Bacterially expressed fusion protein representing amino acids 216-434 of human SLP76 with histidine tag
SLP76 (SH2 domain-containing leukocyte protein of 76 kDa) is a cytosolic adaptor protein which translocates to the plasma mambrane and is involved in multiple signaling pathways in T cells, mast cells, neutrophils and platelets, B cells express its analog SLP65/BLNK (B cell linker protein). SLP76 is phosphorylated by Syk-family and Tec-family tyrosine kinases and couples them to the phosphorylation and activation of PLC-gamma. Via Gads or Grb2, SLP76 also associates with LAT adaptor by involvement of SLP76 proline-rich region. The SH2 domain of SLP76 has been identified as the region involved in binding the serine/threonine kinase HPK1. HPK1 may act as both a positive and a negative regulator by promoting the Jnk-mitogen activated protein kinase (MAPK) pathway and inhibiting the pathway leading to AP-1 activation.
Klonalität:
Monoclonal
Konzentration:
1 mg/ml
Klon-Bezeichnung:
[SLP-76/03]
Isotyp:
Mouse IgG2b
Puffer:
Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
