Mouse Siglec-2/CD22 Protein 3363

$270.00 – $900.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Ser22–Arg702

SKU: 3363parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P35329
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	CD22, or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins. It is found on the surface of mature B cells and to a lesser extent on some immature B cells. CD22 a member of the immunoglobulin superfamily. CD22 functions as an inhibitory receptor for B cell receptor (BCR) signaling. It is also involved in the B cell trafficking to Peyer's patches in mice.
molecular weight	The protein has a predicted MW of 80.25 kDa. Due to glycosylation, the protein migrates to 110-115 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per ug by the LAL method.

Mouse Siglec-2/CD22 Protein 3363

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
CD22, or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins. It is found on the surface of mature B cells and to a lesser extent on some immature B cells. CD22 a member of the immunoglobulin superfamily. CD22 functions as an inhibitory receptor for B cell receptor (BCR) signaling. It is also involved in the B cell trafficking to Peyer's patches in mice.
Protein names B-cell receptor CD22 (B-lymphocyte cell adhesion molecule) (BL-CAM) (Sialic acid-binding Ig-like lectin 2) (Siglec-2) (T-cell surface antigen Leu-14) (CD antigen CD22)
Gene names Cd22,Cd22 Lyb-8 Siglec2
Protein family Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
Mass 10090Da
Function Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.
Subellular location Cell membrane; Single-pass type I membrane protein.
Tissues B-lymphocytes.
Structure Interacts with LYN, SYK, PIK3R1/PIK3R2, PLCG1, SHC1, INPP5D and GRB2 upon phosphorylation. May form a complex with INPP5D/SHIP, GRB2 and SHC1. Interacts with PTPN6/SHP-1 upon phosphorylation (By similarity).
Post-translational modification Phosphorylated on tyrosine residues by LYN.; Phosphorylation of Tyr-783 and Tyr-843 are involved in binding to SYK. Phosphorylation of Tyr-828 is involved in binding to GRB2. Phosphorylation of Tyr-863 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2.
Domain Co
Target Relevance information above includes information from UniProt accession: P35329
The UniProt Consortium

The purity of Mouse Siglec-2 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Mouse Siglec-2/CD22 Protein

Mouse Siglec-2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

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.