Anti-Sds22 (S. pombe) antibody, rabbit serum
Product code63-141

Size

100 µlStorage

Store 4℃ for short term For long term storage store at -20℃.
Aliquot to avoid repeated freezing and thawing.

Concentration

N/A

Buffer

0.05% sodium azide

PurityRabbit antiserum

Immunogen

Recombinant C-terminal region (1.8kb) of S. pombe Sds22 (1)IsotypeRabbit IgG

Reactivity

S. pombe Sds22

Special notes

N/A

Application

1. Immunoblotting (dilution: 1/200~1/500) (Ref 1,2,3)
2. Immunoprecipitation (Ref 2)
3. Immunofluorescence microscopy

Background

Schizosaccharomyces pombe Sds22 protein contains leucine-rich repeats andphysically interacts with the catalytic subunits of two type 1 protein
phosphatases (Dis2 and Sds21). Sds22 is a regulatory subunit of these
phosphatases and the Sds22-bound phosphatases carry a key phosphataseactivity essential for the progression from metaphase to anaphase. Sds22 isessential for cell viability and in its absence, cells were blocked in metaphase.
Sds22 protein is predicted to form a repeating helical rod that is capable ofenhancing a PP1-dependent dephosphorylation activity.

Data Link

UniProtKB P22194 (SDS22_SCHPO)

Please note: All products are FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC
PROCEDURES. NOT FOR MILITARY USE.

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Data Images: 63-141 Anti-Sds22 (S. pombe) antibody, rabbit serum

Fig.1 Immunoblot with anti-Sds22 antiserum of yeast extracts from (1) wild type strain HM123, (2)sds::ura4+ deletion mutant carrying pHR140-2 (ref.2).
The 40kD protein band was identified by immunoblot analysis of wild-type strain using anti-Sds22
antisera (lane1). The 40 kD band is enhanced in the sds22::ura4+ disruptrion mutant strain that isrescued by the multicopy sds22+ plasmid pHR140-2 (lane2).

Fig.2 Sds22 coprecipitates with Dis2 and Sds21 (ref.2).
Yeast extracts of wild type (wt) strain HM123 (lane 1 and 2), dis2::ura4+ deletion mutant (Δd2, lane3), sds21::ura4+ deletion mutant (Δs21, lane4) were immunoprecipitatedfollowed byimmunoblotting with the indicated antiserum, to detect the Sds22 or Dis2/Sds21 proteins.
Lane 1 was immunoprecipitated with the appropriate preimmune serum, lane 2-4 with the anti-Sds22serum.
(a) denotes anti-Sds22 immunoblot; (b) denotes anti-D2C immunoblot. Anti-D2C crossreacts withboth Sds21 and Dis2.
Anti-Sds22 antiserum coprecipitates both Dis2 and Sds21 proteins in the wild type strain (lane 2b).
Consistently, Sds21 alone is precipitated in the dis2 deletion mutant (lane 3b), and Dis2 alone isprecipitated in the sds21 deletion mutant (lane 4b).

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Fig.3 Sds22 subcellular localization
Indirect immunofluorescence microscopy was performed by staining methanol fixed cells with (firstcolumn) anti-Sds22 antiserum, or (second column) DAPI to visualize chromosomal DNA.
(a) wild type HM123; (b) HM123 carrying multicopy sds22+ plasmid pHR140-2. Anti-Sds22 antibodystains the cytoplasm as well as the non-chromosomal domain of the nucleus of a wild type strain, asshown in (a). Nuclear staining increases in strains carrying a multicopy sds22+ plasmid (b).
References: This antibody has been used in Ref. 1, 2 and 3.
1. Ohkura H and Yanagida M “S.pombe gene sds22+ essential for a midmitotic transition encodes aleucine-rich repeat protein that positively modulates protein phosphatase-1.” Cell 64: 149-157(1991) PMID: 1846086
2. Stone EM et al “Mitotic regulation of protein phosphatases by the fission yeast sds22 protein.” CurrBiol 3: 13-26 (1993) PMID: 15335873
3. Ishii K et al “Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphaseis lessened by the dosage increase of a novel gene sds23+.” EMBO J. 15:6629-6640 (1996) PMID:8978689

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