

| Catalog No. | MB011021 |
|---|---|
| Description |
Recombinant Mouse CD22 Protein, C-His (MB011021) expressed in Mammalian Cells, spanning Met1-Arg708. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | Mammalian cells |
| Accession | P35329 |
| Protein length | Met1-Arg708 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Mus musculus (Mouse) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 80.44 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | B-cell receptor CD22, B-lymphocyte cell adhesion molecule, BL-CAM, CD22, SIGLEC2, Sialic acid-binding Ig-like lectin 2, Siglec-2, T-cell surface antigen Leu-14 |
| Background | B-cell receptor CD22 is a ~97 kDa protein. Most highly expressed siglec (sialic acid-binding immunoglobulin-like lectin) on B-cells that plays a role in various aspects of B-cell biology including differentiation, antigen presentation, and trafficking to bone marrow. Binds to alpha 2,6-linked sialic acid residues of surface molecules such as CD22 itself, CD45 and IgM in a cis configuration. Can also bind to ligands on other cells as an adhesion molecule in a trans configuration. Acts as an inhibitory coreceptor on the surface of B-cells and inhibits B-cell receptor induced signaling, characterized by inhibition of the calcium mobilization and cellular activation. Mechanistically, the immunoreceptor tyrosine-based inhibitory motif domain is phosphorylated by the Src kinase LYN, which in turn leads to the recruitment of the protein tyrosine phosphatase 1/PTPN6, leading to the negative regulation of BCR signaling. 1. Kelm, S. et al. (1994) Current biology : CB 4, 965-72. PMID: 7533044 2. Nitschke, L. et al. (1997) Current biology : CB 7, 133-43. PMID: 9016707 |
| Note | For research use only |



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