N-FMOC (13C2, 97-99%;
2,2-D2, 97-99%; 15N, 97-99%)+5

CNLM-2393+10

CLM-2152

Glycine-N-t-BOC (1-13C, 99%)

+1

L-Phenylalanine-N-t-BOC(13C9, 97-99%; 15N, 97-99%)

CLM-8044

L-Proline-N-FMOC (1-13C, 99%)+1

CLM-1900

Glycine-N-t-BOC (2-13C, 99%)

+1

NLM-3906

L-Proline-N-FMOC (15N, 98%)

+1

NLM-2109

Glycine-N-t-BOC (15N, 98%)

+1

NLM-2329

L-Proline-N-t-BOC (15N, 96%)+1

DLM-2153

Glycine-N-t-BOC (2,2-D2, 98%)

+2

CNLM-4347-H

L-Proline-N-FMOC (13C5, 99%; 15N, 99%)

+6

CNLM-9686

Glycine-N-t-BOC (2-13C, 99%; 15N, 98%)

+2

CNLM-8403-H

L-Serine-N-FMOC (13C3, 99%; 15N, 99%)

+4

CNLM-2412

Glycine-N-t-BOC (13C2, 97-99%; 15N, 97-99%)+3

CLM-8167

L-Serine-N-FMOC, O-t-butyl ether (1-13C, 99%)

+1

NLM-8010

L-Histidine-N-FMOC, N-IM-trityl (15N3, 98%)

+3

NLM-4630

L-Serine-N-FMOC, O-t-butyl ether (15N, 98%)

+1

CNLM-4755-H

L-Serine-N-FMOC, O-t-butyl ether(13C3, 99%; 15N, 99%)

+4

Catalog No.

Description

CNLM-6193-H

NLM-647
CNLM-4752-H

CNLM-2392

Chemical purity (CP) is 98% or greater, unless otherwise indicated.
2

North America: 1.800.322.1174 | fax: 1.978.749.2768 | cilsales@isotope.com

Mass Shift from
Unlabeled (Da)| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

isotope.com

Protected Amino Acids (continued)

Preloaded Resins
Mass Shift from
Unlabeled (Da)

Catalog No.

Description

CLM-2007

L-Serine-N-t-BOC, O-benzyl ether (2-13C, 99%)+1

CLM-756

L-Serine-N-t-BOC, O-benzyl ether (3-13C, 99%)

+1

NLM-2025

L-Serine-N-t-BOC, O-benzyl ether (15N, 98%)

+1

NLM-8170

L-Threonine-N-FMOC, O-t-butyl ether (15N, 98%)

+1

CNLM-7615

L-Threonine-N-FMOC, O-t-butyl ether(13C4, 97-99%; 15N, 97-99%)+5

CNLM-7615-H

L-Threonine-N-FMOC, O-t-butyl ether(13C4, 99%; 15N, 99%)

+5

NLM-3681

L-Threonine-N-t-BOC, O-benzyl ether ( N, 98%)

+1

NLM-3423

L-Tryptophan-N-FMOC (a-15N, 98%)

+1

DLM-6113

L-Tryptophan-N-FMOC (indole-D5, 98%)

+5

CNLM-6077

L-Tryptophan-N-FMOC(13C11, 97-99%; 15N2, 97-99%)+13

CLM-2194

L-Tryptophan-N-t-BOC (1-13C, 99%)

+1

NLM-1906

L-Tyrosine-N-t-BOC, O-benzyl ether (15N, 98%)

+1

DLM-2303

L-Tyrosine-N-t-BOC, O-benzyl ether(ring-D4, 98%)

+4

NLM-8169

L-Tyrosine-N-FMOC, O-t-butyl ether (15N, 98%)

+1

CNLM-4349-H

L-Tyrosine-N-FMOC, O-t-butyl ether(13C9, 99%; 15N, 99%)

+10

NLM-7888

L-Valine, N-acetyl (15N, 98%)+1

CLM-3640

L-Valine-N-FMOC (1-13C, 99%)

+1

15

NLM-4243

L-Valine-N-FMOC (15N, 98%)

+1

CLM-7793

L-Valine-N-FMOC (13C5, 97-99%)+5

CNLM-4348-H

L-Valine-N-FMOC (13C5, 99%; 15N, 99%)

+6

DLM-7784

L-Valine-N-FMOC (D8, 98%)

+8

CLM-2158

L-Valine-N-t-BOC (1-13C, 99%)

+1

NLM-2060

L-Valine-N-t-BOC (15N, 98%)

+1

CNLM-2395

L-Valine-N-t-BOC (13C5, 97-99%; 15N, 97-99%)+6

DLM-3651

L-Valine-N-t-BOC (D8, 98%)

+8

”H” denotes an enrichment of ≥99%, as measured by GC-MS.

➤ Please inquire if you desire an alternate labeling patternor protecting group. For complete listing and additional
information, please visit the “Amino Acids” section of
isotope.com/products.

Through collaboration with New
England Peptide, Inc. (NEP), CIL is
pleased to offer synthesis-ready,preloaded resins to aid the solid-phase synthesis of stable isotopelabeled tryptic peptides. The resins are prepared from isotopicallylabeled, protected amino acids with the highest chemical, isotopic,
and chiral purity available. Please inquire for pricing and unit sizes.
Mass Shift from
Unlabeled (Da)

Catalog No.

