Phospho-SHP-1 (Tyr536) Recombinant Rabbit Monoclonal Antibody (Shp1Y536-2A7), Invitrogen™
Rabbit Recombinant Monoclonal Antibody
Manufacturer: Fischer Scientific
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Antigen
Phospho-SHP-1 (Tyr536)
Concentration
0.5 mg/mL
Classification
Monoclonal
Form
Liquid
Regulatory Status
RUO
Formulation
PBS with 0.10% BSA, 50% glycerol and 0.02% sodium azide
Gene Alias
70Z-SHP; EC 3.1.3.48; hcp; Hcph; hematopoietic cell phosphatase; hematopoietic cell protein-tyrosine phosphatase; HPTP1C; me; motheaten; protein tyrosine phosphatase, non-receptor type 6; protein-tyrosine phosphatase 1C; Protein-tyrosine phosphatase SHP-1; PTN6; Ptp1C; PTP-1C; Ptph6; PTPN6; PTPTY-42; SH2 phosphatase 1; SHP1; Shp-1; SHP-1L; SH-PTP1; Tyrosine-protein phosphatase non-receptor type 6
Gene Symbols
PTPN6
Isotype
IgG κ
Purification Method
Protein A/G
Product Type
Antibody
Clone
Shp1Y536-2A7
Applications
Flow Cytometry
Conjugate
Unconjugated
Host Species
Rabbit
Target Species
Human
Gene Accession No.
P29350
Gene ID (Entrez)
5777
Immunogen
A synthetic phospho-peptide corresponding to residues surrounding Tyr536 of human phospho Shp1.
Primary or Secondary
Primary
Content And Storage
-20°C
Gene
PTPN6
Related Products
Description
- 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 beta chain and downregulates IL-3-induced tyrosine phosphorylation and cell proliferation.