PC421
Anti-Vanilloid Receptor Like Protein-1 (744-761) Rabbit pAb
Synonym(s):
Anti-TRPV2
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About This Item
antibody form
purified antibody
Quality Level
clone
polyclonal
form
liquid
contains
≤0.1% sodium azide as preservative (antibody only)
species reactivity
rat, mouse
isotype
IgG
General description
Purified rabbit polyclonal antibody. Recognizes the ~98 kDa vanilloid receptor like protein-1. Supplied with a lyophilized control peptide (100 μg size only).
Recognizes the ~98 kDa (doublet) vanilloid receptor like protein-1 in rat spinal cord extract. Supplied with a control peptide (100 μg size only).
The detection of noxious stimuli (chemical, mechanical, or thermal), a process referred to as nociception, occurs predominantly at the peripheral terminals of primary afferent neurons. This information is ultimately transmitted to the central nervous system to evoke a perception of pain which initiates appropriate protective reflexes. Vanilloid-containing compounds which include capsaicin, the active ingredient in hot chilli peppers, selectively depolarize nociceptors to activate the "nociceptive" pathway. The receptor for capsaicin, vanilloid receptor 1 (VR1), has been identified as a nonselective cation channel that resembles members of the transient receptor potential (TRP) family of ion channels. The vanilloid receptor 1 protein functions both as a receptor for capsaicin and a transducter of noxious thermal stimuli. Immunocytochemical and mRNA localization studies suggest that VR1 protein is localized to small-diameter sensory neurons within the dorsal root ganglia and nerve terminals in the dorsal horn. A capsaicin-receptor homolog has recently been identified, designated the vanilloid-receptor-like protein 1 (VRL-1). VRL-1 is activated by high temperatures and is expressed in medium- to large-diameter neurons within sensory ganglia.
Immunogen
a synthetic peptide (KNSASEEDHLPLQVLQSP) corresponding to amino acids 744-761 of rat vanilloid receptor like protein 1, conjugated to KLH
Application
Frozen Sections (1 μg/ml)
Immunoblotting (2 μg/ml, see application references)
Immunocytochemistry (2 μg/ml, see application references)
Immunoblotting (2 μg/ml, see application references)
Immunocytochemistry (2 μg/ml, see application references)
Physical form
100 μg antibody in 0.05 M sodium phosphate buffer, 0.2% gelatin and 25 μg lyophilized control peptide (immunogen) (100 μg size only).
Reconstitution
Reconstitute the control peptide with 25 μl dH₂O for a working stock of 1 mg/ml. Store lyophilized control peptide at -20°C. Following reconstitution of the control peptide, aliquot and freeze (-20°C).
Analysis Note
Positive Control
Rat or mouse spinal cord extract
Rat or mouse spinal cord extract
Other Notes
A protein database search confirms that this peptide sequence is unique to the Vanilloid-Receptor-Like Protein 1. No cross-reactivity with the capsaicin receptor protein is expected. This signal is completely abolished in immunoblotting by preincubating t
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G J Michael et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 19(5), 1844-1854 (1999-02-19)
Sensitivity to the pungent vanilloid, capsaicin, defines a subpopulation of primary sensory neurons that are mainly polymodal nociceptors. The recently cloned vanilloid receptor subtype 1 (VR1) is activated by capsaicin and noxious heat. Using combined in situ hybridization and histochemical
A Guo et al.
The European journal of neuroscience, 11(3), 946-958 (1999-04-02)
The vanilloid receptor (VR1) protein functions both as a receptor for capsaicin and a transducer of noxious thermal stimuli. To determine the expression and targetting of this protein, we have generated antisera against both the amino and carboxy termini of
S Bevan et al.
Trends in pharmacological sciences, 11(8), 330-333 (1990-08-01)
Capsaicin acts specifically on a subset of primary afferent sensory neurons to open cation-selective ion channels, probably by interacting directly with a membrane receptor-ion channel complex. Another plant product--resiniferatoxin--has structural similarities to capsaicin and opens the same channels, but is
Alexander J Stokes et al.
The Journal of experimental medicine, 200(2), 137-147 (2004-07-14)
Cutaneous mast cell responses to physical (thermal, mechanical, or osmotic) stimuli underlie the pathology of physical urticarias. In vitro experiments suggest that mast cells respond directly to these stimuli, implying that a signaling mechanism couples functional responses to physical inputs
A Szallasi
General pharmacology, 25(2), 223-243 (1994-03-01)
1. Capsaicin was postulated to exert its pharmacological actions by interacting at a specific recognition site (receptor) expressed predominantly by primary afferent neurons. 2. The actual existence of this long-sought "capsaicin-receptor" has recently been demonstrated by the specific binding of
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