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D2194

Sigma-Aldrich

Anti-Derlin-3 antibody produced in rabbit

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

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Synonym(s):
Anti-DERL3, Anti-Der1-like domain family, member 3
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~26 kDa

species reactivity

rat (predicted), human, mouse (predicted)

concentration

~1 mg/mL

technique(s)

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 accession no.

Q96Q80

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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.

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Certificates of Analysis (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)
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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