D4443
Anti-Derlin-1 antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
Anti-DERtrin 1, Anti-Degradation in endoplasmic reticulum protein 1, Anti-Derl-like protein 1
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关于此项目
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IF, WB CL
Citations:
12
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.
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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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
低风险生物材料
常规特殊物品
此项目有
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
Hui You et al.
Free radical biology & medicine, 207, 260-271 (2023-07-28)
The functions of liver fatty acid binding protein 1 (FABP1) in the regulation of nonalcoholic fatty liver disease (NAFLD) have been previously established. However, how FABP1 expression is dynamically regulated in metabolic disorders is unclear. Previous studies have reported that
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
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