ATPase, Na+/K+ Transporting Beta 1 Polypeptide (ATP1B1) Peptide

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Description
ATPase, Na+/K+ Transporting Beta 1 Polypeptide (ATP1B1) Peptide is a synthetic peptide.
Documents del producto
Product specifications
Category | Proteins and Peptides |
Immunogen Target | ATPase, Na+/K+ Transporting Beta 1 Polypeptide (ATP1B1) |
Host | Synthetic |
Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
Conjugation | Unconjugated |
Observed MW | Sequence Fragment: Internal region: C-KTEISFRPNDPKSYE |
Size 1 | 100 µg |
Form | Lyophilized Reconstitute in deionized water. |
Tested Applications | P-ELISA |
Buffer | Prior to lyophilization: Deionized water. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
Gene ID | 481 |
NCBI Accession | NP_001668.1, NP_001001787.1 |
Background | Protein ATP1B1 |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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ATP1B1 Antibody is a Rabbit Polyclonal antibody against ATP1B1. The protein encoded by this gene belongs to the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane. The glycoprotein subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes a beta 1 subunit. Alternatively spliced transcript variants encoding different isoforms have been described, but their biological validity is not known.
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