D1194
Anti-Derlin-2 antibody produced in rabbit
~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
동의어(들):
Anti-DERL2, Anti-Der1-like domain family, member 2
로그인조직 및 계약 가격 보기
크기 선택
100 μL
₩822,658
₩822,658
예상 입고일2025년 5월 19일세부사항
모든 사진(2)
크기 선택
보기 변경
100 μL
₩822,658
About This Item
UNSPSC 코드:
12352203
NACRES:
NA.41
₩822,658
예상 입고일2025년 5월 19일세부사항
추천 제품
생물학적 소스
rabbit
Quality Level
결합
unconjugated
항체 형태
affinity isolated antibody
항체 생산 유형
primary antibodies
클론
polyclonal
양식
buffered aqueous solution
분자량
antigen ~21 kDa
종 반응성
human, mouse
농도
~1.0 mg/mL
기술
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 수납 번호
배송 상태
dry ice
저장 온도
−20°C
타겟 번역 후 변형
unmodified
유전자 정보
human ... DERL2(51009)
mouse ... Derl2(116891)
일반 설명
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.
면역원
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.
애플리케이션
Anti-Derlin-2 antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
생화학적/생리학적 작용
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.
물리적 형태
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
면책조항
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
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
가장 최신 버전 중 하나를 선택하세요:
시험 성적서(COA)
Lot/Batch Number
Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection
Lilley BN, et al.
Journal of Virology, 80(17), 8739-8744 (2006)
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)
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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