Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
express system | HEK293 |
product tag | C-His-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
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 35-45 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Human CD79B Protein 4588
$525.00 – $1,750.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Ala29-Asp159
Biotinylated Human CD79B Protein 4588
protein |
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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 |
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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 26048Da |
Function 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. {ECO:0000269|PubMed:12097390, ECO:0000269|PubMed:8617796, ECO:0000269|PubMed:9057631}. |
Subellular location SUBCELLULAR 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. {ECO:0000250}. |
Tissues TISSUE SPECIFICITY: B-cells. |
Structure SUBUNIT: 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). {ECO:0000250, ECO:0000269|PubMed:35981043}. |
Post-translational modification PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK. |
Domain DOMAIN: The transmembrane helices of CD79A and CD79B chains and two IgM heavy chains assembly in a four-helix bundle structure that appears to be conserved among different BCR isotypes. {ECO:0000269|PubMed:35981043}. |
Target Relevance information above includes information from UniProt accession: P40259 |
The UniProt Consortium |
Data
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