Description

SRPR-ARG-CN

Synthesis-Ready Preloaded Resin L-Arginine(PBF) (13C6, 99%; 15N4, 99%)-2ClTrt Resin
NH

O

15

13

Pbf
N
H

H2
13
C

C
N
H

15

H2
13
C
13
C
H2

15

13
13

C
O

C

H
15

SRPR-LYS-CN

+10

NH2

Cl

Synthesis-Ready Preloaded Resin L-Lysine (BOC)(13C6, 99%; 15N2, 99%)-2ClTrt Resin

+8

O
H2
C

H
N

BOC

H2
C

13

15

13
C
H2

13

13
13
C
H2

13

C

C

O

H
15

NH2

Cl

➤ Please contact us if an alternate preloaded resin would
be beneficial to your research needs.

Isotope-Labeled Peptides
Catalog No.

Description

CNLM-6245

Glutathione (glycine-13C2, 98%+; 15N, 96-99%)
65-70% net peptide / peptide purity 85-90%

CNLM-6245-HP Glutathione (glycine-13C2, 98%+; 15N, 96-99%)90%+ net peptide / peptide purity 95%+
CNLM-8782

Glutathione disulfide (glycines-13C2, 98%+; 15N, 96-99%)
65-70% net peptide / peptide purity 90%+

Example References
Example References
Lau, J.K.-C.; Lam, K.H.B.; Lai, C.-K.; et al. 2019. Imidazolone formation from pronatedtetrapeptides: effects of replacing a glycine by an alanine or proline residue. Int J Mass Spec,
435, 69-77.

Li, F.; Cui, L.; Yu, D.; et al. 2019. Exogenous glutathione improves intracellular glutathione
synthesis via the γ-glutamyl cycle in bovine zygotes and cleavage embryos. J Cell Physiol,234(5), 7384-7394.

Ndao, M.; Goobes, G.; Emani, P.S.; et al. 2018. A REDOR ssNMR investigation of the roleof an N-terminus lysine in R5 silica recognition. Langmuir, 34(29), 8678-8884.

Lutchmansingh, F.K.; Hsu, J.W.; Bennett, F.I.; et al. 2018. Glutathione metabolism in type 2
diabetes and its relationship with microvascular complications and glycemia. PLoS One,13(6),e0198626.

LeBlanc, A.; Michaud, S.A.; Percy, A.J.; et al. 2017. Multiplexed MRM-based protein
quantitation using two different stable isotope-labeled peptide isotopologues for calibration.
J Proteome Res, 16(7), 2527-2536.

Nazari, M.; Bokhart, M.T.; Loziuk, P.L.; et al. 2018. Quantitative mass spectrometry imaging ofglutathione in healthy and cancerous hen ovarian tissue sections by infrared matrix-assisted
laser desorption electrospray ionization (IR-MALDESI). Analyst, 143(3), 654-661.

Percy, A.J.; Hardie, D.B.; Jardim, A.; et al. 2017. Multiplexed panel of precisely quantified
salivary proteins for biomarker assessment. Proteomics, 17(6).

D’Allesandro, A.; Nemkov, T.; Yoshida, T.; et al. 2017. Citrate metabolism in red blood cells
stored in additive solution-3. Transfusion, 57(2), 325-336.

Fernández-Fernández, M.; Rodríguez-González, P.; García Alonso, J.I. 2016. A simplified
calculation procedure for mass isotopomer distribution analysis (MIDA) based on multiple
linear regression. J Mass Spectrom, 51(10), 980-987.

Wisnewski, A.V.; Liu, J.; Nassar, A.F. 2016. Identification of novel reaction products ofmethylene-bis-phenylisocyanate (“MDI”) with oxidized glutathione in aqueous solution andalso during incubation of MDI with a murine hepatic S9 fraction. Toxicol In Vitro, 36, 97-104.

Delgado, D.A.; Doherty, K.; Cheng, Q.; et al. 2016. Distinct membrane disruption pathways
are induced by 40-residue β-amyloid peptides. J Biol Chem, 291(23), 12233-12244.
Wang, D.; Krilich, J.; Baudys, J.; et al. 2015. Optimization of peptide substrates for botulinum
neurotoxin E improves detection sensitivity in the Endopep-MS assay. Anal Biochem, 468,
15-21.
Lee, M.; Hong, M. 2014. Cryoprotection of lipid membranes for high-resolution solid-state
NMR studies of membrane peptides and proteins at low temperature. J Biomol NMR, 59,
263-277.

Chemical purity (CP) is 98% or greater, unless otherwise indicated.
International: tel: +1.978.749.8000 | fax: +1.978.749.2768 | intlsales@isotope.com 3

Cambridge Isotope Laboratories, Inc.

| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

PeptiQuant™ Assay Kits
CIL offers PeptiQuant™ Assay Kits from MRM Proteomics
Inc. for QC and biomarker assessment using bottom-up
LC-MS/MS methodologies. The QC kits are designed toevaluate the performance of an LC-MS platform, either alone
or in combination with a human or mouse plasma proteomic
workflow. The biomarker assessment kits (BAKs) are intended
to help researchers screen target panels of candidate protein
disease biomarkers in human or mouse plasma samples.

