Skip to Content
Merck
All Photos(1)

Documents

P7937

Sigma-Aldrich

Protein Phosphatase-1 Catalytic Subunit, α-Isoform from rabbit

5,000-15,000 units/mg protein, recombinant, expressed in E. coli, lyophilized powder

Synonym(s):

Protein phosphatase

Sign Into View Organizational & Contract Pricing


About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

rabbit

Quality Level

recombinant

expressed in E. coli

Assay

≥80% (GE)

form

lyophilized powder

specific activity

5,000-15,000 units/mg protein

mol wt

37.5 kDa

technique(s)

inhibition assay: suitable

UniProt accession no.

storage temp.

−20°C

Gene Information

General description

Protein phosphatase1 (PP1) is a heterodimeric enzyme with serine/threonine phosphatase activity. It comprises a catalytic subunit and a targeting subunit or a specific protein inhibitor. The targeting subunit determines the enzyme localization, e.g., to glycogen particles (subunit G) or to myofibrils (subunit M).

Application

Protein Phosphatase-1 Catalytic Subunit, α-Isoform from rabbit has been used as a standard in protein phosphatase-1 inhibition assay.
Protein Phosphatase-1 Catalytic Subunit, α-Isoform from rabbit has been used in protein phosphatase reaction and in the digestion of adipocyte extracts.

Biochem/physiol Actions

Protein phosphatase1 (PP1) is involved in glycogen metabolism and in regulation of muscle contractility. In addition, it is implicated in cell cycle and transcriptional regulation. Recombinant rabbit PP1α has properties in common with the native rabbit muscle protein including size, requirement for Mn2+ for activity, specificity for phosphorylase A, and inhibition by okadaic acid, microcystin LR, and phosphatase inhibitor2 (I-2).

Packaging

Package size based on protein content.

Unit Definition

One unit will hydrolyze 1 nmole of p-nitrophenyl phosphate per min at pH 7.4 at 30 °C.

Physical form

Lyophilized powder containing imidazole buffer, pH 7.4, NaCl, DTT, EDTA, MnCl2, Tween 20, and trehalose as stabilizer.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

M C Faux et al.
Trends in biochemical sciences, 21(8), 312-315 (1996-08-01)
One important regulatory mechanism in the control of phosphorylation events is the subcellular location of phosphatases of kinases. Several serine/threonine phosphatases and kinases have now been shown to be associated with targeting subunits; these contribute to the organization and specificity
Insulin resistance of glycogen synthase mediated by o-linked N-acetylglucosamine.
Parker GJ
The Journal of Biological Chemistry, 278(12), 10022-10027 (2003)
Satomi Ohtsuka et al.
Biochemistry, 59(17), 1701-1710 (2020-04-17)
Ca2+/calmodulin-dependent protein kinase kinase (CaMKK) activates particular multifunctional kinases, including CaMKI, CaMKIV, and 5'AMP-activated protein kinase (AMPK), resulting in the regulation of various Ca2+-dependent cellular processes, including neuronal, metabolic, and pathophysiological pathways. We developed and characterized a novel pan-CaMKK inhibitor
A J Zhang et al.
The Journal of biological chemistry, 267(3), 1484-1490 (1992-01-25)
The catalytic subunit of rabbit skeletal muscle protein phosphatase-1 was expressed in Escherichia coli. Expression of phosphatase-1 in the pET3a vector, which is based on the use of the T7 promoter, resulted in the expression of the enzyme as an
Regulation of protein phosphatase-1
James B Aggen
Chemistry and Biology, 7.1, R13-R23 (2000)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service