Human B-Cell Receptor CD22 (CD22) Protein
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Description
Human B-Cell Receptor CD22 (CD22) Protein is a recombinant Human protein produced in a Mammalian cell expression system.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | B-Cell Receptor CD22 (CD22) |
| Host | Mammalian cells |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 78.32 kDa Sequence Fragment: Met1-Arg687 Tag: C-terminal His tag |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 100 µg |
| Size 2 | 1 mg |
| Form | Lyophilized Reconstitute in sterile water to produce a stock solution. |
| Tested Applications | ELISA, WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Availability | Shipped within 5-12 working days. |
| Storage | Store at 2-8 °C if the entire vial will be used within 1 week. Aliquot and store at -20 °C for long-term storage. Avoid repeated freeze-thaw cycles. |
| Dry Ice | No |
| UniProt ID | P20273 |
| Alias | SIGLEC2,SIGLEC-2,B-cell receptor CD22,B-lymphocyte cell adhesion molecule,BL-CAM,Sialic acid-binding Ig-like lectin 2,T-cell surface antigen Leu-14 |
| Background | Protein CD22 |
| Note | This product is for research use only. This product is shipped with ice packs. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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anti- CD22 antibody
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.
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