The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Endotoxin level< 0.100 Eu/µg
% SDS-PAGE. Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per µg (1EU/µg).
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
ReconstitutionReconstitute in water to a concentration of 0.1-1.0 mg/ml
B cell receptor CD22 precursor
B lymphocyte cell adhesion molecule
B-cell receptor CD22
B-lymphocyte cell adhesion molecule
sialic acid binding Ig like lectin 2
Sialic acid binding immunoglobulin like lectin 2
Sialic acid-binding Ig-like lectin 2
T cell surface antigen Leu 14
T-cell surface antigen Leu-14
FunctionMediates 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.
DomainContains 4 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Post-translational modificationsPhosphorylation of Tyr-762, Tyr-807 and Tyr-822 are involved in binding to SYK, GRB2 and SYK, respectively. Phosphorylation of Tyr-842 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2. Phosphorylated on tyrosine residues by LYN.