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Anti-Human TRPM2 Polyclonal Antibody (HA519014)

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Overview
Catalog No.HA519014
Description
Anti-Human TRPM2 Polyclonal Antibody (HA519014) is a rabbit polyclonal antibody detecting TRPM2 in ELISA, IHC, WB. Suitable for Rattus norvegicus, Mus musculus, and Human.
Highlights
  • Affinity Purified — Minimal background and high purity for reliable results.
  • Multi-Application — Validated across multiple applications.
  • Multi-Species — Cross-reactive for translational research.
Species reactivityHuman, Mouse
ApplicationsELISA, IHC, WB
Host speciesRabbit
ClonalityPolyclonal
IsotypeIgG
Immunogen E. coli - derived recombinant Human TRPM2 (Lys140-Arg358).
Target TRPM2
Purification Purified by antigen affinity column.
Accession O94759
Form Liquid
Storage buffer 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Product Usage Information
Application Dilution
ELISA 1:5000-1:20000
IHC 1:50-1:500
WB 1:500-1:2000
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesTransient receptor potential cation channel subfamily M member 2, Estrogen-responsive element-associated gene 1 protein, Long transient receptor potential channel 2, LTrpC-2, LTrpC2, Transient receptor potential channel 7, TrpC7, Transient receptor potential melastatin 2, TRPM2, EREG1, KNP3, LTRPC2, TRPC7
Background

Transient receptor potential cation channel subfamily M member 2 (TRPM2) is a ~171 kDa protein. Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as a ligand-gated ion channel, gated by intracellular adenosine diphosphate ribose (ADP-ribose), Ca(2+), warm temperature, and oxidative stress. The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate. Binding of ADP-ribose to the cytoplasmic Nudix domain causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening. Extracellular Ca(2+) passes through the channel and increases channel activity.

1. Perraud, AL. et al. (2001) Nature 411, 595-9. PMID: 11385575
2. Sano, Y. et al. (2001) Science (New York, N.Y.) 293, 1327-30. PMID: 11509734
3. Hara, Y. et al. (2002) Molecular cell 9, 163-73. PMID: 11804595
4. Zhang, W. et al. (2003) The Journal of biological chemistry 278, 16222-9. PMID: 12594222
5. Perraud, AL. et al. (2005) The Journal of biological chemistry 280, 6138-48. PMID: 15561722
6. Togashi, K. et al. (2006) The EMBO journal 25, 1804-15. PMID: 16601673
7. Csanády, L. et al. (2009) The Journal of general physiology 133, 189-203. PMID: 19171771
8. Yang, W. et al. (2010) The Journal of biological chemistry 285, 30411-8. PMID: 20660597
9. Kühn, FJ. et al. (2015) Scientific reports 5, 8032. PMID: 25620041
10. Li, F. et al. (2016) Journal of cell science 129, 2016-29. PMID: 27068538
Note For research use only.
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
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Formula
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