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Merck

O0382

Sigma-Aldrich

Anti-Opioid δ Receptor antibody produced in rabbit

whole antiserum, lyophilized powder

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

whole antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

lyophilized powder

Mol-Gew.

antigen ~55 kDa

Speziesreaktivität

mouse (predicted), rat

Methode(n)

immunocytochemistry: 1:800 using PLP fixed rat brain sections
western blot: 1:800 using whole brain homogenate

UniProt-Hinterlegungsnummer

Versandbedingung

wet ice

Lagertemp.

−20°C

Angaben zum Gen

mouse ... Oprd1(18386)
rat ... Oprd1(24613)

Allgemeine Beschreibung

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).

Spezifität

The antiserum is specific for the COOH terminal of the opioid δ receptor.

Immunogen

Peptide corresponding to the carboxy-terminal of the opioid δ receptor covalently attached onto a carrier protein.

Haftungsausschluss

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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Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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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