Regarding the methodology, PeptiQuant Plus kits employ mixturesof synthetic SIS and natural (NAT) peptides in the post-digestion
spike of sample or surrogate matrices. Quantitation is performed via
forward curves (approaches described in PubMed IDs: 27341553
and 28516774). These kits have been rigorously characterizedaccording to the complete set of CPTAC (Clinical Proteomic Tumor
Analysis Consortium) guidelines and are available for viewing on
the CPTAC Assay Portal.

PeptiQuant Plus Kits
Biomarker Assessment Kits (BAKs)
Catalog No.

Description

Unit Size

BAK-A6490-125

PeptiQuant Plus Human Plasma Proteomics Kit for Agilent 6490 and 1290 UPLC

20, 50, or 100 samples

BAK-A6495-125

PeptiQuant Plus Human Plasma Proteomics Kit for Agilent 6495 and 1290 UPLC

20, 50, or 100 samples

BAK-SC6500-125

PeptiQuant Plus Human Plasma Proteomics Kit for SCIEX QTRAP® 6500 and 1290 UPLC

20, 50, or 100 samples

BAK-QE-125

PeptiQuant Plus Human Plasma Proteomics Kit for Thermo Scientific™ Q Exactive™ Plus and 1290 UPLC

20, 50, or 100 samples

M-BAK-A6490-125
NEW! M-BAK-A6490-125-2*
NEW! M-BAK-A6490-125-3*

PeptiQuant Plus Mouse Plasma Proteomics Kit for Agilent 6490 and 1290 UPLC

20, 50, or 100 samples

M-BAK-A6495-125

PeptiQuant Plus Mouse Plasma Proteomics Kit for Agilent 6495 and 1290 UPLC

20, 50, or 100 samples

M-BAK-SC6500-125

PeptiQuant Plus Mouse Plasma Proteomics Kit for SCIEX QTRAP 6500 and 1290 UPLC

20, 50, or 100 samples

M-BAK-6545-125-2*

PeptiQuant Plus Mouse Plasma Proteomics Kit for Agilent 6545 and 1290 UPLC

20, 50, or 100 samples

PeptiQuant Plus Mouse Plasma Proteomics Kit for Thermo Scientific™ Q Exactive™ Plus and 1290 UPLC

20, 50, or 100 samples

NEW! M-BAK-A6495-125-2*
NEW! M-BAK-A6495-125-3*

M-BAK-QE-125
NEW! M-BAK-QE-125-2*
NEW! M-BAK-QE-125-3**The -2 and -3 demarcations refer to an alternate set of 125 target proteins.

Quality Control (QC) Kits
Catalog No.

Description

Unit SizeLCMSP-QC-6490-INJ

PeptiQuant Plus Human Plasma Daily QC Kit for Agilent 6490 and 1290 UPLC

10, 20, or 50 injections

LCMSP-QC-6495-INJ

PeptiQuant Plus Human Plasma Daily QC Kit for Agilent 6495 and 1290 UPLC

10, 20, or 50 injections

LCMSP-QC-6500-INJ

PeptiQuant Plus Human Plasma Daily QC Kit for Sciex QTRAP 6500 and 1290 UPLC

10, 20, or 50 injections

LCMSP-QC-QE-INJ

PeptiQuant Plus Human Plasma Daily QC Kit for Thermo Scientific Q Exactive Plus and 1290 UPLC

10, 20, or 50 injections

WFPK-A6490-P

PeptiQuant Plus Human Plasma Workflow QC Kit for Agilent 6490 and 1290 UPLC

1 or 2 runs

WFPK-A6495-P

PeptiQuant Plus Human Plasma Workflow QC Kit for Agilent 6495 and 1290 UPLC

1 or 2 runs

WFPK-SC6500-P

PeptiQuant Plus Human Plasma Workflow QC Kit for Sciex 6500 and 1290 UPLC

1 or 2 runs

WFPK-QE-P

PeptiQuant Plus Human Plasma Workflow QC Kit for Thermo Scientific Q Exactive Plus and 1290 UPLC

1 or 2 runs

➤ Please inquire if an alternate LC-MS/MS platform is desired from the current panel offerings. Visit the “MRM PeptiQuant
Assay Kits” section of isotope.com/products for complete product listings.
PeptiQuant is a trademark of MRM Proteomics Inc.
Example References
Michaud, S.A.; Sinclair, N.J.; Pětrošová, H.; et al. 2018. Molecular phenotyping of laboratory
mouse strains using 500 multiple reaction monitoring mass spectrometry plasma assays.
Commun Biol, 1(78).

Percy, A.J.; Mohammed, Y.; Yang, J.; et al. 2015. A standardized kit for automatedquantitative assessment of candidate protein biomarkers in human plasma. Bioanalysis,
7(23), 2991-3004.

LeBlanc, A.; Michaud, S.A.; Percy, A.J.; et al. 2017. Multiplexed MRM-based protein
quantitation using two different stable isotope-labeled peptide isotopologues for calibration.
J Proteome Res, 16(7), 2527-2536.

