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V2764

Sigma-Aldrich

Anti-Vanilloid Receptor-1 antibody produced in rabbit

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-TRPV1, Anti-VR-1

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About This Item

MDL number:
MFCD02686673
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 90 kDa

species reactivity

rat

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

technique(s)

microarray: suitable
western blot: 1:1,000 using whole cell extract of 293T cells expressing rat VR-1

UniProt accession no.

O35433

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TRPV1(7442)

Related Categories

General description

Vanilloid Receptor-1 (VR-1) is a cation channel protein that stimulates a burning pain sensation upon binding to capsaicin, a component of ′hot′ chilli peppers. VR-1 is also activated by noxious heat stimuli. Moreover, VR-1 can combine both, heat and chemical stimuli to cause a sensation of pain in vivo.

Specificity

Anti-Vanilloid Receptor-1 antibody is specific for vanilloid receptor-1 (90 kDa) in rats. The vanilloid receptor-1 immunizing peptide (rat, amino acids 817-838) specifically inhibits the staining of the vanilloid receptor-1 band in immunoblotting.

Immunogen

synthetic peptide corresponding to the C-terminus of rat vanilloid receptor-1 (amino acids 817-838) conjugated to KLH. The sequence is highly conserved in guinea pig (~85% identity) and human (~70% identity) and is not found in rat VRL-1.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Elvira Varela-López et al.
Oxidative medicine and cellular longevity, 2021, 8531975-8531975 (2021-08-17)
The potential transient vanilloid receptor type 1 (TRPV1) plays important functional roles in the vascular system. In the present study, we explored the role of the TRPV1 in the production of nitric oxide (NO), biopterines (BH4 and BH2), cyclic guanosine
M Tominaga et al.
Neuron, 21(3), 531-543 (1998-10-13)
Capsaicin, the main pungent ingredient in "hot" chili peppers, elicits buming pain by activating specific (vanilloid) receptors on sensory nerve endings. The cloned vanilloid receptor (VR1) is a cation channel that is also activated by noxious heat. Here, analysis of
Amanda Jabin Fågelskiöld et al.
Islets, 4(1), 56-63 (2012-01-26)
We have studied whether functional TRPV1 channels exist in the INS-1E cells, a cell type used as a model for β-cells, and in primary β-cells from rat and human. The effects of the TRPV1 agonists capsaicin and AM404 on the
M J Caterina et al.
Nature, 389(6653), 816-824 (1997-12-31)
Capsaicin, the main pungent ingredient in 'hot' chilli peppers, elicits a sensation of burning pain by selectively activating sensory neurons that convey information about noxious stimuli to the central nervous system. We have used an expression cloning strategy based on
Simon Desiderio et al.
eLife, 12 (2024-02-22)
Touch sensation is primarily encoded by mechanoreceptors, called low-threshold mechanoreceptors (LTMRs), with their cell bodies in the dorsal root ganglia. Because of their great diversity in terms of molecular signature, terminal endings morphology, and electrophysiological properties, mirroring the complexity of
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