SHP-1 (phospho-Y536) polyclonal, anti-human, mouse, rat
€328.00
In stock
SKU
BS4169
Background:
SHP-1 (PTPN6) is a non-receptor protein tyrosine phosphatase that is expressed primarily in hematopoietic cells. The enzyme is composed of two SH2 domains, a tyrosine phosphatase catalytic domain, and a carboxy-terminal regulatory domain. SHP-1 removes phosphates from target proteins to downregulate several tyrosine kinase-regulated pathways. In hematopoietic cells, the amino-terminal SH2 domain of SHP-1 binds to tyrosine phosphorylated erythropoietin receptors (EpoR) to negatively regulate hematopoietic growth. Overexpression of SHP-1 in epithelial cells results in dephosphorylation of the Ros receptor tyrosine kinase and subsequent downregulation of Ros-dependent cell proliferation and transformation. Following ligand binding in myeloid cells, SHP-1 associates with the IL-3R β chain and downregulates IL-3-induced tyrosine phosphorylation and cell proliferation.
Alternative Name:
Tyrosine-protein phosphatase non-receptor type 6, Hematopoietic cell protein-tyrosine phosphatase, Protein-tyrosine phosphatase 1C, PTP-1C, Protein-tyrosine phosphatase SHP-1, SH-PTP1, PTPN6, HCP, PTP1C
Application Dilution: WB: 1:500~1:1000, IHC: 1:50~1:200
Specificity: p-SHP-1 (Y536) polyclonal antibody detects endogenous levels of SHP-1 protein only when phosphorylated at Tyr536.
Immunogen:
Synthetic phosphopeptide derived from human SHP-1 around the phosphorylation site of Tyrosine 536.
MW: ~ 68 kDa
Swis Prot.: P29350
Purification & Purity:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Format:
1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Storage:
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
For research use only, not for use in diagnostic procedure.
SHP-1 (PTPN6) is a non-receptor protein tyrosine phosphatase that is expressed primarily in hematopoietic cells. The enzyme is composed of two SH2 domains, a tyrosine phosphatase catalytic domain, and a carboxy-terminal regulatory domain. SHP-1 removes phosphates from target proteins to downregulate several tyrosine kinase-regulated pathways. In hematopoietic cells, the amino-terminal SH2 domain of SHP-1 binds to tyrosine phosphorylated erythropoietin receptors (EpoR) to negatively regulate hematopoietic growth. Overexpression of SHP-1 in epithelial cells results in dephosphorylation of the Ros receptor tyrosine kinase and subsequent downregulation of Ros-dependent cell proliferation and transformation. Following ligand binding in myeloid cells, SHP-1 associates with the IL-3R β chain and downregulates IL-3-induced tyrosine phosphorylation and cell proliferation.
Alternative Name:
Tyrosine-protein phosphatase non-receptor type 6, Hematopoietic cell protein-tyrosine phosphatase, Protein-tyrosine phosphatase 1C, PTP-1C, Protein-tyrosine phosphatase SHP-1, SH-PTP1, PTPN6, HCP, PTP1C
Application Dilution: WB: 1:500~1:1000, IHC: 1:50~1:200
Specificity: p-SHP-1 (Y536) polyclonal antibody detects endogenous levels of SHP-1 protein only when phosphorylated at Tyr536.
Immunogen:
Synthetic phosphopeptide derived from human SHP-1 around the phosphorylation site of Tyrosine 536.
MW: ~ 68 kDa
Swis Prot.: P29350
Purification & Purity:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Format:
1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Storage:
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
For research use only, not for use in diagnostic procedure.
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