Percy, A.J.; Simon, R.; Chambers, A.G.; et al. 2014. Enhanced sensitivity and multiplexing
with 2D LC/MRM-MS and labeled standards for deeper and more comprehensive protein
quantitation. J Proteomics, 106, 113-124.

Percy, A.J.; Michaud, S.A.; Jardim, A.; et al. 2017. Multiplexed MRM-based assays for thequantitation of proteins in mouse plasma and heart tissue. Proteomics, 17(7).

Percy, A.J.; Chambers, A.G.; Yang, J.; et al. 2013. Method and platform standardizationin MRM-based quantitative plasma proteomics. J Proteomics, 95, 66-76.

Hirtz, C.; Vialaret, J.; Nowak, N.; et al. 2016. Absolute quantification of 35 plasma biomarkers
in human saliva using targeted MS. Bioanalysis, 8(1), 43-53.

Percy, A.J.; Chambers, A.G.; Smith, D.S.; et al. 2013. Standardized protocols for quality
control of MRM-based plasma proteomic workflows. J Proteome Res, 12(1), 222-233.

4

North America: 1.800.322.1174 | fax: 1.978.749.2768 | cilsales@isotope.com

| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

isotope.com

Protein Expression Reagents and Kits
Cell Growth MediaA diverse array of isotope-labeled prokaryotic and eukaryotic cell growth media for the production of isotope-enriched recombinant protein
is available from CIL.

Bacterial Cell Growth Media

Minimal Media Reagents

Celtone®, BioExpress®, E. coli-OD2, and Spectra 9

for E. coli Growths

Catalog No.

Description

Catalog No.

Description

CGM-1030P-C

Celtone Base Powder (13C, 98%)

NLM-467

Ammonium chloride (15N, 99%)

CGM-1030P-D

Celtone Base Powder (D, 97%)

NLM-713

Ammonium sulfate (15N2, 99%)

CGM-1030P-N

Celtone Base Powder ( N, 98%)

DLM-4-99

Deuterium oxide (D, 99%)

CGM-1030P-CN

Celtone Base Powder (13C, 98%; 15N, 98%)

DLM-4-99.8

Deuterium oxide (D, 99.8%)

CGM-1030P-DN

Celtone Base Powder (D, 97%; 15N, 98%)

DLM-4

Deuterium oxide (D, 99.9%)

CGM-1030P-CDN

Celtone Base Powder(13C, 98%; D, 97%; 15N, 98%)

CLM-1396

D-Glucose (13C6, 99%)

DLM-2062

CGM-1030P-U

Celtone Base Powder (unlabeled)

D-Glucose (1,2,3,4,5,6,6-D7, 97-98%)

CDLM-3813

CGM-1050P-C

Celtone Plus Base Powder (13C, 97-99%)

D-Glucose (13C6, 99%; 1,2,3,4,5,6,6-D7, 97-98%)

CLM-1510

CGM-1050P-D

Celtone Plus Base Powder (D, 97%+)

Glycerol (13C3, 99%)

DLM-558

CGM-1050P-N

Celtone Plus Base Powder (15N, 97-99%)

Glycerol (D8, 99%)

CGM-1050P-DN

Celtone Plus Base Powder (D, 97-99%; 15N, 97-99%)

Insect Cell Growth Media BioExpress® 2000

CGM-1050P-CDN

Celtone Plus Base Powder(13C, 97-99%; D, 97-99%; 15N, 97-99%)

Catalog No.

Description

CGM-2000-N

BioExpress 2000 (15N, 98%)

CGM-2000-CN

BioExpress 2000 (13C, 98%; 15N, 98%)

CGM-2000-U

BioExpress 2000 (unlabeled)

CGM-2000-CUSTOM

BioExpress 2000 (custom)*15

CGM-1050P-U

Celtone Plus Base Powder (unlabeled)

CGM-1040-C

Celtone Complete Medium (13C, 98%)

CGM-1040-D

Celtone Complete Medium (D, 97%)

CGM-1040-N

Celtone Complete Medium (15N, 98%)

CGM-1040-CN

Celtone Complete Medium (13C, 98%; 15N, 98%)

CGM-1040-DN

Celtone Complete Medium (D, 97%; N, 98%)

CGM-1040-CDN

Celtone Complete Medium(13C, 98%; D, 97%; 15N, 98%)

CGM-1040-U

Celtone Complete Medium (unlabeled)

CGM-1000-C

BioExpress Cell Growth Media (13C, 98%)
10x concentrate

CGM-1000-D

BioExpress Cell Growth Media (D, 98%)
10x concentrate

CGM-1000-N

BioExpress Cell Growth Media (15N, 98%)
10x concentrate

CGM-1000-CD

BioExpress Cell Growth Media (13C, 98%; D, 98%)
10x concentrate

15*The labeled amino acids must be specified at the time of request for a custom
media quote or order.

Yeast Cell Growth Media OD2 Media
Catalog No.

