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AB51289

Recombinant human SHP1 protein (Tag Free)

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Recombinant human SHP1 protein (Tag Free) is a Human Fragment protein, in the 243 to 541 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Phosphatase Activity, 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

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SDS-PAGE - Recombinant human SHP1 protein (Tag Free) (AB51289)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human SHP1 protein (Tag Free) (AB51289)

Analysis of ab51289 (3 μg) by SDS-PAGE under reducing condition and visualized by Coomassie Blue stain.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

Phosphatase Activity, SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific activity: > 5,000 units/mg of SHP-1. [Unit Definition : One unit will hydrolyze 1 nanomole of p-nitrophenylphosphatate per minute at pH 7.5 at 37°C using 10mM of substrate.]

Accession

P29350

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Phosphatase Activity": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

The catalytic domain of SHP-1 was overexpressed as insoluble protein aggregates (inclusion bodies).
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Sequence info

[{"sequence":"M-GFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ\r\nGRDSNIPGSD YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW\r\nQENSRVIVMT TREVEKGRNK CVPYWPEVGM QRAYGPYSVT\r\nNCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDH GVPSEPGGVL\r\nSFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDC\r\nDIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNIT Y","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":541,"aminoAcidStart":243,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P29350","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
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.

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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Specifications

Form

Liquid

Additional notes

ab51289 was purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer.

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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

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Product protocols

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Target data

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).
See full target information PTPN6
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