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SYVN1 (HRD1) Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - SYVN1 (HRD1) Antibody (C-term) AP2184A
    All lanes : Anti-HRD1 Antibody (A601) at 1:2000 dilution Lane 1: DU145 whole cell lysate Lane 2: Hela whole cell lysate Lane 3: mouse spleen lysate Lane 4: PC-3 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 68 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 1 - SYVN1 (HRD1) Antibody (C-term) AP2184A
    Anti-HRD1 Antibody (A601) at 1:2000 dilution + MOLT-4 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 68 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 3 - SYVN1 (HRD1) Antibody (C-term) AP2184A
    Fluorescent confocal image of HeLa cells stained with SYVN1 (HRD1) (C-term) antibody. HeLa cells were fixed with 4% PFA (20 min), permeabilized with Triton X-100 (0.2%, 30 min). Cells were then incubated with AP2184a SYVN1 (HRD1) (C-term) primary antibody (1:200, 2 h at room temperature). For secondary antibody, Alexa Fluor® 488 conjugated donkey anti-rabbit antibody (green) was used (1:1000, 1h). Nuclei were counterstained with Hoechst 33342 (blue) (10 μg/ml, 5 min).
  • 1 - SYVN1 (HRD1) Antibody (C-term) AP2184A
    Mouse Neuroblastoma Neuro2A (N2A) was transiently transfected, collected at 72h after transfection. Primary antibodies against syvn1 (Abgent # AP2184a, 1:1000) and anti-rabbit secondary POD-conjugated antibodies from Pierce Biotechnology, Inc (Rockford, IL, 1:2000)(Provided by Dr. Susana Granell & Institution University of Arkansas).
  • 14 - SYVN1 (HRD1) Antibody (C-term) AP2184A
    Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
  • 14 - SYVN1 (HRD1) Antibody (C-term) AP2184A
    Formalin-fixed and paraffin-embedded human Liver tissue reacted with SYVN1 (HRD1) Antibody (C-term)(Cat.#AP2184a), which was peroxidase-conjugated to the secondary antibody, followed by AEC staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
IF, WB, IHC-P, E
Primary Accession Q86TM6
Other Accession Q9DBY1, Q8N6E8
Reactivity Human, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Additional info
Gene ID 84447
Other Names E3 ubiquitin-protein ligase synoviolin, 632-, Synovial apoptosis inhibitor 1, SYVN1, HRD1, KIAA1810
Target/Specificity This SYVN1 (HRD1) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 586-617 amino acids from the C-terminal region of human SYVN1 (HRD1).
Dilution WB~~1:1000
IF~~1:200
IHC-P~~1:50~100
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsSYVN1 (HRD1) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SYVN1
Synonyms HRD1, KIAA1810
Function Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation (PubMed:17141218). Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity).
Cellular Location Endoplasmic reticulum membrane; Multi-pass membrane protein
Tissue Location Ubiquitously expressed, with highest levels in liver and kidney (at protein level). Up-regulated in synovial tissues from patients with rheumatoid arthritis (at protein level).
Research Areas
Cytosolic Processing Governs TAP-Independent Presentation of a Critical Melanoma Antigen.
Author : Vigneron N1,2,3,Ferrari V1,2,3,Van den Eynde BJ4,2,3,Cresswell P5,6,Leonhardt RM5.
J Immunol. 2018 Aug 22. pii: ji1701479. doi: 10.4049/jimmunol.1701479. [Epub ahead of print]
30135181
HRD1 prevents apoptosis in renal tubular epithelial cells by mediating eIF2α ubiquitylation and degradation.
Author : Huang Y1,2,Sun Y3,Cao Y3,Sun H1,Li M1,3,You H1,Su D4,Li Y5,Liang X6,7.
Cell Death Dis. 2017 Dec 11;8(12):3202. doi: 10.1038/s41419-017-0002-y.
29233968
Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.
Author : Peters SL1, Déry MA1, LeBlanc AC2.
Hum Mol Genet. 2016 Mar 1;25(5):976-88. doi: 10.1093/hmg/ddv630. Epub 2016 Jan 5.
26740554
Acute ER stress regulates amyloid precursor protein processing through ubiquitin-dependent degradation.
Author : Jung ES1, Hong H2, Kim C1, Mook-Jung I1.
Sci Rep. 2015 Mar 5;5:8805. doi: 10.1038/srep08805.
25740315
Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation.
Author : Grotzke JE1, Lu Q, Cresswell P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3393-8. doi: 10.1073/pnas.1300328110. Epub 2013 Feb 11.
23401531
Vacuolar-type H+-ATPase V1A subunit is a molecular partner of Wolfram syndrome 1 (WFS1) protein, which regulates its expression and stability.
Author : Gharanei S1, Zatyka M, Astuti D, Fenton J, Sik A, Nagy Z, Barrett TG.
Hum Mol Genet. 2013 Jan 15;22(2):203-17. doi: 10.1093/hmg/dds400. Epub 2012 Oct 3.
23035048
Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Author : Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. doi: 10.1074/jbc.M111.248856. Epub 2011 Oct 10.
21987572
Cyclosporin A induces the unfolded protein response in keratinocytes.
Author : Hibino M, Sugiura K, Muro Y, Shimoyama Y, Tomita Y.
Arch Dermatol Res. 2011 Sep;303(7):481-9. doi: 10.1007/s00403-010-1099-3. Epub 2011 Jan 11.
21221615
Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation.
Author : Kaneko M, Koike H, Saito R, Kitamura Y, Okuma Y, Nomura Y.
J Neurosci. 2010 Mar 17;30(11):3924-32. doi: 10.1523/JNEUROSCI.2422-09.2010.
20237263
Correlation between decrease in protein levels of ubiquitin ligase HRD1 and amyloid-beta production.
Author : Saito R, Kaneko M, Okuma Y, Nomura Y.
J Pharmacol Sci. 2010;113(3):285-8. Epub 2010 Jul 1.
20606367
An E3 ubiquitin ligase, Synoviolin, is involved in the degradation of immature nicastrin, and regulates the production of amyloid beta-protein.
Author : Maeda T, Marutani T, Zou K, Araki W, Tanabe C, Yagishita N, Yamano Y, Amano T, Michikawa M, Nakajima T, Komano H.
FEBS J. 2009 Oct;276(20):5832-40. doi: 10.1111/j.1742-4658.2009.07264.x. Epub 2009 Sep 2.
19725872
The unfolded protein response is activated in differentiating epidermal keratinocytes.
Author : Sugiura K, Muro Y, Futamura K, Matsumoto K, Hashimoto N, Nishizawa Y, Nagasaka T, Saito H, Tomita Y, Usukura J.
J Invest Dermatol. 2009 Sep;129(9):2126-35. doi: 10.1038/jid.2009.51. Epub 2009 Mar 12.
19282840
Overexpression of synoviolin in peripheral blood and synoviocytes from rheumatoid arthritis patients and continued elevation in nonresponders to infliximab treatment.
Author : Toh ML, Marotte H, Blond JL, Jhumka U, Eljaafari A, Mougin B, Miossec P.
Arthritis Rheum. 2006 Jul;54(7):2109-18.
16802346
WFS1-deficiency increases endoplasmic reticulum stress, impairs cell cycle progression and triggers the apoptotic pathway specifically in pancreatic beta-cells.
Author : Yamada T, Ishihara H, Tamura A, Takahashi R, Yamaguchi S, Takei D, Tokita A, Satake C, Tashiro F, Katagiri H, Aburatani H, Miyazaki J, Oka Y.
Hum Mol Genet. 2006 May 15;15(10):1600-9. Epub 2006 Mar 28.
16571599

