Recombinant human SHP1 protein
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Recombinant human SHP1 protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.
View Alternative Names
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
- FuncS
Unknown
Functional Studies - Recombinant human SHP1 protein (AB61135)
Sample Kinase Activity Plot.
- FuncS
Unknown
Functional Studies - Recombinant human SHP1 protein (AB61135)
The specific activity of SHP1 (ab61135) was determined to be 1100 nmol phosphate released/min/mg as per activity assay protocol
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human SHP1 protein (AB61135)
SDS PAGE analysis of ab61135
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human SHP1 protein (AB61135)
ab61135 on SDS-PAGE, MW ~93 kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
General info
Function
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).
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.
Post-translational modifications
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).. Ubiquitinated after phosphorylation by TAOK3 (PubMed:38166031). Ubiquitinated by a cooperation between ITCH and WWP2 via 'Lys-27'-mediated polyubiquitin chains resulting in the reduction of its association with LCK (PubMed:29925997).
Subcellular localisation
Nucleus
Target data
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Complementary Products
Product promise
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