Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus.Migone TS, et al. (1998) Proc Natl Acad Sci USA; 95(7): 3845-3850.Timms JF, et al.(1998) Mol Cell Biol; 18(7): 3838-3850.
Host
Rabbit
Immunogen
Peptide sequence around aa.534~538 (S-E-Y-G-N) derived from Human SHP-1.
Raised In
Rabbit
Reactivity
Human, Mouse, Rat
Regulatory
RUO
Relevance
Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus.
Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.
Pathway
Jak-STAT signaling pathway Adherens junction B cell receptor signaling pathway Natural killer cell mediated cytotoxicity T cell receptor signaling pathway
Protein Families
Protein-tyrosine phosphatase family, Non-receptor class 2 subfamily
Tissue Specificity
Isoform 1 is expressed in hematopoietic cells. Isoform 2 is expressed in non-hematopoietic cells.
Buffer
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Format
liquid
Purification
Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide.
Purity
Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide.
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.