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重組人鈉鉀ATP酶蛋白a1

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產品編號bs-42166P
英文名稱Recombinant human ATP1A1 protein, His
中文名稱重組人鈉鉀ATP酶蛋白a1
別    名alpha 1 Sodium Potassium ATPase; A1A1; AT1A1; AT1A1_HUMAN; Atpa-1; ATPase Na+/K+ transporting alpha 1 polypeptide; ATPase Na+/K+ transporting subunit alpha 1; BC010319; EC 3.6.3.9; MGC3285; MGC38419; MGC51750; Na K ATPase alpha A catalytic polypeptide; Na K ATPase catalytic subunit alpha A protein; Na(+)/K(+) ATPase 1; Na(+)/K(+) ATPase alpha-1 subunit; Na+, K+ ATPase alpha subunit; Na+/K+ ATPase alpha 1 subunit; Na+/K+ ATPase 1; Na,K ATPase alpha 1 subunit; Nkaa1b; Sodium potassium ATPase alpha 1 polypeptide; Sodium pump 1; Sodium pump subunit alpha-1; sodium-potassium ATPase catalytic subunit alpha-1; Sodium/potassium-transporting ATPase subunit alpha-1.  
理論分子量39.1kDa
性    狀Lyophilized or Liquid
濃    度>1mg/ml
物    種Human
序    列347-682/1023
純    度> 90% as determined by SDS-PAGE
純化方法AC
表達系統(tǒng)E.coli
活性Not tested
標簽N-His
緩 沖 液20mM Tris-Hcl (pH=8.0)
保存條件Stored at -70℃ or -20℃. Avoid repeated freeze/thaw cycles.
注意事項This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
產品介紹The protein encoded by this gene belongs to the family of P-type cation transport ATPases, 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 catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 1 subunit. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May2009].

SWISS:
P05023

Gene ID:
476

產品圖片
The purity of the protein is greater than 90% as determined by reducing SDS-PAGE.
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