Description

CGM-4020-SL-C

Yeast-OD2 (13C, 98%)

CGM-4020-SL-N

Yeast-OD2 (15N, 98%)

CGM-4020-SL-CN

Yeast-OD2 (13C, 98%; 15N, 98%)

CGM-4020-SL-U

Yeast-OD2 (unlabeled)Mammalian Cell Growth Media BioExpress® 6000
Catalog No.

Description

CGM-6000-N

BioExpress 6000 (15N, 98%)

CGM-6000-CN

BioExpress 6000 (13C, 98%; 15N, 98%)

CGM-1000-CN

BioExpress Cell Growth Media (13C, 98%; 15N, 98%)
10x concentrate

CGM-1000-DN

BioExpress Cell Growth Media (D, 98%; 15N, 98%)
10x concentrate

CGM-6000-U

BioExpress 6000 (unlabeled)

CGM-6000-CUSTOM

BioExpress 6000 (custom)*CGM-1000-CDN

BioExpress Cell Growth Media(13C, 98%; 15N, 98%; D 98%) 10x concentrate*The labeled amino acids must be specified at the time of request for a custom
media quote or order.

CGM-1000-U

BioExpress Cell Growth Media (unlabeled)
10x concentrate

CGM-1020-SL-C

E. coli-OD2 (13C, 98%)

CGM-1020-SL-D

E. coli-OD2 (D, 98%)

CGM-1020-SL-N

E. coli-OD2 (15N, 98%)

CGM-1020-SL-CN

E. coli-OD2 ( C, 98%; N, 98%)

CGM-1020-SL-CDN

E. coli-OD2 (13C, 98%; D, 98%; 15N, 98%)

CGM-1020-SL-U-S

E. coli-OD2 (unlabeled)

CGM-3030-C

Spectra 9 (13C, 98%)

CGM-3030-D

Spectra 9 (D, 97%)

CGM-3030-N

Spectra 9 (15N, 98%)

CGM-3030-CN

Spectra 9 (13C, 98%; 15N, 98%)

CGM-3030-DN

Spectra 9 (D, 97%; 15N, 98%)

CGM-3030-CDN

Spectra 9 (13C, 98%; D, 97%; 15N, 98%)

CGM-3030-U

Spectra 9 (unlabeled)13

15

BioExpress and Celtone are registered trademarks of Cambridge Isotope
Laboratories, Inc.

➤ Please visit the “Cell Growth Media” section of
isotope.com/products for complete product listings
and additional information.
Please see references on next page ➤International: tel: +1.978.749.8000 | fax: +1.978.749.2768 | intlsales@isotope.com 5

| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

Cambridge Isotope Laboratories, Inc.

Kits for Cell-Free Protein Expression Wheat Germ Cell-Free Expression Kits (CellFree Sciences, CFS)
Wheat germ cell-free protein expression systems have beenused over the years to address many different needs in basic
research and applied sciences. CFS is the leading commercial
manufacturer of kits and reagents used in wheat germ-based,
cell-free protein expression. CFS’ proprietary wheat germ embryo
extract, WEPRO®, is the critical ingredient that allows reproducible
production of protein in high yield.

CFS offers several starter kits to characterize yield and protein
quality. These kits enable multiple large-scale reactions thattypically yield microgram amounts of protein. Each kit contains
a positive control that yields about 30 µg of DHFR.
The Premium Plus Expression Kit for MS isperfectly suited to produce isotope-enriched
protein for bottom-up LC-MS studies.

Catalog No.

Description

Contents

Specification

CFS-PRK-G24

Protein Research Kit (G)Premixed transcription and translation reagents for GST-fusion protein expression.
Reaction scale is 226 μL.

24 reactions

CFS-PRK-H24

Protein Research Kit (H)Premixed transcription and translation reagents for His-fusion protein expression.
Reaction scale is 226 μL.

24 reactions

CFS-PRK-S24

Protein Research Kit (S)Premixed transcription and translation reagents for protein expression.
Reaction scale is 226 μL.

24 reactions

CFS-TRI-PLE-BD

Proteoliposome BD Expression Kit

WEPRO 7240, transcription buffer LM, NTP mix, SP6 RNA polymerase, RNase inhibitor,
creatine kinase, pEU-E01-T1R1 plasmid, SUB-AMIX SGC S1-S4, and asolectin liposome.
Reaction scale is 2.5 mL.

6 reactions

CFS-TRI-PLE

Proteoliposome Expression Kit

WEPRO 7240, transcription buffer LM, NTP mix, SP6 RNA polymerase, RNase inhibitor,
creatine kinase, pEU-E01-T1R1 plasmid, SUB-AMIX SGC S1-S4, and asolectin liposome.
Reaction scale is 4 mL.

6 reactions

CFS-EDX-PLUS

Premium PLUS Expression Kit

Expression vector (pEU-E01-MCS), PCR primer for transcription and translation, positive
control, and reaction cups. Reaction scale is 227 µL.

8 reactions

CFS-EDX-PLUS-MS

Premium PLUS Expression Kit
for MS

Expression vector (pEU-E01-MCS), PCR primer set (SPU, deSP6E01), transcription premix
LM, WEPRO 9240 and SUB-AMIX SGC for MS, positive control, and reaction cups.
Reaction scale is 227 µL.

