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>   home   >   Products   >   Primary Antibodies   >   TRPM6 (extracellular) Antibody   

TRPM6 (extracellular) Antibody

Affinity purified polyclonal antibody

  • WB - TRPM6 (extracellular) Antibody AG1342-025
    Western blot analysis of rat kidney (lanes 1 and 4), rat testis (lanes 2 and 5) and mouse kidney (lanes 3 and 6) lysates: 1-3. Anti-TRPM6 (extracellular) antibody (#AG1342), (1:200).
    4-6. Anti-TRPM6 (extracellular) antibody, preincubated with the control peptide antigen.
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession Q8CIR4
Reactivity Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 232888 Da
Homology Rat - 13/14 amino acid residues identical; human - 11/14 amino acid residues identical.
Additional Information
Gene ID 225997
Other Names Transient receptor potential cation channel subfamily M member 6, Channel kinase 2, Melastatin-related TRP cation channel 6, Trpm6
Related products for control experimentsControl peptide antigen (supplied with the antibody free of charge).
Target/Specificity Peptide CVKDYDLERGPDEK, corresponding to amino acid residues 802-815 of mouse TRPM6 (Accession Q8CIR4). 1st extracellular loop.
Dilution WB~~1:200-1:2000
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 0.9 mg/ml.
Buffer After Reconstitution Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.
Storage Before ReconstitutionLyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
Storage After ReconstitutionThe 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 ReconstitutionLyophilized 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.
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Transient receptor potential (TRP) channels are relatively non-selective ion channels enabling the exchange of cations down their electrochemical gradient. This exchange enables the intracellular rise in Na+ and Ca2+ concentration and ultimately in the cell membrane depolarization, important for action potential propagation and muscle contraction1. They are activated by an extremely broad range of stimuli namely, temperature, voltage, pH, endocrine factors as well as signaling molecules2. The TRP channel family is composed of 28 members divided in 7 subgroups: TRPV, TRPC, TRPM, TRPA, TRPN, TRPP and TRPML. All members of the TRP family have 6 transmembrane (TM) domains, and a pore domain between the fifth (S5) and sixth (S6) transmembrane domains. In general, TRP channels enable the passage of either Na+ or Ca2+ ions with little or no preference. However, some channels do exhibit some selectivity. Also, TRP channels do not display the positive charges in the S4 voltage-sensing domain like most voltage sensitive channels, although they do display voltage dependency3. In addition, TRP channels have in the C-terminal intracellular region to the S6 domain a TRP domain comprising 25 amino acids that is more or less conserved among most TRP channels. Within the TRP domain, there is a TRP box composed of six amino acids, and TRP box 2 – a proline rich domain1,3. The TRP domain seems to be responsible for the binding of PIP2, a phospholipid important for the regulation of channel activity4. The TRPM subfamily consists of 8 members divided in to three major groups: TRPM1/3, TRPM4/5, and TRPM6/7. TRPM2 and TRPM8 are not included in any of the groups since they are quite different even with respect to each other. TRPM2, TRPM6 and TRPM7 are distinctly different from the other TRP channels and other ion channels as all three have an active kinase domain in the C-terminal tail. TRPM6 kinase domain is able to phosphorylate TRPM7 thus increasing TRPM7 channel activity. However, TRPM7 cannot phosphorylate TRPM65; it can though autophosphorylate and phosphorylate other proteins1,6. The significance of the kinase activity of these two channels has yet to be determined. Both channels are regulated by cytosolic Mg2+. Extracellular Mg2+ inhibits the channels. Both TRPM6 and TRPM7 are thus important regulators of Mg2+ homeostasis7. TRPM7 does so in a more or less ubiquitous manner whereas TRPM6 does so selectively in the kidney and intestines where it is selectively expressed. Indeed, mutations in TRPM6 results in hypomagnesemia with secondary hypocalcemia8-10. TRPM6 and TRPM7 are able to form homo- and heterodimers, where every channel-type formed demonstrates different properties related to cation affinity, and pH sensitivity7.  Abgent is pleased to offer a highly specific antibody directed against an the 1st extracellular loop of mouse TRPM6. Anti-TRPM6 (extracellular) antibody (#AG1342) can be used in western blot analysis, and has been designed to recognize TRPM6 from mouse, rat and human samples.


References 1. Ramsey, S.I. et al. (2006) Annu. Rev. Physiol. 68, 619. 2. Pedersen, S.F. et al. (2005) Cell Calcium 38, 233. 3. Montell, C. (2005) Sci. STKE 2005, re3. 4. Hilgemann, D.W. et al. (2001) Sci. STKE 2001, re19. 5. Schmitz, C. et al. (2005) J. Biol. Chem. 280, 37763. 6. Matsushita, M. et al. (2005) J. Biol. Chem. 280, 20793. 7. Touyz, R.M. (2008) Am. J. Physiol. 294, H1103. 8. Venkatachalam, K. and Montell, C. (2007) Annu. Rev. Biochem. 76, 387. 9. Walder, R.Y. et al. (2002) Nat. Genet. 31, 171. 10. Schlingmann, K.P. et al. (2002) Nat. Genet. 31, 166.

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Cat# AG1342-025
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