|Application ||WB, IP|
|Calculated MW||86706 Da|
|Other Names||Transient receptor potential cation channel subfamily V member 2, TrpV2, Osm-9-like TRP channel 2, OTRPC2, Stretch-activated channel 2B, Vanilloid receptor-like protein 1, VRL-1, Trpv2, Sac2b, Vrl1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)KKNPTSKPGKNSASEE, corresponding to amino acid residues 735-750 of rat TRPV2 (Accession Q9WUD2).ֲ Intracellular, C-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||0.65 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|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||2 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
TRP channels are a large family (about 28 genes) of plasma membrane, non-selective cationic channels that are either specifically or ubiquitously expressed in excitable and non-excitable cells.1 The TRP channels have putative six-transmembrane domains (TM) with a pore domain between the fifth and the sixth TM, and all assemble as tetramers. Both the N- and the C-terminus of all TRPs are intracellular.3 According to IUPHAR, the TRP family is comprised of three main subfamilies on the basis of sequence homology; TRPC, TRPM and TRPV (to date, three additional subfamilies are also considered to belong to the TRP family: the TRPA, TRPML, and TRPP).1-4 The TRPV subfamily consists of six members, TRPV1-6.5 Four members of the TRPV family have been described as a thermosensitive ion channels (TRPV1 to TRPV4). Each channel exhibits distinct thermal activation thresholds ranging from noxious cold (<17°C) to noxious heat (>52°C).6,7 Although it shares around 50% homology with TRPV1, TRPV2 is not activated by capsaicin nor by protons. It has a high temperature threshold of ~52°C and is considered to play an essential role in the perception of high-intensity noxious heat stimulation.8-10 The TRPV2 is also considered to be a stretch-activated channel and to play a role in skeletal and cardiac muscle degeneration and pain pathway.8 TRPV2 channel is expressed in DRG neurons, different brain region and non-neuronal tissues such as spleen, lung and, intestine and in component of the immune system.5,11-12 Abgent is pleased to release two novel antibodies to both intracellular TRPV2 and extracellular TRPV2, Anti-TRPV2 (#AG1350) and Anti-TRPV2 (extracellular) (#ACC-039) respectively.
References 1. Pan, J.P. et al. (2011) Brain Res. 412, 18. 2. Peng, G. et al. (2010) Am. J. Physiol. 299, L621. 3. Montell, C. et al. (2002) Mol. Cell. 9, 229. 4. Clapham, D.E. (2003) Nature 426, 517. 5. Moran, M.M. et al. (2004) Curr.Opin.Neurobiol. 14, 362. 6. Clapham, D.E. et al. (2003) Pharmacol. Rev. 55, 591. 7. Gunthorpe, M.J.et al. (2002) Trends. Pharmacol. Sci. 23, 183. 8. Tominaga, M. and Caterina, M.J. (2004) J.Neurobiol. 61, 3. 9. Voets, T. et al. (2004) Nature 430, 748. 10. Pedersen, S.F. et al. (2005) Cell Calcium 38, 233. 11. Muraki, K. et al. (2003) Circ. Res. 93, 829. 12. Shimosato, G. et al. (2005) Pain 119, 225. 13. Saunders, C.I. et al. (2007) Mol. Immunol. 44, 1429. 14. Caterina, M.J. et al. (1999) Nature 398, 436.
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