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> Anti-Aquaporin 2 (Ser269) Antibody

Anti-Aquaporin 2 (Ser269) Antibody

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Referência p112-269

Tamanho : 100uL

Marca : Phosphosolutions

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Anti-Aquaporin 2 (Ser269) Antibody

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Our Anti-Aquaporin 2 (Ser269) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat Aquaporin 2 (Ser269) and is antigen affinity purified from pooled serum. It is great for use in WB, IHC, ICC, IP.

Immunolabeling of vasopressin treated mouse kidney (inner medulla) showing specific labeling of the AQP2 protein phosphorylated at Ser269 (Cat. No. p112-269, red, 1:1000). Nuclei labeled with DAPI. Magnification 10x. Image kindly provided by Juan Pablo Arroyo Ornelas, Vanderbilt University.
Immunolabeling of vasopressin treated mouse kidney (inner medulla) showing specific labeling of the AQP2 protein phosphorylated at Ser269 (Cat. No. p112-269, red, 1:1000) and total AQP2 (green). Nuclei labeled with DAPI. Magnification 600x. Image kindly provided by Juan Pablo Arroyo Ornelas, Vanderbilt University.
Western blot of rat kidney lysate showing specific immunolabeling of the ~29 kDa and 37 kDa glycosylated form of the AQP2 protein phosphorylated at Ser269 in the vasopressin (AVP) treated lane (+), but not in the control lane (-).
Western analysis of rat kidney inner medullary (IM) lysate from ddAVP and ddAVP + ADM-treated IM probed for total (bottom) and pSer269 (cat. p112-269, 1:1000)(top) AQP2. Brackets indicate the glycosylated AQP2 protein between 35 and 45 kDa, and the arrow indicates the un glycosylated AQP2 protein at 29 kDa. The matched pair comparisons were achieved by comparing Lane 1 with Lane 5; Lane 2 with Lane 6; Lane 3 with Lane 7; and Lane 4 with Lane 8. Image from publication CC-BY-4.0. PMID: 37047509
Immunolabeling of vasopressin treated mouse kidney (inner medulla) showing specific labeling of the AQP2 protein phosphorylated at Ser269 (Cat. No. p112-269, red, 1:1000). Nuclei labeled with DAPI. Magnification 10x. Image kindly provided by Juan Pablo Arroyo Ornelas, Vanderbilt University.

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