The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported. [provided by RefSeq, Jul
Catalog No
A0026
Reactivity
Human, Mouse, Rat
Applications
WB, IHC-p, IF(paraffin section), ELISA
Modification
Phospho Specific
Source
Polyclonal Rabbit
Dilution
Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/10000. Not yet tested in other applications.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Western blot analysis of lysates from RAW264.7 cells treated with EGF 200ng/ml 5', using SHP-1 (Phospho-Tyr536) Antibody. The lane on the right is blocked with the phospho peptide.
Immunohistochemistry analysis of paraffin-embedded human breast carcinoma, using SHP-1 (Phospho-Tyr536) Antibody. The picture on the right is blocked with the phospho peptide.
Immunohistochemical analysis of paraffin-embedded Human breast cancer. Antibody was diluted at 1:100(4° overnight). High-pressure and temperature Tris-EDTA,pH8.0 was used for antigen retrieval. Negetive contrl (right) obtaned from antibody was pre-absorbed by immunogen peptide.
Author:
Sanae Ben Mkaddem, Amaya Murua, Héloise Flament, Dimitri Titeca-Beauport, Carine Bounaix, Luca Danelli, Pierre Launay, Marc Benhamou, Ulrich Blank, Eric Daugas, Nicolas Charles & Renato C. Monteiro