Anti-TRPV2 (VRL1) (extracellular) Antibody

Transient receptor potential cation channel subfamily V member 2, Vanilloid receptor-like protein 1, VRL-1, Osm-9-like TRP channel 2, OTRPC2, Stretch-activated channel 2B, SAC2B
    Cat #: ACC-039
    Alternative Name Transient receptor potential cation channel subfamily V member 2, Vanilloid receptor-like protein 1, VRL-1, Osm-9-like TRP channel 2, OTRPC2, Stretch-activated channel 2B, SAC2B
  • Lyophilized Powder
  • Antigen Incl.
  • Type: Polyclonal
    Host: Rabbit
    Reactivity: m, r
    • Peptide (C)HQPSLDQPAIPSSKAT, corresponding to amino acid residues 413-428 of rat TRPV2 (Accession Q9WUD2). 1st extracellular loop.
    • Anti-TRPV2 (VRL1) (extracellular) Antibody
    Accession (Uniprot) Number Q9WUD2
    Gene ID 29465
    Peptide confirmation Confirmed by amino acid analysis and mass spectrometry.
    Homology Mouse - 15/16 amino acid residues identical.
    RRID AB_2040268.
    Purity Affinity purified on immobilized antigen.
    Form Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.
    Isotype Rabbit IgG.
    Storage before reconstitution The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C.
    Reconstitution 25 μl, 50 μl or 0.2 ml double distilled water (DDW), depending on the sample size.
    Antibody concentration after reconstitution 0.6 mg/ml.
    Storage after reconstitution The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing. Centrifuge all antibody preparations before use (10000 x g 5 min).
    Negative control antigen storage before reconstitution Lyophilized powder can be stored intact at room temperature for 2 weeks. For longer periods, it should be stored at -20°C.
    Negative control antigen reconstitution 100 µl double distilled water (DDW).
    Negative control antigen storage after reconstitution -20°C.
    Preadsorption Control 1 μg peptide per 1 μg antibody.
    Standard quality control of each lot Western blot analysis.
    Applications: ic, if, ifc, ih, ip, lci, wb
    Western blot
    • Anti-TRPV2 (VRL1) (extracellular) Antibody
      Western blot analysis of ND7/23 cell line membrane (lanes 1 and 3), RBL lysates (lanes 2 and 4) and rat brain membrane (lanes 5 6):
      1,2,5. Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039), (1:200).
      3,4,6. Anti-TRPV2 (VRL1) (extracellular) Antibody, preincubated with the negative control antigen.
    • Anti-TRPV2 (VRL1) (extracellular) Antibody
      Immunoprecipitation of rat basophilic leukemia (RBL) cell lysate:
      1. RBL lysate.
      2. Lysate immunoprecipitated with Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039), (6 µg).
      3. Lysate immunoprecipitated with pre-immune rabbit serum. The upper arrow indicates TRPV2 while the lower arrow indicates the IgG heavy chain. Western blot analysis was performed with Anti-TRPV2 (VRL1) (extracellular) Antibody.
    • Anti-TRPV2 (VRL1) (extracellular) Antibody
      Expression of TRPV2 in mouse DRG
      Immunohistochemical staining of TRPV2 in mouse dorsal root ganglion (DRG) using Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039).  A. TRPV2 (green) appears in patches along the perimeter of the DRG (arrows). B. Neurons containing neurofilament 200 (red) are scattered in the DRG, also in patches (arrows). C. A merge of the two panels shows that the spatial distribution of neurofilament 200 and TRPV2 expression overlaps. However, DRGs showing robust expression of neurofilament 200 do not contain TRPV2.
    Indirect flow cytometry
    • Anti-TRPV2 (VRL1) (extracellular) Antibody
      Cell surface detection of TRPV2 in intact living RBL cells:
      ___ Unstained cells.
      ___ Cells + Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039).
    Live cell imaging / Immunocytochemistry
    • Anti-TRPV2 (VRL1) (extracellular) Antibody
      Expression of TRPV2 in RBL cells
      Cell surface detection of TRPV2 in intact living rat basophilic leukemia (RBL) cells with Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039), (1:100), followed by goat anti-rabbit-AlexaFluor-550 secondary antibody (red), (x100).
    1. Montell, C. et al. (2002) Mol. Cell 9, 229.
    2. Clapham, D.E. (2003) Nature 426, 517
    3. Moran, M.M. et al. (2004) Curr. Opin. Neurobiol. 14, 362.
    4. Clapham, D.E. et al. (2003) Pharmacol. Rev. 55, 591.
    5. Gunthorpe, M.J. et al. (2002) Trends Pharmacol. Sci. 23, 183.
    6. Tominaga, M. and Caterina, M.J. et al. (2004) J. Neurobiol. 61, 3.
    7. Voets, T. et al. (2004) Nature 430, 748.
    8. Pedersen, S.F. et al. (2005) Cell Calcium 38, 233.
    9. Muraki, K. et al. (2003) Circ. Res. 93, 829.
    10. Shimosato, G. et al. (2005) Pain 119, 225.
    11. Saunders, C.I. et al. (2007) Mol. Immunol. 44, 1429.
    12. Caterina, M.J. et al. (1999) Nature 398, 436.
    Scientific background

