Cynomolgus Complement Component C2 Protein 3072

$315.00 – $1,050.00

Summary

Expression: HEK293
Active: Yes (catalytic)
Amino Acid Range: Ala21-Leu752

SKU: 3072parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	XP_005553508
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Single nucleotide polymorphism (SNP) of complement component 2 (C2) has been found to be significantly associated with hepatocellular carcinoma (HCC). Significantly lower C2 expression was found at HCC compared to healthy controls, and C2 was associated with TNM stages. Higher C2 expression was significantly associated with better prognosis, and multivariate analysis showed that C2 was also an independent factor for the prognosis of HCC.
molecular weight	The protein has a predicted MW of 82.18 kDa. Due to glycosylation, the protein migrates to 90-110 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Cynomolgus Complement Component C2 Protein 3072

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Single nucleotide polymorphism (SNP) of complement component 2 (C2) has been found to be significantly associated with hepatocellular carcinoma (HCC). Significantly lower C2 expression was found at HCC compared to healthy controls, and C2 was associated with TNM stages. Higher C2 expression was significantly associated with better prognosis, and multivariate analysis showed that C2 was also an independent factor for the prognosis of HCC.
Protein names Complement C2 (EC 3.4.21.43) (C3/C5 convertase) [Cleaved into: Complement C2b fragment; Complement C2a fragment]
Protein family Peptidase S1 family
Mass 83268Da
Function Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.
Catalytic activity CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-\|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-\|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.; EC=3.4.21.43;
Subellular location Secreted.
Structure C2a interacts with Schistosoma haematobium TOR (via N-terminal extracellular domain). This results in inhibition of the classical and lectin pathway of complement activation, probably due to interference with binding of C2a to C4b such that C3 convertase cannot be formed. This infers resistance to complement-mediated cell lysis, allowing parasite survival and infection. {ECO:0000269\|PubMed:10734221}.
Domain The MIDAS-like motif in the VWFA domain binds divalent metal cations.
Target Relevance information above includes information from UniProt accession: P06681
The UniProt Consortium

Data

Activity assay with Cynomolgus Complement Component C2 Protein

Measured by its ability to cleave a colorimetric peptide substrate, N-carbobenzyloxy-Gly-Arg-ThioBenzyl ester (Z-GR-SBzl), in the presence of 5,5'Dithio-bis (2-nitrobenzoic acid) (DTNB). The specific activity is >100 pmol/min/µg.

HPLC of Cynomolgus Complement Component C2 Protein

The purity of Cynomolgus Complement Component C2 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Cynomolgus Complement Component C2 Protein

Cynomolgus Complement Component C2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.