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P4649

Sigma-Aldrich

Phosphorylase b from rabbit muscle

For use as a marker in SDS-PAGE

Synonym(s):

α-Glucan Phosphorylase, 1,4-α-D-Glucan:orthophosphate α-D-glucosyltransferase, Glycogen Phosphorylase

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About This Item

CAS Number:
9012-69-5
Enzyme Commission number:
2.4.1.1 (BRENDA, IUBMB)
EC Number:
232-737-0
MDL number:
MFCD00131905
UNSPSC Code:
12352204
NACRES:
NA.54

form

powder

mol wt

observed mol wt ~97 kDa

packaging

vial of 0.5 mg

storage temp.

2-8°C

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General description

Phosphorylase b is a dimer, usually exists in inactive form in the skeletal muscles. Equilibrium exists between an active relaxed (R) state and a less active tense (T). Phosphorylase b favors the T state. The enzyme possesses three domains, the N-terminal domain, glycogen-binding domain and the C-terminal domain.

Application

Phosphorylase b from rabbit muscle has been used as a molecular weight marker in 12% polyacrylamide gel for keratinase, and stress-70 protein.
Phosphorylase b from rabbit muscle is to be used as a marker in SDS-PAGE. Phosphorylase b is used during chemical cross-linking studies as a SDS-PAGE molecular weight standard.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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B Chen et al.
The Journal of biological chemistry, 275(45), 34946-34953 (2000-08-17)
The envelope glycoprotein, gp160, of simian immunodeficiency virus (SIV) shares approximately 25% sequence identity with gp160 from the human immunodeficiency virus, type I, indicating a close structural similarity. As a result of binding to cell surface CD4 and co-receptor (e.g.
Signal Transduction and Protein Phosphorylation (2012)
Characterization of alkaline keratinase of Bacillus licheniformis strain HK-1 from poultry waste
Korkmaz H, et al.
Annales de Microbiologie, 54(2), 201-211 (2004)
Crystallographic studies on the activity of glycogen phosphorylase b
Weber IT, et al.
Nature, 274(5670), 433-433 (1978)
Stress-70 proteins in marine mussel Mytilus galloprovincialis as biomarkers of environmental pollution: a field study
Hamer B, et al.
Environment International, 30(7), 873-882 (2004)
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