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D2194

Sigma-Aldrich

Anti-Derlin-3 antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-DERL3, Anti-Der1-like domain family, member 3

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

200

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen ~26 kDa

Reattività contro le specie

rat (predicted), human, mouse (predicted)

Concentrazione

~1 mg/mL

tecniche

immunoprecipitation (IP): 5-10 μg using extract of HEK-293T cells expressing recombinant human Derlin-3
indirect immunofluorescence: 10-20 μg/mL using human HeLa cells
western blot: 2-5 μg/mL using whole extract of HEK-293T cells expressing recombinant human Derlin-3

N° accesso UniProt

Q96Q80

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... DERL3(91319)
mouse ... Derl3(70377)
rat ... Derl3(690315)

Descrizione generale

Derlin-3 is a mammalian homologues of yeast Der1p, a transmembrane protein required for yeast endoplasmic reticulum (ER)-associated degradation (ERAD). Derlin 3 is encoded by the gene mapped to human chromosome 22q11.23. It is expressed in the ER and is a member of the derlin protein family.

Immunogeno

synthetic peptide corresponding to amino acid residues 192-205 of human Derlin-3, conjugated to KLH. The corresponding sequence differs by 3 amino acids in mouse and 2 amino acids in rat.

Applicazioni

Anti-Derlin-3 antibody produced in rabbit has been used in immunoblotting, immunoprecipitation, and immunofluorescence.

Azioni biochim/fisiol

Derlin-3 is involved in the degradation of misfolded glycoproteins in the ER. Derlin-3 shares ~30% sequence identity with Derlin-1 and spans the lipid bilayer of the ER four times, showing structural similarity to Derlin-1. It is a component of the mammalian ER-associated degradation (ERAD) mechanism and is upregulated by unfolded protein response (UPR). Overexpression of this gene leads to increase in degradation of misfolded glycoprotein, whereas its knockdown blocks degradation. Derlin-3 also interacts with the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex.

Stato fisico

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

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

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificati d'analisi (COA)

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Overexpression of Derlin 3 is associated with malignant phenotype of breast cancer cells
Shibata M, et al.
Oncology Reports, 38(3), 1760-1766 (2017)
Peter J Belmont et al.
Circulation research, 106(2), 307-316 (2009-11-27)
Stresses, such as ischemia, impair folding of nascent proteins in the rough endoplasmic reticulum (ER), activating the unfolded protein response, which restores efficient ER protein folding, thus leading to protection from stress. In part, the unfolded protein response alleviates ER
Brendan N Lilley et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(40), 14296-14301 (2005-09-28)
Polypeptides that fail to pass quality control in the endoplasmic reticulum (ER) are dislocated from the ER membrane to the cytosol where they are degraded by the proteasome. Derlin-1, a member of a family of proteins that bears homology to
Yukako Oda et al.
The Journal of cell biology, 172(3), 383-393 (2006-02-02)
Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. Components of both productive folding and ER-associated degradation (ERAD) mechanisms are known to be up-regulated by the

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