D1194
Anti-Derlin-2 antibody produced in rabbit
~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-DERL2, Anti-Der1-like domain family, member 2
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~21 kDa
species reactivity
human, mouse
concentration
~1.0 mg/mL
technique(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
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... DERL2(51009)
mouse ... Derl2(116891)
Related Categories
General description
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.
Immunogen
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.
Application
Anti-Derlin-2 antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
Biochem/physiol Actions
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.
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
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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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)
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
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
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