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Merck
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Documentos Principais

D1194

Sigma-Aldrich

Anti-Derlin-2 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Anti-DERL2, Anti-Der1-like domain family, member 2

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

antigen ~21 kDa

reatividade de espécies

human, mouse

concentração

~1.0 mg/mL

técnica(s)

indirect immunofluorescence: 5-10 μg/mL using HeLa cells
western blot: 2.0-4.0 μg/mL using whole extract of mouse 3T3 cells

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... DERL2(51009)
mouse ... Derl2(116891)

Descrição geral

Derlin-1, Derlin-2, and Derlin-3 are the mammalian homologues of yeast Der1p, a transmembrane protein required for yeast endoplasmic reticulum-associated degradation (ERAD). Derlin-2 is approximately 30% identical to Derlin-1. In rat Derlin-2 is present to the endoplasmic reticulum(ER) membrane and forms a multisubunit complex with other proteins.

Imunogênio

synthetic peptide corresponding to amino acid residues 223-239 of human derlin-2 conjugated to KLH via an N-terminal added cysteine residue. The corresponding sequence is identical in mouse.

Aplicação

Anti-Derlin-2 antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

Ações bioquímicas/fisiológicas

Derlin-2, also known as F-LANa, is involved in the degradation of misfolded glycoproteins in the ER. Derlin-2 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-2 also interacts with the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

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


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection
Lilley BN, et al.
Journal of Virology, 80(17), 8739-8744 (2006)
Guohui Ren et al.
American journal of physiology. Renal physiology, 314(3), F471-F482 (2017-11-24)
Podocytes are terminally differentiated cells of the kidney filtration barrier with a limited proliferative capacity and are the primary glomerular target for various sources of cellular stress. Accordingly, it is particularly important for podocytes to cope with stress efficiently to
Podocytes exhibit a specialized protein quality control employing derlin-2 in kidney disease
Ren G, et al.
American Journal of Physiology: Renal Physiology, 314(3), F471-F482 (2017)
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
Akansha Tiwari et al.
Journal of cell science, 126(Pt 9), 1962-1968 (2013-02-28)
Stromal cell-derived factor 2-like 1 (SDF2L1) is an endoplasmic reticulum (ER)-localized protein whose function is undefined. Here we show that SDF2L1 protein levels are increased in response to ER stress-inducing compounds, but not other cell stressors that we tested in

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