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Anti-CD22 antibody

SKU Product Brand Unit Availability Price Quantity  
AB-06-5055
Anti-CD22 antibody
Erpan Tech In stock

Specifications        

Product Cat#: AB-06-5055
Product type: Primary antibody
Antigen: CD22
Immunogen: Synthetic peptide within Human CD22 aa 1-100 (N terminal).
Species immunized: Rabbit
Isotype: IgG
Applications: Western Blot (1:500-1:1000); Immunohistochemistry-Paraffin (1:500-1:1000)
Reactivity: Human
Clonality (clone number): Monoclonal, PO00-31
Form: Liquid
Buffer: 1*PBS buffer (pH7.4), 0.1% BSA, 40% Glycerol, 0.05% NaN3.
Concentration: 1 mg/ml
Purity: Protein A purified.
Storage: Aliquot and freeze at -20°C. Avoid multiple freeze/thaw cycles.
Conjugate: Unconjugated
Alternative names: B cell receptor CD22 precursor antibody
B lymphocyte cell adhesion molecule antibody
B-cell receptor CD22 antibody
B-lymphocyte cell adhesion molecule antibody
BL CAM antibody
BL-CAM antibody
BLCAM antibody
CD 22 antibody
CD22 antibody
CD22 antigen antibody
CD22 molecule antibody
CD22 protein antibody
CD22_HUMAN antibody
Lectin 2 antibody
Leu14 antibody
Lyb8 antibody
MGC130020 antibody
sialic acid binding Ig like lectin 2 antibody
Sialic acid binding immunoglobulin like lectin 2 antibody
Sialic acid-binding Ig-like lectin 2 antibody
SIGLEC 2 antibody
Siglec-2 antibody
SIGLEC2 antibody
T cell surface antigen Leu 14 antibody
T-cell surface antigen Leu-14 antibody
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Target information

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.

Provider

Erpantech Laboratory