Human Lyn kinase, cytoplasmic tyrosine kinase, recombinant and active enzyme.
Lyn is a Src family kinase primary expressed in hematopoietic cells, predominantly in B cells. The modular structure is formed by a N-terminal tail, which is myristylated and palmitylated localizing Lyn to lipid rafts within the plasma membrane, a Src homology 3 (SH3) domain, a SH2 domain, the catalytic core and a C-terminal negative regulatory domain. Lyn is associated with the BCR in resting cells and serves upon antigen binding and BCR aggregation to phosphorylate tyrosine containing ITAM motifs on Ig-α/β. The BCR signal is further amplified by phosphorylation of CD19 and Syk. On the other hand Lyn activation results in CD22 phosphorylation and the recruitment and activation of the tyrosine phosphatase SHP-1, which downmodulates BCR-mediated signaling.
Specific activity : 94.000 pmol/mg x min
Method for determination of Km value & specific activity: Filter binding assay MAFC membrane
Protein concentration: 0.222 mg/ml (Bradford method using BSA as standard protein)
Size: 20 µg
Ordering information: shipped on dry ice
Product specific literature:
DeFranco AL, Chan VW, Lowell CA. (1998) "Positive and negative roles of the tyrosine kinase Lyn in B cell function." Semin Immunol.10 (4):299-307.
Gauld SB, Cambier JC. (2004) "Src-family kinases in B-cell development and signaling." Oncogene. 18;23(48):8001-6.
Xu Y, Harder KW, Huntington ND, Hibbs ML, Tarlinton DM. (2005) "Lyn tyrosine kinase: accentuating the positive and the negative." Immunit,. 22(1):9-18.
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