Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunofluorescence (IF)
Purification
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
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).
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice
Avoid freeze-thaw cycles.
Storage
4 °C,-20 °C
Storage Comment
Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots.
Expiry Date
6 months
Peters, Déry, LeBlanc: "Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP." in: Human molecular genetics, Vol. 25, Issue 5, pp. 976-88, (2016) (PubMed).
Jung, Hong, Kim, Mook-Jung: "Acute ER stress regulates amyloid precursor protein processing through ubiquitin-dependent degradation." in: Scientific reports, Vol. 5, pp. 8805, (2015) (PubMed).
Grotzke, Lu, Cresswell: "Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 110, Issue 9, pp. 3393-8, (2013) (PubMed).
Gharanei, Zatyka, Astuti, Fenton, Sik, Nagy, Barrett: "Vacuolar-type H+-ATPase V1A subunit is a molecular partner of Wolfram syndrome 1 (WFS1) protein, which regulates its expression and stability." in: Human molecular genetics, Vol. 22, Issue 2, pp. 203-17, (2012) (PubMed).
Hibino, Sugiura, Muro, Shimoyama, Tomita: "Cyclosporin A induces the unfolded protein response in keratinocytes." in: Archives of dermatological research, Vol. 303, Issue 7, pp. 481-9, (2011) (PubMed).
Lee, Hammerle, Andrews, Stokes, Mustelin, Silva, Black, Doedens: "Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels." in: The Journal of biological chemistry, Vol. 286, Issue 48, pp. 41530-8, (2011) (PubMed).
Kaneko, Koike, Saito, Kitamura, Okuma, Nomura: "Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 30, Issue 11, pp. 3924-32, (2010) (PubMed).
Saito, Kaneko, Okuma, Nomura: "Correlation between decrease in protein levels of ubiquitin ligase HRD1 and amyloid-beta production." in: Journal of pharmacological sciences, Vol. 113, Issue 3, pp. 285-8, (2010) (PubMed).
Sugiura, Muro, Futamura, Matsumoto, Hashimoto, Nishizawa, Nagasaka, Saito, Tomita, Usukura: "The unfolded protein response is activated in differentiating epidermal keratinocytes." in: The Journal of investigative dermatology, Vol. 129, Issue 9, pp. 2126-35, (2009) (PubMed).
Maeda, Marutani, Zou, Araki, Tanabe, Yagishita, Yamano, Amano, Michikawa, Nakajima, Komano: "An E3 ubiquitin ligase, Synoviolin, is involved in the degradation of immature nicastrin, and regulates the production of amyloid beta-protein." in: The FEBS journal, Vol. 276, Issue 20, pp. 5832-40, (2009) (PubMed).
Toh, Marotte, Blond, Jhumka, Eljaafari, Mougin, Miossec: "Overexpression of synoviolin in peripheral blood and synoviocytes from rheumatoid arthritis patients and continued elevation in nonresponders to infliximab treatment." in: Arthritis and rheumatism, Vol. 54, Issue 7, pp. 2109-18, (2006) (PubMed).
Yamada, Ishihara, Tamura, Takahashi, Yamaguchi, Takei, Tokita, Satake, Tashiro, Katagiri, Aburatani, Miyazaki, Oka: "WFS1-deficiency increases endoplasmic reticulum stress, impairs cell cycle progression and triggers the apoptotic pathway specifically in pancreatic beta-cells." in: Human molecular genetics, Vol. 15, Issue 10, pp. 1600-9, (2006) (PubMed).
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.