Human Protein Kinase, AMP-Activated, Beta 1 Non-Catalytic Subunit (PRKAB1) Protein
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Description
Human Protein Kinase, AMP-Activated, Beta 1 non-Catalytic Subunit Protein is a recombinant protein kinases.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Protein Kinase, AMP-Activated, Beta 1 Non-Catalytic Subunit (PRKAB1) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Expression | Recombinant |
| Purity | > 85% (SDS-PAGE) |
| Size 1 | 1 µg |
| Size 2 | 5 µg |
| Size 3 | 50 µg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Storage | Store at 4 °C if the entire vial will be used within 2-4 weeks. Store at -20 °C for long term storage. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q9Y478 |
| Background | Protein PRKAB1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.
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