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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human PRKACA Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 33.95 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | His40-Lys310 |
Aliases /Synonyms | PRKACA, PKACA, PKA C-alpha, cAMP-dependent protein kinase catalytic subunit alpha |
Reference | ARO-P12319 |
Note | For research use only. |
Recombinant Human PRKACA Protein, also known as protein kinase A catalytic subunit alpha, is a highly active enzyme that plays a crucial role in cellular signaling and regulation. This protein is encoded by the PRKACA gene and is a member of the protein kinase A (PKA) family. PKA is a key regulator of various cellular processes such as metabolism, cell growth, and gene expression. Recombinant Human PRKACA Protein is produced through genetic engineering techniques and is widely used in biochemical and biomedical research.
Recombinant Human PRKACA Protein is a monomeric protein with a molecular weight of approximately 40 kDa. It consists of two subunits, the catalytic subunit alpha and the regulatory subunit beta. The catalytic subunit alpha is responsible for the enzymatic activity of PKA, while the regulatory subunit beta helps in the regulation of its activity. The catalytic subunit alpha is composed of two domains, the N-terminal domain and the C-terminal domain. The N-terminal domain contains the ATP binding site, while the C-terminal domain contains the catalytic site. The structure of Recombinant Human PRKACA Protein is highly conserved among species, indicating its importance in cellular function.
Recombinant Human PRKACA Protein is a serine/threonine protein kinase that phosphorylates a variety of substrates, including proteins involved in cellular signaling pathways. It is activated by the binding of cAMP to the regulatory subunit beta, which causes the release of the catalytic subunit alpha. The released catalytic subunit alpha then phosphorylates its target proteins, leading to changes in their activity and function. This process is crucial for the regulation of various cellular processes, such as metabolism, cell proliferation, and gene expression. Recombinant Human PRKACA Protein is highly active and has a broad substrate specificity, making it a valuable tool for studying cellular signaling pathways.
Recombinant Human PRKACA Protein has a wide range of applications in biochemical and biomedical research. Its high activity and specificity make it a valuable tool for studying cellular signaling pathways and their role in various diseases. Some of the key applications of Recombinant Human PRKACA Protein are:
Recombinant Human PRKACA Protein is a crucial target for drug discovery and development. Many small molecule inhibitors have been designed to specifically target this protein and modulate its activity. These inhibitors have shown promising results in preclinical studies for the treatment of diseases such as cancer, diabetes, and cardiovascular disorders.
Recombinant Human PRKACA Protein has been identified as a potential biomarker for various diseases. Its activity has been found to be dysregulated in many cancers and other disorders, making it a potential diagnostic and prognostic marker. Furthermore, the levels of this protein can also be measured in bodily fluids, such as blood and urine, making it a non-invasive biomarker for disease detection and monitoring.
Recombinant Human PRKACA Protein has been extensively used in protein-protein interaction studies. Its ability to phosphorylate specific substrates allows researchers to study the role of different proteins in cellular signaling pathways. This has led to a better understanding of the complex network of interactions that regulate various cellular processes.
The crystal structure of Recombinant Human PRKACA Protein has been determined, providing valuable insights into its mechanism of action and potential binding sites for small molecule inhibitors. This information has been used in the design and development of more potent and specific inhibitors for therapeutic use.
Recombinant Human PRKACA Protein has been
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