P4649
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
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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)
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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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