O0382
Anti-Opioid δ Receptor antibody produced in rabbit
whole antiserum, lyophilized powder
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About This Item
Prodotti consigliati
Origine biologica
rabbit
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
whole antiserum
Tipo di anticorpo
primary antibodies
Clone
polyclonal
Forma fisica
lyophilized powder
PM
antigen ~55 kDa
Reattività contro le specie
mouse (predicted), rat
tecniche
immunocytochemistry: 1:800 using PLP fixed rat brain sections
western blot: 1:800 using whole brain homogenate
N° accesso UniProt
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
Informazioni sul gene
mouse ... Oprd1(18386)
rat ... Oprd1(24613)
Descrizione generale
Opioid peptides are endogenous neuromodulators that play a major role in nociception by interacting with several membrane receptors. Molecular cloning techniques have characterized the nucleotide sequence of several distinct opioid receptors, including the δ-, κ- and μ-opioid receptors.1 The cloned receptors are highly homologous (65%), differing only at the N- and C-termini and at the extracelluar loops that confer binding specificity. All three receptors interact with heterotrimeric G proteins.
δ-Opioid receptors (DOR) are located postsynaptically on pallidostriatal feedback neurons. DORs also modulate nociception presynaptically in the periaqueductal gray where immunolabeling of DOR has been shown to be intracellular and often associated with large dense-core vesicles. Additionally, receptor autoradiographic investigations have localized DORs to the external plexiform layer of the olfactory bulb, the nucleus accumbens, several layers of the cerebral cortex and several nuclei of the amygdala.
References
1. Goldstein, A. Trends Pharmacol. Sci., 8, 456-459 (1987).
δ-Opioid receptors (DOR) are located postsynaptically on pallidostriatal feedback neurons. DORs also modulate nociception presynaptically in the periaqueductal gray where immunolabeling of DOR has been shown to be intracellular and often associated with large dense-core vesicles. Additionally, receptor autoradiographic investigations have localized DORs to the external plexiform layer of the olfactory bulb, the nucleus accumbens, several layers of the cerebral cortex and several nuclei of the amygdala.
References
1. Goldstein, A. Trends Pharmacol. Sci., 8, 456-459 (1987).
Specificità
The antiserum is specific for the COOH terminal of the opioid δ receptor.
Immunogeno
Peptide corresponding to the carboxy-terminal of the opioid δ receptor covalently attached onto a carrier protein.
Esclusione di responsabilità
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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Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
Certificati d'analisi (COA)
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
S R Childers
Life sciences, 48(21), 1991-2003 (1991-01-01)
Although pharmacological data provide strong evidence for different types of opioid receptors (e.g., mu, delta, and kappa), they share many common properties in their ability to couple to second messenger systems. All opioid receptor types are coupled to G-proteins, since
M F Olive et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 17(19), 7471-7479 (1997-09-20)
Parallel studies have demonstrated that enkephalin release from nerve terminals in the pallidum (globus pallidus and ventral pallidum) can be modulated by locally applied opioid drugs. To investigate further the mechanisms underlying these opioid effects, the present study examined the
The delta-opioid receptor: molecular pharmacology, signal transduction, and the determination of drug efficacy.
R M Quock et al.
Pharmacological reviews, 51(3), 503-532 (1999-09-02)
P A Zaki et al.
Annual review of pharmacology and toxicology, 36, 379-401 (1996-01-01)
Since the discovery of opioid receptors over two decades ago, an increasing body of work has emerged supporting the concept of multiple opioid receptors. Molecular cloning has identified three opioid receptor types--mu, delta, and kappa--confirming pharmacological studies that previously postulated
B L Kieffer
Cellular and molecular neurobiology, 15(6), 615-635 (1995-12-01)
1. Opioid peptides are a family of structurally related neuromodulators which play a major role in the control of nociceptive pathways. These peptides act through membrane receptors of the nervous system, defined as mu, delta and kappa and endowed with
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