产品名称：Anti-AQP9抗体

Cat. Number:

YB2060R

Quantity size:

0.1ml

Concentration:

Anti-AQP9抗体1mg/ml   Buffer = 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.

Background:

Anti-AQP9抗体Water is a critical component of all living cells. Interestingly, tissue membranes show a great degree of water permeability. Mammalian red cells, renal proximal tubules, and descending thin limb of Henle are extraordinarily permeable to water. Water crosses hydrophobic plasma membranes either by simple diffusion or through a facilitative transport mechanism mediated by special protein "aquaporin". A new member of AQP family, Aquaporin-9 (AQP9), has been cloned from human leukocytes by homology cloning (Ishibashi et al. 1997). It is mostly homologous with AQP3 and AQP7 (54-48% identity). AQP9 (295 AA) is primarily expressed in peripheral leukocytes, and lesser amounts in liver, lung and spleen. AQP9 is permeable to water and urea. Unlike AQP3 and AQP7, it did not facilitate glycerol transport. AQP families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic. A new member of the AQP family, AQP9, has been cloned from human leukocytes. It is homologous with AQP3 and AQP7 (54-48% identity). AQP9 (295aa) is primarily expressed in peripheral leukocytes, and in lesser amounts in liver, lung and spleen. AQP9 is permeable to water and urea. Unlike AQP3 and AQP7, it does not facilitate glycerol transport. AQP families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic.

Also known as:

Anti-AQP9抗体aquaporin Protein-9; Aquaporin 9; AQP 9; AQP9; Aquaporin9; HsT 17287; HsT17287; Small solute channel 1; SSC 1; SSC1; Aquaporin-9; AQP-9; Aquaglyceroporin-9; AQP9_HUMAN.

Specificity:

Storage:

Anti-AQP9抗体Shipped at 4℃, Store at -20℃ (Avoid repeated freeze/thaw cycles).

Application:

Anti-AQP9抗体WB=1:100-500  ELISA=1:500-1000  IHC-P=1:100-500  IHC-F=1:100-500  Flow-Cyt=1:50-300  ICC=1:100-500  IF=1:100-500   
Not yet tested in other applications. 
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