Cart (0 Items)
Your cart is currently empty.
View ProductsSize | 100ug |
---|---|
Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human ATP1B2 Protein, N-His |
---|---|
Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 26.14 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 | Gly81-Thr290 |
Aliases /Synonyms | ATP1B2, Adhesion molecule in glia, Sodium/potassium-transporting ATPase subunit beta-2, Sodium/potassium-dependent ATPase subunit beta-2, AMOG |
Reference | ARO-P11857 |
Note | For research use only. |
Recombinant Human ATP1B2 Protein, also known as Sodium/Potassium-transporting ATPase subunit beta-2, is a protein that plays a crucial role in maintaining the balance of sodium and potassium ions in cells. This protein is encoded by the ATP1B2 gene and is a member of the ATPase family of proteins.
The Recombinant Human ATP1B2 Protein is composed of 302 amino acids with a molecular weight of approximately 33 kDa. It is a transmembrane protein that consists of two subunits – alpha and beta. The alpha subunit is responsible for the catalytic activity of the protein, while the beta subunit is involved in regulating the activity and stability of the alpha subunit.
The beta subunit of the Recombinant Human ATP1B2 Protein contains a large extracellular domain, a single transmembrane domain, and a small cytoplasmic domain. The extracellular domain is glycosylated and contains binding sites for sodium, potassium, and ATP. The transmembrane domain anchors the protein to the cell membrane, while the cytoplasmic domain interacts with the alpha subunit and other regulatory proteins.
The main function of Recombinant Human ATP1B2 Protein is to maintain the electrochemical gradient of sodium and potassium ions across the cell membrane. This is essential for various cellular processes such as nerve conduction, muscle contraction, and nutrient uptake.
The alpha subunit of the protein uses energy from ATP to transport three sodium ions out of the cell and two potassium ions into the cell. This process is crucial for maintaining the resting membrane potential of cells and for generating action potentials in nerve and muscle cells.
The beta subunit of the Recombinant Human ATP1B2 Protein plays a regulatory role by modulating the activity of the alpha subunit. It also helps in targeting the protein to specific locations in the cell and in maintaining its stability.
Recombinant Human ATP1B2 Protein has a wide range of applications in both research and therapeutic settings.
In research, this protein is used as an antigen in various studies related to ion transport, membrane proteins, and neurological disorders. It is also used in drug discovery and development, as aberrations in the function of this protein have been linked to several diseases, including hypertension, diabetes, and neurological disorders.
In therapeutic applications, Recombinant Human ATP1B2 Protein is being investigated as a potential target for the treatment of diseases such as hypertension and epilepsy. It is also being studied for its potential role in drug resistance in cancer cells.
In summary, Recombinant Human ATP1B2 Protein is a crucial protein involved in maintaining the balance of sodium and potassium ions across the cell membrane. Its structure, function, and applications make it a valuable protein for both research and therapeutic purposes. Further studies on this protein may lead to a better understanding of its role in various diseases and the development of new treatments.
Got a question or need a quote?
Message us and we’ll get back to you 48 hours or less.
Reviews
There are no reviews yet.