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SRP0215

Sigma-Aldrich

PTP1B full length Active human

recombinant, expressed in E. coli, aqueous solution, ≥55% (SDS-PAGE)

Synonym(s):

PTPN1, Protein tyrosine phosphatase, non-receptor type 1

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥55% (SDS-PAGE)

form

aqueous solution

mol wt

76 kDa

packaging

pkg of 20 μg

storage condition

(Tightly closed)
avoid repeated freeze/thaw cycles

concentration

1.65 mg/mL

technique(s)

inhibition assay: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PTPN1(5770)

General description

Research area: Cell signaling

The gene PTPN1 (protein tyrosine phosphatase-1B) is mapped to human chromosome 20q13.13 and encodes a member of the protein tyrosine phosphatase (PTP) family. The open reading frame of 1305 bp encodes a protein of 435 amino acids. It is localized at the cytoplasmic side of the endoplasmic reticulum. PTP1B is characterized by a phosphatase catalytic domain and a proline-rich domain.

Application

PTP1B full length Active human is useful for the study of enzyme kinetics, regulation, to dephosphorylate target substrates and for screening inhibitors.
PTPN1 has been used for dephosphorylation of PP2A (protein phosphatase 2A).It has also been used in recombinant protein tyrosine phosphatase-1B (PTP1B) assay.

Biochem/physiol Actions

The protein protein tyrosine phosphatase-1B (PTP1B) catalyzes the dephosphorylation of tyrosine residues of the activated insulin receptor and the insulin receptor substrate 1, thereby downregulating the insulin signaling cascade. It dephosphorylates JAK2 and STAT3 and inhibits leptin signaling. Polymorphism of this gene in mice has shown to be associated with type 2 diabetes and obesity. PTP1B dephosphorylates the epidermal growth factor receptor. It acts as a modulator of insulin-like growth factor receptor (IGFR) and MET-mediated signaling responses. The protein may be useful as a drug target in type 2 diabetes and obesity. It has been shown to enhance tumor progression in various cancers like that of the breast, colon and prostate. It acts a tumor suppressor in other cancers (lymphomas and esophageal cancers). PTP1B is implicated in the positive regulation of integrin and cadherin signaling.(1) In addition, human PTP1B is also involved in casein kinase II (CKII) and p60c-src-induced signal transduction pathway.

Unit Definition

One unit will hydrolyze 1 nmol p-nitrophenyl phosphate per minute at pH 7.4 and 30°C.

Physical form

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol, and 3 mM DTT.

Preparation Note

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

inhibitor

Product No.
Description
Pricing

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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PTP1B-dependent regulation of receptor tyrosine kinase signaling by the actin-binding protein Mena.
Hughes SK
Molecular Biology of the Cell, 26(21), 3867-3878 (2015)
E J Jung et al.
Biochemical and biophysical research communications, 246(1), 238-242 (1998-05-26)
We have cloned a soluble chicken protein tyrosine phosphatase, named CPTP1, from the cDNA library of chicken intestine. The CPTP1 showed 92% sequence identity to the corresponding 321 amino acid residues of human PTP1B (HPTP1B). CPTP1 lacked 13 amino acids
PTP1B promotes cell proliferation and metastasis through activating src and ERK1/2 in non-small cell lung cancer.
Liu H
Cancer Letters, 359(2), 218-225 (2015)
Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology.
Liu R
Journal of Cellular and Molecular Medicine, 12, 241-257 (2008)
Alicja Kuban-Jankowska et al.
Anticancer research, 37(9), 4799-4806 (2017-09-06)
Rapidly-dividing cancer cells have higher requirement for iron compared to non-transformed cells, making iron chelating a potential anticancer strategy. In the present study we compared the anticancer activity of uncommon iron chelator aurintricarboxylic acid (ATA) with the known deferoxamine (DFO).

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