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Aquaporin-2 (AQP2) (rat) antibody

$155.00$435.00

Item Cat No.: 20102rs

Antibody: Rat Aquaporin-2 (AQP2) polyclonal antibody

Concentration: 0.25 mg/ml purified IgG

Application: Validated by immunofluorescence labeling (1:100)

Reactivity: Human, Mouse, Rat

Anti-Aquaporin-2 (AQP2) antibody is validated on mouse tissue and recommended for immunofluorescence labeling, IHC, or western blot of materials from rodent and human tissues.

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Anti-Aquaporin-2 (AQP2) antibody is validated on mouse tissue and recommended for immunofluorescence labeling, IHC, or western blot of materials from rodent and human tissues.

Aquaporin, also known as water channel, mediates water permeation across the cell membrane. There are approximately 10 aquaporin genes in human genome. Aquaporin proteins are composed of six transmembrane domains, three extracellular loops, two intracellular loops and two intracellular termini.

Aquaporin-2 is encoded by the Aqp2 gene in human. Aquaporin-2 is highly expressed in the collecting duct epithelium of the kidney. Mutations in Aqp2 gene cause diabetes insipidus.

This antibody is raised in rat and particularly suited for use as a molecular marker to label the collecting duct cells in co-localization studies.

Host/Isotype: Rat/IgG

Class: Polyclonal

Immunogen: Synthetic peptide (17-aa) derived from the C-terminal region of human Aquaporin-2 protein

Species homology of immunogen: Synthetic peptide sequence is identical to mouse or rat sequence

Conjugation: Unconjugated

Storage buffer: PBS, pH 7.2, 0.1% sodium azide

Storage condition: –20°C


For Research Use Only. Not for use in clinical diagnostics.

Delineating cell lineage in the collecting duct of mouse kidney

Differentiating principal cell from intercalated cell Expand The collecting duct in the kidney consists in three types of cells, principal cells, alpha-intercalated cells and beta-intercalated cells. The principal cells are primarily responsible for salt and water transport while alpha- and beta-intercalated cells are responsible for acid-base transport. Figure legend Anti-Aqp2 antibody labels the luminal membrane […]

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Protocol for Staining Aquaporin

Materials and Reagents Expand Equipment Leica CM1950 automatic sectioning cryostat. Thermo Fisher Scientific round (12 mm diameter) cover glass (thickness No 1.5). Thermo Fisher Scientific ColorFrostTM Plus slides made of positively charge uncoated glass.   Tissue-tek Expand Tissue-tek OCT 4583 compound from VWR. Tissue-tek cryomolds from VWR. Fixation Buffers Expand 2% paraformaldehyde in PBS NaCl […]

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Be the first to review “Aquaporin-2 (AQP2) (rat) antibody”

"I am really impressed with your approach. We tried multiple times previously to create monoclonal and polyclonal antibodies to claudin-2 and MLCK1. We have had limited success generating polyclonals and no success generating monoclonals. You have generated outstanding monoclonals to both. I look forward to continuing to work with you."

Jerrold R. Turner, M.D., Ph.D.

Brigham and Women’s Hospital | Harvard Medical School

"The polyclonal antibody you generated for KIAA0408 is stunning! KIAA0408 is a novel cilium molecule that has never been studied. So, clearly there will be a lot of demand for it as we have discovered a very interesting finding and the story will be published in a high impact journal. I am strongly inclined to generate monoclonal antibody for this protein too and we should think about patenting it."

Univ.-Prof. Jay Gopalakrishnan PhD

Heinrich-Heine-Universität | Universitätsklinikum Düsseldorf

"Your ARL13B antibody works beautifully!!! We’re so happy to have a cilia-specific antibody made in rat! I can send you high resolution images to be posted on your website."

Julie Craft Van De Weghe, PhD

School of Medicine | University of Washington

"The assay is a homophilic interaction mediated cell adhesion on purified protein (in this case, immobilized purified Pcdhga9 to Pcdhga9 expressed on cell surface). Compared to control, cell adhesion is reduced in the presence of Pcdhga9 monoclonal antibody supernatants!"

Divyesh Joshi, PhD

School of Medicine | Yale University

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