16 reactions

CFS-EDX-PLE-PLUS

Proteoliposome Premium PLUS
Expression Kit

Expression vector, primers for DNA preparation by PCR, prepared apolection-liposomes,
positive control, and reaction cups. Reaction scale is 226 µL.

8 reactions➤ Please visit the “CellFree Protein Expression” section of isotope.com/products and cfscience.com for additional informationon these and other products.
Example References
Lacabanne, D.; Fogeron, M.L.; Wiegand, T.; et al. 2019. Protein sample preparation forsolid-state NMR investigations. Prog Nucl Magn Reson Spectrosc, 110, 20-33.
Novikova, I.V.; Sharma, N.; Moser, T.; et al. 2018. Protein structural biology using cell-free
platform from wheat germ. Adv Struct Chem Imaging, 4(1), 13.
Narumi, R.; Masuda, K.; Tomonaga, T.; et al. 2018. Cell-free synthesis of stable isotopelabeled internal standards for targeted quantitative proteomics. Synth Syst Biotechnol, 3(2),97-104.

Takemori, N.; Takemori, A.; Tanaka, Y.; et al. 2016. High-throughput production of a stable
isotope-labeled peptide library for targeted proteomics using a wheat germ cell-free synthesis
system. Mol Biosyst, 12(8), 2389-2393.
Takemori, N.; Takemori, A.; Matsuoka, K.; et al. 2015. High-throughput synthesis of stable
isotope-labeled transmembrane proteins for targeted transmembrane proteomics using awheat germ cell-free protein synthesis system. Mol Biosyst, 11(2), 361-365.
Goshima, N.; Kawamura, Y.; Fukumoto, A.; et al. 2008. Human protein factory for converting
the transcriptome into an in vitro-expressed proteome. Nat Methods, 5(12), 1011-1017.

Cell Growth Media (continued from previous page)
Example References
Minikel, E.V.; Kuhn, E.; Cocco, A.R.; et al. 2019. Domain-specific quantification of prion
protein in cerebrospinal fluid by targeted mass spectrometry. bioRxiv.

Zhang, C.; Liu, Y.; Andrews, P.C. 2013. Quantification of histone modifications using 15N
metabolic labeling. Methods, 61(3), 236-243.

Lacabanne, D.; Fogeron, M.L.; Wiegand, T.; et al. 2019. Protein sample preparation forsolid-state NMR investigations. Prog Nucl Magn Reson Spectrosc, 110, 20-33.

Saxena, K.; Dutta, A.; Klein-Seetharaman, J.; et al. 2012. Isotope labeling in insect cells.
Methods Mol Biol, 831, 37-54.

Goswami, D.; Tuske, S.; Pascal, B.D.; et al. 2015. Differential isotopic enrichment to facilitatecharacterization of asymmetric multimeric proteins using hydrogen/deuterium exchange mass
spectrometry. Anal Chem, 87(7), 4015-4022.

CIL Application Notes

Acedo, J.Z.; van Belkum, M.J.; Lohans, C.T.; et al. 2015. Solution structure of acidocin B,a circular bacteriocin produced by Lactobacillus acidophilus M46. Appl Environ Microbiol,
81(8), 2910-2918.
Zhang, C.; Gao, S.; Molascon, AJ.; et al. 2014. Quantitative proteomics reveals histone
modifications in crosstalk with H3 lysine 27 methylation. Mol Cell Proteomics, 13(3), 749-759.
Hessling, B.; Büttner, K.; Hecker, M.; et al. 2013. Global relative quantification with liquid
chromatography-matrix-assisted laser desorption ionization time-of-flight (LC-MALDI-TOF) –cross-validation with LTQ-Orbitrap proves reliability and reveals complementary ionizationpreferences. Mol Cell Proteomics, 12(10), 2911-2920.

6

North America: 1.800.322.1174 | fax: 1.978.749.2768 | cilsales@isotope.com

Berthold, D.A.; Jeisy, V.J.; Sasser, T.L.; et al. 2007. Top ten tips for producing 13C, 15N
protein in abundance. (Application Note 15)
Strauss, A.; Fendrich, G.; Jahnke, W. 2007. Efficient uniform labeling of proteins
expressed in baculovirus-infected insect cells using BioExpress® 2000 (insect cell) medium.
(Application Note 14)
Rhima, M.; Neil, L.C.; Gardner, K.H. 2003. Optimization of BioExpress® supplementationof M9 cultures. (Application Note 12)

| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

isotope.com

Isotope-Labeled Proteins
We offer a number of isotope-labeled recombinant proteinsfor MS and NMR research. In MS studies, these can be added
to samples at the beginning of experimental workflows to help
control or correct for analytical variability. This is toward improving

the accuracy of protein quantification. For NMR spectroscopy, these
proteins are used to assess NMR spectrometer performance, aid thedevelopment of new pulse sequences, and for training purposes.
Please inquire for quantity and pricing.

Catalog No.

