SYVN1 Antibody, FITC conjugated
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Description
Introduction to SYVN1 Antibody, FITC Conjugated
SYVN1 (Synoviolin 1), also known as HRD1, is an E3 ubiquitin ligase critical for endoplasmic reticulum (ER)-associated degradation (ERAD). FITC-conjugated SYVN1 antibodies are fluorescently labeled probes used to detect and localize SYVN1 protein in cellular studies. These antibodies enable visualization of SYVN1 in immunofluorescence (IF) microscopy, flow cytometry (FCM), and related techniques.
Applications in Research
FITC-conjugated SYVN1 antibodies are employed in diverse experimental workflows:
Immunofluorescence (IF) Microscopy
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Localization studies: Detect SYVN1 in ER membranes or cytoplasmic aggregates .
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Colocalization experiments: Track interactions with ER stress markers (e.g., BiP/GRP78) or autophagy-related proteins (e.g., SQSTM1/p62) .
Flow Cytometry (FCM)
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Quantify SYVN1 expression: Measure protein levels in cell populations, particularly in immune or epithelial cells .
Western Blotting (WB)
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Validate protein degradation: Confirm SYVN1-mediated ubiquitination of substrates (e.g., SIRT2, SERPINA1 E342K/ATZ) .
ER Stress and Asthma Pathogenesis
SYVN1 suppresses ER stress by degrading SIRT2, a regulator of epithelial-mesenchymal transition (EMT). FITC-conjugated antibodies confirmed SYVN1’s colocalization with SIRT2 in bronchial epithelial cells (BEAS-2B), supporting its role in mitigating airway remodeling .
Autophagy and Protein Degradation
SYVN1 facilitates lysosomal degradation of misfolded proteins (e.g., SERPINA1 E342K/ATZ) via SQSTM1/p62-dependent autophagy. FITC-labeled SYVN1 antibodies enabled visualization of its interaction with lysosomal markers (e.g., LAMP1) in HEK293T cells .
Diabetic Retinopathy (DR) Models
High SYVN1 expression reduced vascular leakage and endothelin-1 (ET-1) levels in diabetic mice. FITC-dextran perfusion assays demonstrated SYVN1’s protective effects against retinal microvascular permeability .
Product Specs
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Generally, we can ship the products within 1-3 business days after receiving your orders. Delivery times may vary based on the purchasing method or location. For specific delivery times, please consult your local distributors.
Synonyms
SYVN1; HRD1; KIAA1810; E3 ubiquitin-protein ligase synoviolin; RING-type E3 ubiquitin transferase synoviolin; Synovial apoptosis inhibitor 1
Target Names
Uniprot No.
Target Background
Function
SYVN1 (Synoviolin) is an E3 ubiquitin-protein ligase that specifically accepts ubiquitin from the endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. SYVN1 is a component of the endoplasmic reticulum quality control (ERQC) system, also known as ER-associated degradation (ERAD), which is involved in the ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. SYVN1 also promotes the degradation of normal but naturally short-lived proteins, such as SGK. It protects cells from ER stress-induced apoptosis and safeguards neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. SYVN1 sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation, and apoptosis. It mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1. During the early stage of B cell development, SYVN1 is required for the degradation of the pre-B cell receptor (pre-BCR) complex, thus supporting further differentiation into mature B cells.
