|Application ||WB, DB|
|Other Accession||P41499, P35235|
|Calculated MW||H=45 KDa|
|Antigen Region||574-590 aa|
|Other Names||PTPN11; PTP2C; SHPTP2; Tyrosine-protein phosphatase non-receptor type 11; Protein-tyrosine phosphatase 1D; Protein-tyrosine phosphatase 2C; SH-PTP2; SH-PTP3|
|Target/Specificity||This SHP2 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding Y584 of human SHP2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-SHP2(Y584) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73 (PubMed:26742426).|
|Cellular Location||Cytoplasm. Nucleus|
|Tissue Location||Widely expressed, with highest levels in heart, brain, and skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
SHP2 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. This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.
Carver, K.C., et al. J. Biol. Chem. 285(11):8003-8012(2010)
Pierpont, E.I., et al. Am. J. Med. Genet. A 152A (3), 591-600 (2010)
Rani, D.S., et al. Mitochondrion 10(2):166-173(2010)
Bakken, T., et al. Virology 397(2):379-388(2010)
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