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D4443

Sigma-Aldrich

Anti-Derlin-1 antibody produced in rabbit

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

Synonym(s):

Anti-DERtrin 1, Anti-Degradation in endoplasmic reticulum protein 1, Anti-Derl-like protein 1

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About This Item

MDL number:
MFCD08705450
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~22 kDa

species reactivity

rat, hamster, monkey, mouse, bovine, human, canine

concentration

~1 mg/mL

technique(s)

indirect immunofluorescence: 2.5-5 μg/mL using rat NRK cells
western blot (chemiluminescent): 0.2-0.4 μg/mL using whole extract of human HeLa and mouse 3T3 cells.

UniProt accession no.

Q9BUN8

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DERL1(79139)
mouse ... Derl1(67819)

General description

Derlin-1 is a 22kDa hydrophobic protein that spans the lipid bilayer of the ER four times with its amino- and carboxy-terminus in the cytosol. It is expressed with high levels in liver, spleen, pancreas, lung, thymus, and ovary.
Derlin-1 shares human homology with yeast Der1p.

Immunogen

a synthetic peptide corresponding to the C-terminal region of human Derlin-1 with N-terminal added cysteine, conjugated to KLH. The corresponding sequence is identical in mouse.

Application

Anti-Derlin-1 antibody produced in rabbit has been used in:
  • immunostaining
  • co-immunoprecipitation
  • immunofluorescence

Biochem/physiol Actions

Derlin-1 can interact with peptide:N-glycanase (PNGase), a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins.
Derlin-1 is required for the dislocation of misfolded proteins from the ER lumen to the cytosol, where they are destroyed by the ubiquitin-proteasome system. It interacts with PNGase, a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins. It forms a membrane protein complex with VIMP ( (VCP-interacting membrane protein) and this complex serves as a receptor for p97. p97 interacts with several ubiquitin ligases, thus recruiting them to Derlin-1.

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Zlatka Kostova et al.
The EMBO journal, 22(10), 2309-2317 (2003-05-14)
The surveillance of the structural fidelity of the proteome is of utmost importance to all cells. The endoplasmic reticulum (ER) is the organelle responsible for proper folding and delivery of proteins to the secretory pathway. It contains a sophisticated protein
Molecular characterization and expression of DERL1 in bovine ovarian follicles and corpora lutea
Ndiaye K, et al.
Reproductive Biology and Endocrinology, 8(1), 94-94 (2010)
Yihong Ye et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(40), 14132-14138 (2005-09-28)
Misfolded proteins are eliminated from the endoplasmic reticulum (ER) by retrotranslocation into the cytosol, a pathway hijacked by certain viruses to destroy MHC class I heavy chains. The translocation of polypeptides across the ER membrane requires their polyubiquitination and subsequent
Yihong Ye et al.
Nature, 429(6994), 841-847 (2004-06-25)
Elimination of misfolded proteins from the endoplasmic reticulum (ER) by retro-translocation is an important physiological adaptation to ER stress. This process requires recognition of a substrate in the ER lumen and its subsequent movement through the membrane by the cytosolic
Brendan N Lilley et al.
Nature, 429(6994), 834-840 (2004-06-25)
After insertion into the endoplasmic reticulum (ER), proteins that fail to fold there are destroyed. Through a process termed dislocation such misfolded proteins arrive in the cytosol, where ubiquitination, deglycosylation and finally proteasomal proteolysis dispense with the unwanted polypeptides. The
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