SHP-2, His-Tag Recombinant

Catalog #

79018

$385 *

Size: 20 µg

Qty

Bulk/Custom

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Description

Human recombinant SHP-2 (Src homology domain 2 containing tyrosine phosphatase, also known as protein tyrosine phosphatase N11, PTPN11), full length encompassing amino acids 2-593 (end). This construct contains an N-terminal His-tag (6xHis). The recombinant protein was affinity purified and tested for activity.

This product has been cited 1 time.

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Synonyms

SHP2, CFC, NS1, BPTP3, PTP2C, PTP-1D, SH-PTP2, SH-PTP3, MGC14433, SHP

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Product Data Gallery

4-20% SDS-PAGE Coomassie Staining

SHP-2 Activity

SHP-2 (Full-Length) inhibition curve using a fluorogenic assay (#79330). Representative data only; data may vary by lot.

Product Info

Storage and Usage

Citations1

Species

Human

Host Species/Expression System

E. coli

Purity

≥80%

Format

Aqueous buffer solution

Formulation

40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 0.04% Tween-20, and 20% glycerol.

70 kDa

Amino Acids

2-593

Specific Activity

≥50 pmol/min/µg

Genbank #

NM_002834

UniProt #

Q06124

Tag(s)

N-terminal His-tag

Background

Mammalian PTPases can be subdivided into 1 of 2 broad categories: transmembrane receptor PTPases and intracellular PTPases. PTPN11 is one of the 2 closely related mammalian intracellular PTPases whose sequences encode 2 tandem SRC homology 2 (SH2) domains that are located at the amino-terminal side of a single PTPase catalytic domain. 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.

References

1. B.G. Neel et al. Trends Biochem. Sci. (2003) 28: 284

2. J.V. Ravetch & L.L. Lanier Science (2000) 290: 84

Application Reference(s):

1. PCC0208023, a potent SHP2 allosteric inhibitor, imparts an antitumor effect against KRAS mutant colorectal cancer (2020)
2. Allosteric inhibition of SHP2 stimulates anti-tumor immunity by transforming the immunosuppressive environment (2020)