biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~70 kDa
species reactivity
mouse, human
concentration
~1.0 mg/mL
technique(s)
immunoprecipitation (IP): 5-10 μg using lysate of mouse brain, indirect immunofluorescence: suitable, western blot: 2-4 μg/mL using whole extract of HEK-293T cells expressing human HRD1/SYVN1.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SYVN1(84447)
mouse ... Syvn1(74126)
rat ... Syvn1(361712)
General description
Synoviolin (SYVN1) is an endoplasmic reticulum (ER)-membrane resident E3 ubiquitin ligase. The SYVN1 gene is mapped to human chromosome 11q13.1. Also known as HRD1, this protein has five transmembrane domains and a really interesting new gene (RING) finger domain.
Application
Anti-HRD1/SYVN1 antibody produced in rabbit has been used in immunoblotting and immunoprecipitation.
Biochem/physiol Actions
Anti-HRD1/SYVN1 recognizes human and mouse HRD1/SYVN1.
Synoviolin (SYVN1) protects against endoplasmic reticulum (ER) stress-induced apoptosis through ER stress-associated protein degradation (ERAD). The really interesting new gene (RING) finger domain of SYVN1 mediates the transfer of ubiquitin from E2 to substrates and a proline-rich domain. E3 ubiquitin-protein ligase (HRD1) expression is strongly induced by ER stress. HRD1 interacts with parkin-associated endothelin receptor-like receptor (Pael-R), promoting its degradation, and protects neurons from cell death caused by the accumulation of Pael-R. HRD1 is also found to enhance the degradation and suppress the toxicity of polyglutamine-expanded huntingtin. In addition to its role in ERAD, HRD1 targets tumor suppressor gene p53 for proteasomal degradation. Overexpression of HRD1 is implicated in the pathogenesis of rheumatoid arthritis. The deletion of gene locus of SYVN1 is implicated in spastic paraplegia, optic atrophy, and neuropathy (SPOAN) disorder.
Physical form
Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
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
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
Hui Yang et al.
Experimental cell research, 313(3), 538-550 (2006-12-05)
E3 ubiquitin ligases catalyze the conjugation of ubiquitin onto proteins, which acts as a signal for targeting proteins for degradation by the proteasome. Hrd1 is an endoplasmic reticulum (ER) membrane-spanning E3 with its catalytic active RING finger facing the cytosol.
Tomohiro Omura et al.
Journal of neuroscience research, 86(7), 1577-1587 (2008-02-05)
HRD1 is an E3 ubiquitin ligase and plays an important role in endoplasmic reticulum-associated degradation (ERAD). Parkin-associated endothelin receptor-like receptor (Pael-R) is a substrate of the E3 ubiquitin ligase parkin, which has been implicated in ER stress-induced cell death in
Kit Briant et al.
Journal of cell science, 128(22), 4112-4125 (2015-10-09)
Clearance of misfolded proteins from the endoplasmic reticulum (ER) is mediated by the ubiquitin-proteasome system in a process known as ER-associated degradation (ERAD). The mechanisms through which proteins containing aberrant transmembrane domains are degraded by ERAD are poorly understood. To
Jeffrey M Lynch et al.
Cell, 149(6), 1257-1268 (2012-06-12)
Thrombospondin (Thbs) proteins are induced in sites of tissue damage or active remodeling. The endoplasmic reticulum (ER) stress response is also prominently induced with disease where it regulates protein production and resolution of misfolded proteins. Here we describe a function
Yupeng Zhao et al.
iScience, 23(9), 101494-101494 (2020-09-12)
Atlastin (ATL) is a class of dynamin-like GTPases shaping endoplasmic reticulum (ER) by mediating homotypic membrane fusion. Defect of ATLs leads to abnormal ER structure and hereditary spastic paraplegia (HSP), a neurodegenerative disease with progressive spasticity. How ATLs are regulated
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