biological source
rabbit
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
Quality Level
Gene Information
human ... DERL2(51009)
mouse ... Derl2(116891)
General description
Derlin-1、Derlin-2和Derlin-3是酵母Der1p的哺乳动物同源物,Der1p是酵母内质网相关降解(ERAD)所需的跨膜蛋白。Derlin-2与Derlin-1大约30%相同。在大鼠中,Derlin-2存在于内质网(ER)膜上,并与其他蛋白质形成多亚基复合物。
Immunogen
合成肽,对应于人derlin-2的氨基酸残基223-239,通过一个在N端添加的半胱氨酸残基与KLH偶联。在小鼠中的相应序列是相同的。
Application
兔抗Derlin-2抗体可用于免疫印迹和免疫荧光分析。
Biochem/physiol Actions
Derlin-2,也称为F-LANa,参与ER中错误折叠的糖蛋白的降解。Derlin-2与Derlin-1具有约30%的序列同一性,并且四次跨越ER的脂质双层,显示出与Derlin-1的结构相似性。它是哺乳动物ER相关降解(ERAD)机制的组成部分,并被未折叠的蛋白反应(UPR)上调。该基因的过表达导致错误折叠糖蛋白的降解增加,而其敲低阻止了降解。Derlin-2还与酵母Hrd1p/Hrd3p泛素-连接酶复合物的哺乳动物直系同源物相互作用。
Physical form
溶于含15 mM叠氮化钠的0.01 M磷酸盐缓冲生理盐水(pH 7.4)的溶液。
Disclaimer
除非我们的产品目录或产品附带的其他公司文档另有说明,否则我们的产品仅供研究使用,不得用于任何其他目的,包括但不限于未经授权的商业用途、体外诊断用途、离体或体内治疗用途或任何类型的消费或应用于人类或动物。
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存储类别
10 - Combustible liquids
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
此项目有
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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