AB3071
Anti-Aquaporin 0 Antibody
Chemicon®, from rabbit
Sinónimos:
AQP0, MIP, Major Intrinsic Protein
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Productos recomendados
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.
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
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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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
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Biochimica et biophysica acta, 1862(8), 1433-1442 (2016-05-08)
Major intrinsic protein (MIP) is a functional water-channel (AQP0) that also plays a key role in establishing lens fiber cell architecture. Genetic variants of MIP have been associated with inherited and age-related forms of cataract; however, the underlying pathogenic mechanisms
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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