Gene References Into Functions
- This research demonstrated that the stability of Herp is regulated by synoviolin through lysine ubiquitination-independent proteasomal degradation. PMID: 29863080
- Hrd1 is an E3 ubiquitin ligase in human T cells. Elevated Hrd1 expression is observed in CD4-positive T cells from multiple sclerosis patients. PMID: 27417417
- PADI4 directly interacts with SYVN1, and overexpression of PADI4 suppresses the ubiquitination of proteins. Therefore, a reduction in ER stress induced by PADI4 may prevent the initiation of chronic RA by suppressing the proliferative signals of RA synoviocytes. PMID: 29039504
- Amyloid beta oligomers modulate BACE1 through an XBP-1-dependent pathway involving HRD1. PMID: 27853315
- Findings support a model of Hrd1 complex formation, where the Hrd1 cytoplasmic domain and FAM8A1 play a central role in the assembly and activity of this ERAD machinery. PMID: 28827405
- The HSP70-Hrd1 axis represents a potential therapeutic target for restoring the oncorepressor activity of unstable lymphoma-associated Blimp-1 mutants. PMID: 28842558
- This study demonstrated that SYVN1 enhances SERPINA1(E342K)/ATZ degradation through SQSTM1-dependent autophagy and attenuates SERPINA1(E342K)/ATZ cytotoxicity. PMID: 28121484
- Results showed that overexpression of Hrd1 increased the proteasomal degradation and microtubule-dependent aggresome formation of OPTN in the microtubular organizing center, whereas knockdown of Hrd1 stabilized OPTN and inhibited aggresome formation of OPTN. PMID: 28334804
- Data indicate that E3 ubiquitin ligase HRD1 (HRD1) decreased the protein level of S100A8 through ubiquitination. PMID: 28423597
- Analysis of affinity-captured Hrd1 complexes from these cells by size-exclusion chromatography, immunodepletion, and absolute quantification mass spectrometry identified two major high-molecular-mass complexes with distinct sets of interacting proteins and variable stoichiometries, suggesting a previously unrecognized heterogeneity in the functional units of Hrd1-mediated protein degradation. PMID: 28411238
- This study provides new insights into the CFTR biosynthetic pathway. It suggests that SYVN1 and FBXO2 represent two distinct multiprotein complexes that may degrade DeltaF508-CFTR in airway epithelia and identifies a new role for NEDD8 in regulating DeltaF508-CFTR ubiquitination. PMID: 27756846
- The study shows that mir125b is up-regulated in osteoarthritis (OA) and inversely correlated with SYNV1 expression. Findings demonstrated that miR- 125b-5p could promote apoptosis of synovial cells by targeting the SYVN1 gene, and excessive apoptosis of synovial cells could contribute to the development of OA. PMID: 28260078
- HRD1 is a novel substrate for USP19. USP19 negatively regulates the ubiquitination of HRD1 and prevents it from undergoing proteasomal degradation. PMID: 27827840
- Prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP. PMID: 26740554
- OS-9, an ER-resident lectin, acts downstream of Grp94 to further recognize misfolded alpha1 subunits in a glycan-dependent manner. This delivers misfolded alpha1 subunits to the Hrd1-mediated ubiquitination and the valosin-containing protein-mediated extraction pathway. PMID: 26945068
- These findings uncover a novel role for HRD1 in breast cancer. PMID: 26536657
- The inherently unstable nature of the human SEL1L protein lies in its transmembrane domain, and association of HRD1 with the SEL1L transmembrane domain restored its stability. PMID: 26471130
- Specific silencing of Derlin-2, p97, and HRD1 by shRNAs increases steady state levels of proinsulin. These ERAD constituents are critically involved in proinsulin degradation and may therefore also play a role in subsequent antigen generation. PMID: 26107514
- Charcot-Marie-Tooth disease-related PMP22 is trapped in the endoplasmic reticulum by calnexin-dependent retention and Rer1-mediated early Golgi retrieval systems and partly degraded by the Hrd1-mediated endoplasmic reticulum-associated degradation system. PMID: 25385046
- Results show that HRD1 and RFP2 are required for the disposal of V247M alpha-sarcoglycan mutant. PMID: 24565866
- Herp localizes to the endoplasmic reticulum-derived quality control compartment (ERQC) and recruits HRD1, which targets to endoplasmic reticulum associated degradation the substrate presented by the OS-9 lectin at the ERQC. PMID: 24478453
