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539735

PTP1B, Human, Recombinant, E. coli

Sinónimos:

Protein Tyrosine Phosphatase 1B

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A ustedes/SKUDisponibilidadPrecio
50 μg
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671,00 €

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NACRES:
NA.77
UNSPSC Code:
12352202
Form:
liquid
Assay:
≥90% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
37,400 g/mol

671,00 €


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biological source

human

Quality Segment

recombinant

expressed in E. coli

assay

≥90% (SDS-PAGE)

form

liquid

specific activity

≥20 U/mg

mol wt

37,400 g/mol

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

shipped in

wet ice

storage temp.

−70°C

Gene Information

human ... PTP1B(5770)

General description

Research area: Cell Signaling

Recombinant, human PTP1B expressed in E. coli. PTP1B, an ubiquitous nontransmembrane protein tyrosine phosphatase, was originally identified in human placenta. This highly active enzyme is useful for the study of tyrosine phosphatase kinetics, substrate specificity, and for screening inhibitors. PTP1B comprises three domains: an N-terminal catalytic domain (1–300), a regulatory domain (301–400), and a C-terminal domain (401–435) that is accountable for directing the enzyme to the endoplasmic reticulum (ER) membrane.

Application

Protein tyrosine phosphatase 1B (PTP1B), Human, Recombinant, E. coli has been used in the dephosphorylation assay of Glutathione S-transferase (GST) fusion proteins as well as in the in vitro kinase assays. It has also been used to construct a 66-member PTP1B library for discovery of enzyme inhibitors using click chemistry.[1]

Biochem/physiol Actions

Protein tyrosine phosphatase 1B (PTP1B) serves as a crucial enzyme in dephosphorylating insulin receptor and its downstream signaling components. Furthermore, it participates in the negative regulation of the leptin signaling pathway by dephosphorylation of the upstream signaling molecules, leading to the suppression of the neuropeptide Y synthesis, an appetite-stimulating hormone. Improper functioning of PTP1B has been associated with a variety of human diseases, including cancer, diabetes, obesity and inflammation.[1]

Packaging

Please refer to vial label for lot-specific concentration.

Physical form

In 50 mM HEPES, 1 mM DTT, 1 mM EDTA, 0.05% NP-40, pH 7.2.

Preparation Note

Following initial thaw, aliquot and freeze (-70°C).

Other Notes

One unit is defined as the amount of enzyme that will hydrolyze 1 µmol of phosphopeptide substrate (Cat. No. 539737) per min at 30°C, pH 7.2 using 150 µM of substrate.
Puius, Y.A., et al. 1997. Proc. Natl. Acad. Sci. USA94, 13420.
Liu, F., et al. 1996. J. Biol. Chem.271, 31290.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Standard Handling (A)

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Este artículo
539568616374553325
assay

≥90% (SDS-PAGE)

assay

-

assay

≥95% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

biological source

human

biological source

-

biological source

-

biological source

-

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

mol wt

37,400 g/mol

mol wt

-

mol wt

-

mol wt

-

form

liquid

form

liquid

form

liquid

form

liquid

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles


Clase de almacenamiento

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable



Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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