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AB3071

Sigma-Aldrich

Anti-Aquaporin 0 Antibody

Chemicon®, from rabbit

Synonym(s):

AQP0, MIP, Major Intrinsic Protein

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

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)

Specificity

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.

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.

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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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Yichen Wang et al.
Investigative ophthalmology & visual science, 58(10), 3896-3922 (2017-08-02)
Previous research showed that the absence of β1-integrin from the mouse lens after embryonic day (E) 13.5 (β1MLR10) leads to the perinatal apoptosis of lens epithelial cells (LECs) resulting in severe microphthalmia. This study focuses on elucidating the molecular connections
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
Thuzar Thein et al.
Development (Cambridge, England), 143(21), 3994-4002 (2016-11-03)
Fibroblast growth factor (FGF) signaling is an essential regulator of lens epithelial cell proliferation and survival, as well as lens fiber cell differentiation. However, the identities of these FGF factors, their source tissue and the genes that regulate their synthesis
Julie M Hayes et al.
Molecular biology of the cell, 23(24), 4725-4738 (2012-10-26)
Lens fiber formation and morphogenesis requires a precise orchestration of cell- extracellular matrix (ECM) and cell-cell adhesive changes in order for a lens epithelial cell to adopt a lens fiber fate, morphology, and migratory ability. The cell-ECM interactions that mediate

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