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AB3075
Sigma-AldrichAnti-Aquaporin 7 Antibody
Detect Aquaporin 7 using this Anti-Aquaporin 7 Antibody validated for use in ELISA & WB.
More>>Detect Aquaporin 7 using this Anti-Aquaporin 7 Antibody validated for use in ELISA & WB. Less<<
Anti-Aquaporin 7 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
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. Aquaporin-7 (rAQP7, 269aa) is abundantly expressed in testis. It is involved in water, glycerol and urea transport. Aquaporin-7 is also found in adipose tissue, kidney, and heart. Aquaporin-7 has been localized to in the spermatids and at maturing sperms. Aquaporin families of proteins are predicted to contain six transmembrane domains. The N and C-terminus are predicted to be cytoplasmic.
References
Product Information
Format
Affinity Purified
Presentation
Affinity Purified 1 mg/ml soln in PBS, pH 7.5 and 0.1% BSA and 0.05% sodium azide
Detect Aquaporin 7 using this Anti-Aquaporin 7 Antibody validated for use in ELISA & WB.
Key Applications
ELISA
Western Blotting
Application Notes
Note: We recommend the use of 0.5-1.0% milk in all primary/secondary antibody incubations to suppress non-specific reactivity.
Western blot: 1-10 μg/mL using Chemiluminescence technique
ELISA: 0.5-1.0 μg/mL when tested against 1 μg/mL of the immunogen peptide.
Immunohistochemistry: We recommend using the affinity purified antibody at 2-10 μg/mL in paraformaldehyde fixed sections of tissues.
Optimal working dilutions must be determined by end user.
Biological Information
Immunogen
An 18 AA synthetic peptide within the N-terminal domain of rat Aquaporin-7 (Ishibashi et al. 1997) was selected for antibody production. This domain is predicted to be cytoplasmic.
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
Aquaporin 7. The immunogen peptide is unique to Aquaporin-7 without significant homology to any other Aquaporins.
Species Reactivity
Rat
Species Reactivity Note
The peptide has 81% similarity with the mouse Aquaporin-7
Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin 7 facilitates water, glycerol and urea transport. It may play an important role in sperm function.
FUNCTION: SwissProt: O14520 # Forms a channel for water and glycerol. SIZE: 342 amino acids; 37232 Da SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. DOMAIN: SwissProt: O14520 Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Ala-Ala/Ser (NPA). SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Maintain frozen at -20°C in undiluted aliquots for up to 6 months after date of receipt.
Aquaporin expression is downregulated in a murine model of colitis and in patients with ulcerative colitis, Crohn's disease and infectious colitis. J A Hardin, L E Wallace, J F K Wong, Cell and tissue research
318
313-23
2004
Colitis is associated with alterations in electrolyte and water transport. These changes give rise to some of the symptoms experienced by patients with colitis. Alterations in fluid flux may also contribute to increased susceptibility to mucosal injury. Recently, endogenous water channel proteins (aquaporins; AQPs), have been identified in colonic tissue. The expression of AQP4, AQP7 and AQP8 was examined, via reverse transcription/polymerase chain reaction, Western blotting and immunohistochemistry, in a murine model of colitis and in patients with inflammatory bowel disease or infectious colitis. Colitis was induced in C57BL/6 mice by the addition of 2.5% dextran sodium sulphate (DSS) to their drinking water. AQP expression in these mice was assessed following 12 h to 7 days of DSS exposure and during the recovery phase from 1 to 15 days following cessation of DSS exposure. Colonic water transport was measured after 1 and 3 days of DSS and following 7 days of recovery. The expression of AQP4 and AQP8 mRNA was significantly decreased after 12-24 h of DSS exposure and remained depressed throughout the treatment period. Expression of AQP7 was more variable. Protein expression followed a similar pattern to that observed for AQP mRNA. Significant alteration in colonic fluid secretion was correlated with reduced expression of AQP isoforms. Significantly, patients with active ulcerative colonic, Crohn's colitis or infectious colitis had similar dramatic reductions in AQP expression that appeared to be correlated with disease activity. Thus, colonic injury in both mouse and man is associated with a downregulation in AQP expression.
