|Calculated MW||28882 Da|
|Homology||Mouse -15/18 amino acid residues identical; human -11/18 amino acid residues identical.|
|Other Names||Aquaporin-7, AQP-7, Aquaglyceroporin-7, Aqp7|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide corresponding to amino acidֲ residues 7-24 of rat AQP-7 (Accession number P56403). Intracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
|Formulation||Lyophilized powder. Phosphate buffered saline (PBS), pH 7.4, 0.025% NaN3.|
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Provided below are standard protocols that you may find useful for product applications.
Aquaporin 7 (AQP-7) belongs to a family of membrane proteins that allow passage of water and certain other solutes through biological membranes. The family is composed of 13 members (AQP-0 to AQP-12). Little is known about the function of the two newest members, AQP-11 and AQP-12. The aquaporins can be divided into two functional groups based on their permeability characteristics: the aquaporins that are only permeated by water and the aquaglyceroporins that are permeated by water and other small solutes such as glycerol. This last group includes AQP-7, AQP-3, AQP-9 and AQP-10. The proteins present a conserved structure of six transmembrane domains with intracellular N- and C-termini. The functional channel is a tetramer but each subunit has a separate pore and therefore the functional channel unit, contains four pores. AQP-7 is expressed in ovary, testis, kidney and adipose tissue. The function of AQP-7 in adipose tissue attracted much interest as mice deficient in AQP-7 developed adult-onset obesity and type 2 diabetes. AQP-7 modulates adipocyte glycerol permeability thereby controlling triglyceride accumulation and fat cell size
References 1. Kuriyama, H. et al. (1997) Biochem. Biophys. Res. Commun. 241, 53. 2. King, L.S. et al. (2004) Nat. Rev. Mol. Cell Biol. 5, 687. 3. Fruhbeck, G. et al. (2006) Trends Pharmacol. Sci. 27, 345.
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