Description

Concentration and Composition

NLM-9539

Human apolipoprotein A-1 (15N, 98%)

~1.2 mg/mL in PBS (pH 7.4), CP >90%

CNLM-9513

Human IGF-1 (Lys-13C6, 15N2, 99%; Arg-13C6, 15N2, 99%)

10 µg/mL in 20 mM sodium phosphate (pH 7) with 10 mg/mL trehalose

NEX-UB1-CN

Human ubiquitin (13C, 95%; 15N, 95%)*

0.25, 0.5, or 1 mM in 90% H2O/10% D2O with 0.02% NaN3 and 20 mM sodium
phosphate (pH 7.2)

NEX-UB1-N

Human ubiquitin (15N, 95%)*

0.25, 0.5, or 1 mM in 90% H2O/10% D2O with 0.02% NaN3 and 20 mM sodium
phosphate (pH 7.2)

NEX-MBP1-CN

E. coli maltose binding protein (13C, 95%; 15N, 95%)*

0.25, 0.5, or 1 mM in 90% H2O/10% D2O with 0.02% NaN3 and 20 mM sodium
phosphate (pH 7.2)

NEX-XF1-CN

X-filtered NOESY NMR standard (13C, 95%; 15N, 95%)*

Mixture of labeled and unlabeled 16 kDa protein (A. fulgidus antitoxin vapB21
homodimer). 1 mM protein in 90% H2O/10% D2O with 20 mM NH4OAc (pH 5.5),
100 mM NaCl, 5 mM CaCl2, and 0.02% NaN3

NEX-GB1-CN

GB1 (13C, 95%; 15N, 95%)*

0.25, 0.5, or 1 mM in 50 mM sodium phosphate (pH 5.5), 10% D2O, 0.02% NaN3

NEX-CAL-CN

Calbindin-D9k (13C, 95%; 15N, 95%)*

0.25, 0.5, or 1 mM in 50 mM ammonium acetate (pH 6.0), 10% D2O, 0.02% NaN3

NEX-SH3-CN

SH3 Domain (13C, 95%; 15N, 95%)*

0.25, 0.5, or 1 mM in 50 mM sodium citrate (pH 3.5), 10% D2O, 0.02% NaN3

*	Alternate labels are available; please inquire.

➤ Please visit the “Protein Standards” section of isotope.com/products for additional information.
Example References
Ting, Y.S.; Egertson, J.D.; Bollinger, J.G; et al. 2017. PECAN: library-free peptide detection fordata-independent acquisition tandem mass spectrometry data. Nat Methods, 14(9), 903-908.
Goulding, S.P.; Szumlinski, K.K.; Contet, C.; et al. 2017. A mass spectrometry-based
proteomic analysis of Homer2-interacting proteins in the mouse brain. J Proteomics, 166,
127-137.
Spencer, S.E.; Corso, T.N.; Bollinger, J.G.; et al. 2017. Automated Trapping Column Exchanger
for High-Throughput Nanoflow Liquid Chromatography. Anal Chem, 89(4), 2383-2389.

Henderson, C.M.; Vaisar, T.; Hoofnagle, A.N. 2016. Isolating and quantifying plasma HDL
proteins by sequential density gradient ultracentrifugation and targeted proteomics.
Methods Mol Biol, 1410, 105-120.
Li, B.; Makino, S.I.; Beebe, E.T.; et al. 2016. Cell-free translation and purification of
Arabidopsis thaliana regulator of G signaling 1 protein. Protein Expr Purif, 126, 33-41.
Harbers, M. 2014. Wheat germ systems for cell-free protein expression. FEBS Lett, 588(17),2762-73.

Protein/Peptide Standard Mix
CIL is proud to offer ProteusQC™, a new and versatile standard
for MS-based bottom-up quantitative proteomics. It comprises abalanced mix of human 15N-enriched apolipoprotein A-1 (ApoA-1)
together with six 13C/ 15N-enriched ApoA-1 tryptic peptides.
ProteusQC can be used to index retention times, evaluate digestion
efficiency (of ApoA-1), assess system suitability, and perform
absolute/relative protein quantification. The peptides derived fromthe 15N-labeled ApoA-1 SIS protein can also serve as global internal
standards for the endogenous proteins in the user’s target panel, as
was demonstrated previously for an array of moderate abundanceproteins in MRM and PRM applications. Please inquire for pricing.
Catalog No.

Description

CNLM-9919

ProteusQC (labeled ApoA-1 + 6 labeled ApoA-1
tryptic peptides)➤ Please visit the “Protein Standards” section of
isotope.com/products for additional information.

Unit Size
10 µL

Example References
Percy, A.J.; Byrns, S.; Pennington, S.R.; et al. 2016. Clinical translation of MS-based,
quantitative plasma proteomics: status, challenges, requirements, and potential.
Expert Rev Proteomics, 13(7), 673-84.
Ronsein, G.E.; Pamir, N.; von Haller, P.D.; et al. 2015. Parallel reaction monitoring (PRM) andselected reaction monitoring (SRM) exhibit comparable linearity, dynamic range and precision
for targeted quantitative HDL proteomics. J Proteomics,113, 388-399.
Hoofnagle, A.N.; Becker, J.O.; Oda, M.N.; et al. 2012. Multiple-reaction monitoring-mass
spectrometric assays can accurately measure the relative protein abundance in complex
mixtures. Clin Chem, 58(4), 777-781.
CIL Application Note
Vaisar, T.; Percy, A.J.; Backiel, K.; et al. 2017. Stable Isotope-Labeled ApoA-1 as a Global
Standard for Quantitative Proteomic Studies. (Application Note 46)

