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Merck

D2194

Sigma-Aldrich

Anti-Derlin-3 antibody produced in rabbit

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

Synonym(e):

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

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~26 kDa

Speziesreaktivität

rat (predicted), human, mouse (predicted)

Konzentration

~1 mg/mL

Methode(n)

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

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Immunogen

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

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

10 - Combustible liquids

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Overexpression of Derlin 3 is associated with malignant phenotype of breast cancer cells
Shibata M, et al.
Oncology Reports, 38(3), 1760-1766 (2017)
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
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
Davy Vanhoutte et al.
Nature communications, 12(1), 3928-3928 (2021-06-26)
The thrombospondin (Thbs) family of secreted matricellular proteins are stress- and injury-induced mediators of cellular attachment dynamics and extracellular matrix protein production. Here we show that Thbs1, but not Thbs2, Thbs3 or Thbs4, induces lethal cardiac atrophy when overexpressed. Mechanistically

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