Recombinant human SHP1 protein is a Human Fragment protein, in the 243 to 541 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, Phosphatase Activity.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application Phosphatase Activity | Reactivity Reacts | Dilution info - | Notes - |
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Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis (PubMed:14739280, PubMed:29925997). Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities (PubMed:21258366, PubMed:9733788). When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events (PubMed:11907092, PubMed:14739280, PubMed:37932456, PubMed:38166031). Modulates the signaling of several cytokine receptors including IL-4 receptor (PubMed:9065461). Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling (PubMed:34811497, PubMed:38532423). Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Acts also as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A (PubMed:37595871).
HCP, PTP1C, PTPN6, Tyrosine-protein phosphatase non-receptor type 6, Hematopoietic cell protein-tyrosine phosphatase, Protein-tyrosine phosphatase 1C, Protein-tyrosine phosphatase SHP-1, SH-PTP1, PTP-1C
Recombinant human SHP1 protein is a Human Fragment protein, in the 243 to 541 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, Phosphatase Activity.
pH: 7.5
Constituents: 20% Glycerol (glycerin, glycerine), 0.395% Tris HCl, 0.0292% EDTA, 0.0156% 2-Mercaptoethanol, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab51289 was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer.
Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis (PubMed:14739280, PubMed:29925997). Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities (PubMed:21258366, PubMed:9733788). When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events (PubMed:11907092, PubMed:14739280, PubMed:37932456, PubMed:38166031). Modulates the signaling of several cytokine receptors including IL-4 receptor (PubMed:9065461). Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling (PubMed:34811497, PubMed:38532423). Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Acts also as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A (PubMed:37595871).
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.
Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation (By similarity). Phosphorylation at Tyr-564 by LYN enhances phosphatase activity. Phosphorylation at Thr-394 by TAOK3 leads to polyubiquitination and subsequent proteasomal degradation (PubMed:38166031).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
The catalytic domain of SHP-1 was overexpressed as insoluble protein aggregates (inclusion bodies).
SHP1 also known as PTPN6 belongs to the family of protein tyrosine phosphatases and has a protein mass of approximately 68 kDa. It plays a critical role in cell signaling by dephosphorylating specific targets leading to the modulation of signal transduction pathways. SHP1 is ubiquitously expressed with high levels observed in hematopoietic cells suggesting a specialized function in the immune system.
SHP1 influences cell proliferation survival and differentiation by acting as a negative regulator of signaling pathways. It is not a part of a larger protein complex but it associates transiently with different receptors and substrates. It plays an important role in the immune response by regulating cytokine signaling which is important for maintaining the balance between immune activation and tolerance.
SHP1 significantly impacts the JAK/STAT and B cell receptor signaling pathways. In the JAK/STAT pathway SHP1 interacts with JAK kinases contributing to the downregulation of cytokine signaling. In B cell receptor signaling it associates with Syk influencing immune cell activation and function.
SHP1 has a role in autoimmune diseases such as rheumatoid arthritis and certain types of leukemia. In rheumatoid arthritis defective regulation by SHP1 can lead to excessive inflammation while in leukemia its altered activity impacts cell growth and survival. It interacts with proteins such as STATs and SOCS which are important in these pathologies.
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Analysis of ab51289 (3 μg) by SDS-PAGE under reducing condition and visualized by Coomassie Blue stain.
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