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
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
Looking for similar products? Visit Product Comparison Guide
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
Biochemistry (2011)
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
Environment International, 30(7), 873-882 (2004)
Characterization of alkaline keratinase of Bacillus licheniformis strain HK-1 from poultry waste
Annales de Microbiologie, 54(2), 201-211 (2004)
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