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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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

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 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’.

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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.
Phosphorylase Is Regulated by Allosteric Interactions and Reversible Phosphorylation
Berg JM, et al.
Biochemistry (2011)
C Donnet et al.
The Journal of biological chemistry, 276(10), 7357-7365 (2000-12-02)
Thermal denaturation can help elucidate protein domain substructure. We previously showed that the Na,K-ATPase partially unfolded when heated to 55 degrees C (Arystarkhova, E., Gibbons, D. L., and Sweadner, K. J. (1995) J. Biol. Chem. 270, 8785-8796). The beta subunit
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)
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)

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