BACKGROUND

HRD1 is a ubiquitin ligase whose expression is induced by the unfolded protein response (UPR) following endoplasmic reticulum stress. Expression of HRD1 protects cells from apoptosis by inducing degradation of abnormally processed proteins that accumulate in the endoplasmic reticulum. HRD1 is expressed in many tissues, strongly expressed in brain, pancreas, liver, kidney and skeletal muscle. Amano T, et al. reported that Synoviolin/Hrd1 (expressed in rheumatoid synovium) is a novel causative factor for arthropathy by triggering synovial cell outgrowth through its antiapoptotic effects. HRD1 contains one ring-type zinc finger.

REFERENCES

References for protein:
1.Kaneko M, FEBS Lett. 2002. 532: 147-152.
2.Amano T, et al. Genes Dev. 2003. 17: 2436-2449.

References for HeLa cell line:
1. Scherer WF, Syverton JT, Gey GO (May 1953). "Studies on the propagation in vitro of poliomyelitis viruses. IV. Viral multiplication in a stable strain of human malignant epithelial cells (strain HeLa) derived from an epidermoid carcinoma of the cervix". J. Exp. Med. 97 (5): 695–710. [PubMed:13052828].

2. Macville M, Schröck E, Padilla-Nash H, Keck C, Ghadimi BM, Zimonjic D, Popescu N, Ried T (January 1999). "Comprehensive and definitive molecular cytogenetic characterization of HeLa cells by spectral karyotyping". Cancer Res. 59 (1): 141–50. [PubMed: 9892199].
3. Rahbari R, Sheahan T, Modes V, Collier P, Macfarlane C, Badge RM (April 2009). "A novel L1 retrotransposon marker for HeLa cell line identification". BioTechniques 46 (4): 277–84. [PubMed: 19450234].

4. Capes-Davis A, Theodosopoulos G, Atkin I, Drexler HG, Kohara A, MacLeod RA, Masters JR, Nakamura Y, Reid YA, Reddel RR, Freshney RI (July 2010). "Check your cultures! A list of cross-contaminated or misidentified cell lines". Int. J. Cancer 127 (1): 1–8. [PubMed:20143388].

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