protein

Recombinant human PTP1B protein

PTB2001

20 ug

55 USD

Recombinant human PTP1B protein

1-321aa

PTB2001

NP_002818.1

The protein coding region of the catalytic domain of PTP-1B (amino acids 1-321) was cloned into an E. coli expression vector. The catalytic domain of PTP-1B was overexpressed in E. coli as a soluble protein, and it was purified by conventional column chromatographic techniques.

Protein tyrosine phosphatase non-receptor type 1, PTPN1, PTP1B, PTP-1B, Protein Tyrosine Phosphatase 1B, EC 3.1.3.48, Protein-tyrosine phosphatase1B, Tyrosine-protein phosphatase non-receptor type 1, Protein tyrosine phosphatase non-receptor type 1, Protein Tyrosine Phosphatase Non Receptor Type-1

1mg/ml (determined by Bradford assay)

Liquid in. 25mM Tris-HCl buffer (pH 7.5) containing 2mM beta-mercaptoethanol, 1mM EDTA1mM DTT, 20% glycerol

Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Chernoff J., et al. (1990) Proc. Natl. Acad. Sci. uSA. 87, 2735-9

> 95% by SDS-PAGE

Specific activity is > 10,000unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.

SDS-PAGE, Enzyme Activity

Human

Signal Transduction

37.3 kDa (321aa)

< 1 EU per 1ug of protein (determined by LAL method)

Specific activity is > 10,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.

MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSLK CAQYWPQKEE KEMIFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE PPPEHIPPPP RPPKRILEPH N

Non-Tagged

E.coli

Recombinant Protein

P18031

PTP1B, Protein tyrosine phosphatase non-receptor type 1, PTPN1, PTP1B, PTP-1B, Protein Tyrosine Phosphatase 1B, EC 3.1.3.48, Protein-tyrosine phosphatase1B, Tyrosine-protein phosphatase non-receptor type 1, Protein tyrosine phosphatase non-receptor type 1, Protein Tyrosine Phosphatase Non Receptor Type-1,PTB2001-10ug,PTB2001-20ug,PTB2001-50ug,PTB2001-100ug,PTB2001-250ug,PTB2001-500ug,PTB2001-1mg,PTB2001-10,PTB2001-20,PTB2001-50,PTB2001-100,PTB2001-250,PTB2001-500,PTB2001-1

Kimura K, et al. Pyrroloquinoline quinone stimulates epithelial cell proliferation by activating epidermal growth factor receptor through redox cycling. (Free Radic Biol Med. 2012){https://pubmed.ncbi.nlm.nih.gov/22824864/};;Maeda A, et al. Safranal, a novel protein tyrosine phosphatase 1B inhibitor, activates insulin signaling in C2C12 myotubes and improves glucose tolerance in diabetic KK-Ay mice. (Mol Nutr Food Res. 2014){https://pubmed.ncbi.nlm.nih.gov/24668740/};;Quang TH, et al. Protein Tyrosine Phosphatase 1B Inhibitors from the Roots of Cudrania tricuspidata. (Molecules. 2015){https://pubmed.ncbi.nlm.nih.gov/26091075/};;Naito Y. et al. Bis(hinokitiolato)zinc complex ([Zn(hkt)2]) activates Akt/protein kinase B independent of insulin signal transduction. (J Biol Inorg Chem. 2016){https://doi.org/10.1007/s00775-016-1364-9};;Cho KH, et al. Isolation and structure determination of a new diketopiperazine dimer from marine-derived fungus Aspergillus sp. SF-5280. (Nat Prod Res. 2018){https://pubmed.ncbi.nlm.nih.gov/28670919/};;Park JS, et al. Furanoaustinol and 7-acetoxydehydroaustinol: new meroterpenoids from a marine-derived fungal strain Penicillium sp. SF-5497. (J Antibiot (Tokyo). 2018){https://pubmed.ncbi.nlm.nih.gov/29463888/};;VK Thu, et al. Protein tyrosine phosphatase 1B inhibitory triterpene glycosides from Mussaenda pilosissima Valeton. (Phytochemistry Letters. 2020){https://doi.org/10.1016/j.phytol.2020.01.023.};;Kim HJ, et al. PTP1B Inhibitory Secondary Metabolites from an Antarctic Fungal Strain Acremonium sp. SF-7394. (Molecules. 2021){https://pubmed.ncbi.nlm.nih.gov/34576982/};;Tran Thi Hong H, Iridoids from the aerial parts of Adenosma caeruleum with their nitric oxide inhibitory effects. (J Mol Struct. 2024){https://doi.org/10.1016/j.molstruc.2023.137149}