    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 six putative 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-termini of all TRPs are intracellular3.

    According to IUPHAR, the TRP family is comprised of numerous subfamilies on the basis of sequence homology; TRPC, TRPM, TRPV, TRPA, TRPML, and TRPP1-4. The TRPV subfamily consists of six members, TRPV1-65.

    Four members of the TRPV family have been described as 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 stimulation8-10. TRPV2 is also considered to be a stretch-activated channel and to play a role in skeletal and cardiac muscle degeneration and pain pathway8. The TRPV2 channel is expressed in DRG neurons, different brain regions and non-neuronal tissues such as the spleen, lung and intestine and in components of the immune system5,11,12.

    Application key:

    CBE- Cell-based ELISA, FC- Flow cytometry, ICC- Immunocytochemistry, IE- Indirect ELISA, IF- Immunofluorescence, IFC- Indirect flow cytometry, IHC- Immunohistochemistry, IP- Immunoprecipitation, LCI- Live cell imaging, N- Neutralization, WB- Western blot

    Species reactivity key:

    H- Human, M- Mouse, R- Rat
    Image & Title: Anti-TRPV2 (VRL1) (extracellular) AntibodyExpression of TRPV2 in mouse cardiomyocytes.Immunocytochemical staining of mouse cardiomyocytes. Staining of cells using Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039) (green) shows that TRPV2 is translocated to the sarcolemma along the T-tubules in cardiomyocytes from DMD mice (lower left panel).Adapted from Lorin, C. et al. (2015) with permission of European Society of Cardiology.
    Last update: 02/02/2020

    Anti-TRPV2 (VRL1) (extracellular) Antibody (#ACC-039) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot, immunoprecipitation, immunohistochemistry, live cell imaging, and indirect flow cytometry applications. It has been designed to recognize TRPV2 from mouse and rat samples.

    For research purposes only, not for human use



    Scientific Background


    Western blot citations
    1. Rat astrocyte lysates.
      Zhang, H. et al. (2016) Eur. J. Neurosci. 44, 2493.
    2. Mouse cardiomyocyte lysates (1:200).
      Lorin, C. et al. (2015) Cardiovasc. Res. 106, 153.
    Immunohistochemistry citations
    1. Rat brain sections.
      Zhang, H. et al. (2016) Eur. J. Neurosci. 44, 2493.
    Immunocytochemistry citations
    1. Rat astrocytes.
      Zhang, H. et al. (2016) Eur. J. Neurosci. 44, 2493.
    2. Mouse cardiomyocytes (1:100).
      Lorin, C. et al. (2015) Cardiovasc. Res. 106, 153.
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