磷酸化水通道蛋白2抗体

?磷酸化水通道蛋白2抗体Quantity size:

0.1ml

Concentration:

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

Background:

Aquaporins (AQPs) are a large family of integral membrane water transport channel proteins that facilitate the transport of water through the cell membrane. This function is conserved in animals,磷酸化水通道蛋白2抗体 plants and bacteria. Many isoforms of aquaporin have been identified in mammals, designated AQP0 through AQP10. Aquaporins are widely distributed and it is not uncommon for more than one type of AQP to be present in the same cell. Although most aquaporins are only permeable to water, AQP3, AQP7,磷酸化水通道蛋白2抗体 AQP9 and one of the two AQP10 transcripts are also permeable to urea and glycerol. AQP2 is the only water channel that is activated by vasopressin to enhance water reabsorption in the kidney collecting duct. Aquaporins are involved in renal water absorption, generation of pulmonary secretions, lacrimation, and the secretion and reabsorption of cerebrospinal fluid and aqueous humor.

磷酸化水通道蛋白2抗体Also known as:

Aquaporin 2 (phospho S256); Aquaporin 2 (phospho Ser256); p-Aquaporin 2 (phospho S256); p-Aquaporin 2 (S256); ADH water channel; AQP 2; AQP CD; AQP2; AQPCD; Aquaporin 2 collecting duct; Aquaporin CD; Aquaporin2; Aquaporine 2; Collecting duct water channel protein; MGC34501; Water channel protein for renal collecting duct; WCH CD; WCHCD; AQP2_HUMAN.

Specificity:

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Rabbit Polyclonal IgG, affinity purified by Protein A.

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Reacts with: Human, Mouse, Rat, Chicken, Dog, Pig, Cow, Horse, Rabbit, Monkey, .

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Immunogen: KLH conjugated synthesised phosphopeptide derived from human AQP2 around the phosphorylation site of Ser256.

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Predicted Molecular Weight: 29kDa.

磷酸化水通道蛋白2抗体Storage:

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

Application:

WB=1:100-500  ELISA=1:500-1000  IHC-P=1:100-500  IHC-F=1:100-500  ICC=1:100-500  IF=1:100-500   
Not yet tested in other applications. 
Optimal working dilutions must be determined by the end user.

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