GMP Human FGF basic Protein
Catalog # GMP-FGCH17Features

Sterility

Designed under ISO 9001:2015 and ISO 13485:2016
Manufactured and QC tested under a GMP compliance factory
Animal-Free materials
Beta-lactam materials free

The sterility testing was performed by membrane filtration method described in
CP<1101>, USP<71> and Eur. Ph. 2.6.1.

Mycoplasma
Negative.

PurityBatch-to-batch consistency
Stringent quality control tests
No animal derived peptone and lactose used in production process>95% as determined by SDS-PAGE.

Formulation

SourceLyophilized from 0.22 μm filtered solution in PBS, pH7.4 with protectants.

GMP Human FGF basic Protein(GMP-FGCH17) is expressed from E. coli cells.

Contact us for customized product form or formulation.

It contains AA Pro 143 - Ser 288 (Accession # P09038-4).
Predicted N-terminus: Pro 143

Molecular Characterization

Shipping
This product is supplied and shipped with blue ice, please inquire the shipping
cost.

StorageUpon receipt, store it immediately at -20°C or lower for long term storage.
This protein carries no "tag".
The protein has a calculated MW of 16.5 kDa. The protein migrates as 17 kDa±3
kDa under reducing (R) condition (SDS-PAGE).

Endotoxin

Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:-20°C to -70°C for 5 years in lyophilized state;-70°C for 12 months under sterile conditions after reconstitution.

Less than 10 EU/mg by the LAL method.

Host Cell Protein<0.5 ng/µg of protein tested by ELISA.

Host Cell DNA<0.02 ng/μg of protein tested by qPCR.

SDS-PAGE

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9/18/2024

GMP Human FGF basic Protein
Catalog # GMP-FGCH17

GMP Human FGF basic Protein on SDS-PAGE under reducing (R) condition.
The gel was stained with Coomassie Blue. The purity of the protein is greaterthan 95%.

Bioactivity-Bioactivity CELL BASE

GMP Human FGF basic Protein (Cat. No. GMP-FGCH17)

The activity of GMP Human FGF basic Protein (Cat. No. GMP-FGCH17) was

stimulates proliferation of NIH/3T3 cells. The specific activity of GMP Humanhigher than other competing products.

FGF basic Protein is >2.50 x 10^6 IU/mg, which is calibrated against BasicFibroblast Growth Factor WHO International Standard (NIBSC code: 90/712)(QC tested).

Application Data

FGF basic (Cat. No. GMP-FGCH17) could highly support stemness maintenance in ESC/iPSC compared to other companies.
Left: The mRNA expression of pluripotent stem cell markers (Oct4, Nanog) was higher in Acro than in company R and company P.
Right: When FGF basic (35 μg/mL) is added into the culture media (StemSure hPSC medium) for iPSC, the cells remain high expression of pluripotent (Oct4+ orNanog+; pink) markers.

Bioactivity-Stability

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9/18/2024

GMP Human FGF basic ProteinCatalog # GMP-FGCH17

The Cell based assay shows that GMP Human FGF basic Protein (Cat. No.

The Cell based assay shows that GMP Human FGF basic Protein (Cat. No.

GMP-FGCH17) is stable at 37°C for 24 hours.

GMP-FGCH17) is stable after freezing and thawing 3 times.

The Cell based assay shows that GMP Human FGF basic Protein (Cat. No.

The Cell based assay shows batch-to-batch consistency between Acro's GMP

GMP-FGCH17 ) is stable at 4℃ for 30 days.

and PG FGF basic.

MANUFACTURING SPECIFICATIONSACROBiosystems GMP grade products are produced under a quality management system and in compliance with relevant guidelines: Ph. Eur General Chapter
5.2.12 Raw materials of biological origin for the production of cell-based and gene therapy medicinal products; USP<92>Growth Factors and Cytokines Used in Cell
Therapy Manufacturing; USP<1043>Ancillary Materials for Cell, Gene, and Tissue-Engineered Products; ISO/TS 20399-1:2018, Biotechnology - Ancillary
Materials Present During the Production of Cellular Therapeutic Products.

ACROBiosystems Quality Management System Contents：
Designed under ISO 9001:2015 and ISO 13485:2016, Manufactured and QC tested under a GMP compliance factory.
Animal-Free materials
Materials purchased from the approved suppliers by QA
ISO 5 clean rooms and automatic filling equipment
Qualified personnel
Quality-related documents review and approve by QA
Fully batch production and control records

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9/18/2024

GMP Human FGF basic Protein
Catalog # GMP-FGCH17

Equipment maintenance and calibration
Validation of analytical procedures
Stability studies conducted
Comprehensive regulatory support files
Request For Regulatory Support Files（RSF）

ACROBiosystems provide rigorous quality control tests (fully validated equipment, processes and test methods) on our GMP grade products to ensure that they meetstringent standards in terms of purity, safety, activity and inter-batch stability, and each bulk QC lot mainly contains the following specific information:
SDS-PAGE
Protein content
Endotoxin level
Residual Host Cell DNA content
Residual Host Cell Protein content
Biological activity analysis
Microbial testing
Mycoplasma testingIn vitro virus assay
Residual moisture
Batch-to-batch consistency

Background
FGF basic (also known as FGF2 and HBGF-2) is an 18-34 kDa, heparin-binding member of the FGF superfamily of molecules (1-3). Superfamily members arecharacterized by the presence of a centrally placed beta -trefoil structure. FGF acidic (FGF-1) and FGF basic (FGF2) were the first two identified FGFs, and thedesignations acidic and basic refer to their relative isoelectric points. Human FGF basic is 288 amino acids (aa) in length. There are multiple start sites, four of which
utilize atypical CUG codons, and one that initiates at an AUG start site (4 - 6). The four CUG start sites generate high molecular weight (HMW) FGF basic. There isa 34 kDa, 288 aa form, a 24 kDa, 210 aa form, a 22.5 kDa, 201 aa form, and a 22 kDa, 196 aa form. All are retained intracellularly, undergo extensive methylation,and possess one or more nuclear localization signals (NLS) (7-9). The AUG initiating form is 18 kDa and 155 aa in length. There is no signal sequence (ss). It is,however, secreted directly through the plasma membrane via a mechanism that appears to be dependent upon tertiary structure (10). In place of a ss, there is
purportedly a 9 aa N-terminal prosegment that precedes a 146 aa mature segment (11). Early isolations of 18 kDa bovine FGF basic yielded 146 aa molecules, aneffect attributed to the presence of acid proteases (12). The molecule contains a heparin-binding site (aa residues 128-144), and undergoes phosphorylation at Ser117(13). There is also an ill-defined C-terminal NLS that may be more “functional” (or 3-dimensional) than structural (7). Human 146 aa FGF basic is 97% aa identicalto mouse FGF basic (14).

Clinical and Translational Updates

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9/18/2024