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Safety Information

P2014

Sigma-Aldrich

Phosphorylase Kinase from rabbit muscle

lyophilized powder, ≥60 units/mg protein

Synonym(s):

ATP:phosphorylase-b phosphotransferase, Dephosphophosphorylase kinase

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About This Item

CAS Number:
9001-88-1
Enzyme Commission number:
2.7.1.38 (BRENDA, IUBMB)
MDL number:
MFCD00131906
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

≥60 units/mg protein

composition

Protein, 20-40% biuret

foreign activity

ATPase ≤0.5%
phosphorylase a ≤1%
phosphorylase b ≤5%

storage temp.

−20°C

General description

Phosphorylase kinase contains four subunits each containing an α, β, γ, and sigma component. The sigma component binds 4 calcium molecules and is termed calmodulin while the γ unit acts as the catalytic subunit.

Application

Phosphorylase kinase from rabbit muscle has been used in a study to assess features of glycogen phosphorylase. It has also been used in a study to investigate the activation of different forms of muscle phosphorylase kinase by actin.

Unit Definition

One unit will form 1.0 μmolar unit of phosphorylase a from phosphorylase b per min at pH 7.7 at 30°C in the presence of ATP.

Physical form

Lyophilized powder containing (NH4)2SO4, sucrose, β-glycerophosphate and dithioerythritol

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P2014-BULK:
P2014-2.5KU:
P2014-200UN:
P2014-VAR:
P2014-1KU:

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Certificates of Analysis (COA)

Lot/Batch Number
SLBT1593
011M7671V
105K7570
123K7400
109H7465

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G Kamp
Biological chemistry Hoppe-Seyler, 367(2), 109-117 (1986-02-01)
The activities of glycogen phosphorylases a and b from the body wall musculature of the marine worm Arenicola marina (Annelida, Polychaeta) were determined after various periods of anoxia. Already under normoxic conditions one third of the total activity was produced
M Amin-ul Mannan et al.
Journal of molecular biology, 425(12), 2083-2099 (2013-04-02)
The endoplasmic reticulum transmembrane receptor Ire1 senses over-accumulation of unfolded proteins in the endoplasmic reticulum and initiates the unfolded protein response (UPR). The cytoplasmic portion of Ire1 has a protein kinase domain (KD) and a kinase extension nuclease (KEN) domain
Kathryn A Skelding et al.
Advances in experimental medicine and biology, 740, 703-730 (2012-03-29)
Calcium/calmodulin-stimulated protein kinases can be classified as one of two types - restricted or multifunctional. This family of kinases contains several structural similarities: all possess a calmodulin binding motif and an autoinhibitory region. In addition, all of the calcium/calmodulin-stimulated protein
Thomas P Howard et al.
Plant signaling & behavior, 6(12), 2026-2030 (2011-11-25)
The chloroplast protein CP12 forms a multi-enzyme complex with the Calvin-Benson cycle enzymes phosphoribulokinase (PRK) and NADP-glyceraldehyde-3-phosphate dehydrogenase (GAPDH). PRK and GAPDH are inactivated when present in this complex, a process shown in vitro to be dependent upon oxidized CP12.
S Camus et al.
Oncogene, 31(39), 4333-4342 (2011-12-20)
Angiogenesis is essential for development and tumor progression. With the aim of identifying new compound inhibitors of the angiogenesis process, we used an established enhanced green fluorescent protein-transgenic zebrafish line to develop an automated assay that enables high-throughput screening of
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