Human CD79B Protein 4527

$270.00 – $900.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Ala29-Asp159

SKU: 4527parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P40259
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE
background	CD79B (also known as B29, Ig beta and B cell antigen receptor complex-associated protein beta-chain) is a 36-40 kDa member of the Ig-Superfamily. It is required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.
molecular weight	The protein has a predicted MW of 18.1 kDa. Due to glycosylation, the protein migrates to 33-42 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human CD79B Protein 4527

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
CD79B (also known as B29, Ig beta and B cell antigen receptor complex-associated protein beta-chain) is a 36-40 kDa member of the Ig-Superfamily. It is required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.
Protein names B-cell antigen receptor complex-associated protein beta chain (B-cell-specific glycoprotein B29) (Ig-beta) (Immunoglobulin-associated B29 protein) (CD antigen CD79b)
Gene names CD79B,CD79B B29 IGB
Mass 9606Da
Function Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.
Subellular location Cell membrane; Single-pass type I membrane protein. Note=Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts.
Tissues B-cells.
Structure Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains (PubMed:35981043). Interacts with LYN (By similarity).
Post-translational modification Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK.
Domain Th
Target Relevance information above includes information from UniProt accession: P40259
The UniProt Consortium

Data

Immobilized Human CD79B, His Tag at 0.5µg/ml (100µl/Well). Dose response curve for Anti-CD79B Antibody, hFc Tag with the EC50 of 3.7ng/ml determined by ELISA.

Human CD79B 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.