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Merck

P4649

Sigma-Aldrich

磷酸化酶 b 来源于兔肌肉

For use as a marker in SDS-PAGE

别名:

α-葡聚糖磷酸化酶, 1,4-α-D-葡聚糖:正磷酸盐 α-D-葡萄糖基转移酶, 糖原磷酸化酶

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About This Item

CAS号:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352204
NACRES:
NA.54

形狀

powder

分子量

observed mol wt ~97 kDa

包裝

vial of 0.5 mg

儲存溫度

2-8°C

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一般說明

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.

應用

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.

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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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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