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Merck

AB3071

Anti-Aquaporin 0 Antibody

Chemicon®, from rabbit

Sinónimos:

AQP0, MIP, Major Intrinsic Protein

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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA, WB
Citations:
18
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biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable, western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... MIP(4284)

Immunogen

A 17 AA synthetic peptide within the carboxy terminal domain of human Aquaporin-0 (Shiels et al. 1988; Kent et al. 1990; Pisano et al. 1991; Shiels et al. 1996) was selected for antibody production. This domain is predicted to be cytoplasmic.

Application

Detect Aquaporin 0 using this Anti-Aquaporin 0 Antibody validated for use in ELISA & WB.
We recommend the use of 0.5-1% milk in all primary/secondary dilutions in order to suppress non-specific bands.

Western blot: 1-10 μg/mL using Chemiluminescence technique

ELISA: 0.5-1.0 μg/mL

Optimal working dilutions must be determined by end user.

Biochem/physiol Actions

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". Over the last decade, genes for several members of aquaporin family have been cloned, expressed, and their distribution studied in many tissues. Aquaporin-0 or MIP26 (major intrinsic protein 26 kDa), and Aquaporin-1 (purified from red cells) also called CHIP-28 (channel forming integral protein, 28 kDa; 268 AA; gene locus 7p14) has been the foundation of the growing family of aquaporins. The lens specific Aquaporin-0 represents up to 80% of total lens membrane protein. Defects in MIP26 are a cause of autosomal dominant cataract. The cataract Fraser mutation (CAT-FR or Shriveled) is a transposon-induced splicing error that substitutes a long terminal repeat sequence for the c-terminus of MIP. The lens opacity mutation (LOP) is an AA substitution that inhibits targeting of MIP to the cell membrane. Human Aquaporin-0 is a 263 amino acid transmembrane protein belonging to the MIP family. Aquaporin families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany


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Clase de almacenamiento

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable



Certificados de análisis (COA)

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Yuefang Zhou et al.
Differentiation; research in biological diversity, 102, 1-9 (2018-05-26)
Ephrin type-A receptor 2 (EPHA2) and one of its ligands, ephrin-A5 (EFNA5), have been associated with loss of eye lens transparency, or cataract, - an important cause of visual impairment. Here we show that mice functionally lacking EPHA2 (Epha2-null), EFNA5
Mallika Pathania et al.
TheScientificWorldJournal, 2014, 524929-524929 (2014-02-15)
We report analysis of the ocular lens phenotype of the recessive, larval lethal zebrafish mutant, lama1 (a69/a69). Previous work revealed that this mutant has a shortened body axis and eye defects including a defective hyaloid vasculature, focal corneal dysplasia, and
Thomas M Bennett et al.
Biochemical and biophysical research communications, 478(2), 988-993 (2016-08-16)
Major intrinsic protein or aquaporin-0 (MIP/AQP0) functions as a water channel and a cell-junction molecule in the vertebrate eye lens. Loss of MIP function in the lens leads to degraded optical quality and cataract formation by pathogenic mechanisms that are



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SKUGTIN
AB307104053252674815