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Name :
SHP-1 Protein

Description :
PTPN6 is an enzyme that belongs to the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of PTPN6 contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of PTPN6 with its substrates. PTPN6 is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. It has been shown that PTPN6 interacts with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling.

Species :
Mouse

Uniprotkb :
Baculovirus-Insect Cells

Tag :
His,GST

Synonyms :
SH-PTP1, Hcph, 70Z-SHP, Ptp1C, protein tyrosine phosphatase, non-receptor type 6, me, hcp, PTPTY-42, SHP-1

Construction :
A DNA sequence encoding the mouse PTPN6 (P29351-2) (Ala207-Lys597) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Protein Purity :
> 85 % as determined by SDS-PAGE

Molecular Weight :
Approxiamtely 72.7 kDa

Endotoxin :

Formulatione :
Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.0, 10% glycerol. Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

Reconstitution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Stability & Storage :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Research Background :
PTPN6 is an enzyme that belongs to the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of PTPN6 contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of PTPN6 with its substrates. PTPN6 is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. It has been shown that PTPN6 interacts with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling.

References and Literature :
1. Yu CL,et al.(2000) Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation. J Biol Chem. 275(1):599-604. 2. Wu DW,et al.(2000) SH2-Containing protein tyrosine phosphatase-1 (SHP-1) association with Jak2 in UT-7/Epo cells. Blood Cells Mol Dis. 26(1):15-24. 3. Jiao H,et al.(1996) Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1. Mol Cell Biol. 16(12):6985-92.

MedChemExpress (MCE) recombinant proteins include: cytokines, enzymes, growth factors, hormones, receptors, transcription factors, antibody fragments, etc. They are often essential for supporting cell growth, stimulating cell signaling pathways, triggering or inhibiting cell differentiation; and are useful tools for elucidating protein structure and function, understanding disease onset and progression, and validating pharmaceutical targets. At MedChemExpress (MCE), we strive to provide products with only the highest quality. Protein identity, purity and biological activity are assured by our robust quality control and assurance procedures.
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Author: Menin- MLL-menin