Supplement to May 2017 issue (#52) – “Mass Spectrometry Takes Flight”

ACCELERATE AND
ENHANCE BOTTOMUP PROTEOMICWORKFLOWS WITH
PROTEUSQC™
Improve process control and peptide/protein
quantification in biosamples with the ProteusQC™
standard mixture.
By Andrew J. Percy and Krista Backiel
Abstract
Much research within the field of proteomics has focusedon the identification and quantification of candidate protein
biomarkers using bottom-up LC-MS methodologies. Althoughsignificant progress has been made, bioanalytical development isoften slowed by the absence of stable isotope-labeled standards
for workflow suitability assessment and quantification datanormalization. We describe herein the implementation andmerits of a novel standard mixture (referred to as ProteusQCTM)
for bottom-up proteomic applications.
Scope and Application
To improve assay development time and data quality of qualitativeand quantitative analysis in bottom-up (and perhaps middledown) proteomics, a highly characterized mixture of differently
labeled protein/peptides has been prepared and evaluatedextensively (Figure 1A).
This stable isotope-labeled mix consists of a set of proteolyticallystable, apolipoprotein A-1 (ApoA-1) standards whose combination
affords unique analytical benefits. For straightforward use, analiquot of the ProteusQC mixture (diluted as necessary) is spiked
into a neat biosample(s) before bottom-up sample preparationand downstream LC-MS/MS sample processing. Data analysis
is readily accomplished with vendor-neutral Skyline software (1),which is further supported by a number of adaptable external
tools, such as SProCoP (2) (for QC performance evaluation) and
QuaSAR (for curve-based quantification).
In principle, upon tryptic digestion and LC-MS/MS,
ProteusQC produces 14 ApoA-1 peptides that are broadly
dispersed over a wide chromatographic space and are well suited
to serve as reference (or internal) standards for retention timeindexing, digestion condition evaluation (Figure 1B), method
and system suitability, as well as absolute/relative protein

Figure 1. ProteusQC™ and an example of its product utility. A) The

mixture consists of 15N-labeled ApoA-1 and 6 13C/15N-labeled ApoA-1

peptides (highlighted in red). B) Digestion efficiency check of a matrix-freeand matrix-containing sample measured by bottom-up LC-PRM/MS.

quantification. Manuscripts are in preparation by MacCoss andcolleagues (on development and utility) and Pennington andcolleagues (on application to PsA and RA sera patient samples).
Independent from this, quantification has been demonstrated
with a variety of biosamples processed via targeted LC-MS/
MS. In one example, 15N-labeled ApoA-1 peptides from a
ProteusQC digest enabled precise and accurate quantificationof endogenous ApoA-1, as well as other target proteins, in highdensity lipoprotein and mouse sera samples through a global
peptide normalization strategy (see CIL application note #46).
The use of a single protein as a global standard offers a numberof practical (e.g., increases multiplexing) and economic (e.g.,decreases cost) advantages, as demonstrated initially by Hoofnagle
et al. (3), that are valuable for assay development and performance.
In summary, the diverse merits of ProteusQC should help advancethe application of bottom-up proteomics in basic research andclinical translation studies.
References
1.

B MacLean et al., “Skyline: an open source document editor for creating and2.

MS Bereman et al., “Implementation of statistical process control for proteomic

3.

AN Hoofnagle et al., “Multiple-reaction monitoring-mass spectrometric assays

analyzing targeted proteomics experiments”, Bioinformatics, 26, 966–968 (2010).
experiments via LC MS/MS”, J Am Soc Mass Spectrom, 25, 581–587 (2014).
can accurately measure the relative protein abundance in complex mixtures”,
Clin Chem, 58, 777–781 (2012).

Contact: Andrew Percy, PhD
Email: apercy@isotope.com

For additional information on
the utility and application ofProteusQC™, download thefull magazine article fromthe Analytical Scientist at
isotope.com.

Download the full application note: tas.txp.to/0517/ISOTOPE
www.isotope.com

International: tel: +1.978.749.8000 | fax: +1.978.749.2768 | intlsales@isotope.com 7

Cambridge Isotope Laboratories, Inc.

| Stable Isotope-Labeled Peptide and Protein Reagents/Kits

Please visit isotope.com for a complete list of isotope-labeled compounds.

Research products are distributed and sold worldwide via our extensive network.
CIL’s distributor listing is available at isotope.com.

To request a quotation or place an order:
North America: 1.978.749.8000 | 1.800.322.1174 | cilsales@isotope.com
International: +1.978.749.8000 | intlsales@isotope.com
Fax: 1.978.749.2768 | isotope.com

Cambridge Isotope Laboratories, Inc. 3 Highwood Drive, Tewksbury, MA 01876 USA
North America: 1.800.322.1174 | International: +1.978.749.8000 | fax: +1.978.749.2768 | isotope.com

PL_RSCH_PEP (6/28/19)

Supersedes all previously published literature