- Hrd1 was identified as a novel E3 ubiquitin ligase responsible for compromised Nrf2 response during liver cirrhosis PMID: 24636985
- A new HRD1-associated membrane protein named HERP2, which is homologous to the previously identified HRD1 partner HERP1. Despite sequence homology, HERP2 is constitutively expressed in cells, whereas HERP1 is highly induced by ER stress. PMID: 24366871
- The interactions between P97 and these motifs, including VCP-binding motif (VBM) and VCP-interacting motif (VIM). The solution structures of the VBM motif from HRD1 and the VIM motif from SVIP are both comprised mainly of a single alpha-helix. PMID: 24100225
- Derlin2 functions with HRD1 in ERAD of certain substrates independent of their glycosylation status. PMID: 23867461
- A subset of integral membrane proteins, therefore, requires an early dislocation event to expose part of their luminal domain to the cytosol, before HRD1-mediated polyubiquitination and dislocation PMID: 23929775
- Synoviolin up-regulates amyloid beta production by targeting a negative regulator of gamma-secretase, Rer1, for degradation. PMID: 23129766
- Hrd1 functions as an E3 targeting tau or abnormal p-tau for proteasome degradation. PMID: 22280354
- Regulation of the stability and assembly of the HRD1-SEL1L complex is crucial to optimize the degradation kinetics of ERAD substrates PMID: 21454652
- Binding of Herp to Hrd1-containing ERAD complexes positively regulates the ubiquitylation activity of these complexes, thus permitting cell survival during ER stress. PMID: 21149444
- Data support a physiological role for HRD1 and UBE2J1 in the homeostatic regulation of MHC class I assembly and expression PMID: 21245296
- Using brain tissue from Alzheimer's disease and normal subjects, a negative correlation was found between the expressed levels of HRD1 and of amyloid-beta; this suggests the possible involvement of HRD1 in amyloid-beta generation. PMID: 20606367
- Serine-dependent, HRD1-mediated ubiquitination targets TCRalpha to the ERAD pathway PMID: 20519503
- HRD1 promotes ubiquitination and degradation of amyloid precursor protein (APP) that leads to decreased amyloid beta production, whereas HRD1 loss in Alzheimer's disease leads to accumulation of APP and increased levels of amyloid beta. PMID: 20237263
- These data demonstrate a role of the E3 ubiquitin ligases in CTA1 retro-translocation. PMID: 19864457
- The results support that gp78 is an E3 targeting CFTRDeltaF508 for degradation and Hrd1 inhibits CFTRDeltaF508 degradation by acting as an E3 for gp78. PMID: 19828134
- HRD1 protects against endoplasmic reticulum stress-induced apoptosis through endoplasmic reticulum-associated degradation. PMID: 12459480
- Endogenous hHrd1 resides in the ER and has a ubiquitin-ligase activity PMID: 12646171
- Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum PMID: 14593114
- Results showed that Synoviolin, a novel causative factor for rheumatoid arthritis, is up-regulated in proliferating synovial cells in the disease. PMID: 16786162
- Elevated peripheral blood (PB) levels of synoviolin were associated with nonresponse to infliximab treatment. Upregulation of synoviolin by IL-lbeta and TNFalpha may contribute to prolonged survival of immune cells and rheumatoid arthritis chronicity. PMID: 16802346
- These results suggest that Hrd1 is a novel htt-interacting protein that can target pathogenic httN for degradation and is able to protect cells against httN-induced cell death. PMID: 17141218
- The endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin' destroys p53 PMID: 17170702
- Endoplasmic reticulum stress-induced HRD1 and SEL1 expressions are mediated by IRE1-XBP1- and ATF6-dependent pathways, respectively PMID: 17967421
- Synoviolin is overexpressed in the synovial cells of patients with rheumatoid arthritis, resulting in a state in which the cell deals with accumulated unfolded proteins excessively PMID: 18235538
- OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD PMID: 18264092
- These findings reveal a role for SEL1L and HRD1 in IgM quality control. PMID: 18314878
- The proline-rich domain of HRD1 is necessary to promote the degradation of Pael-R, and the protein's transmembrane domain is necessary to transfer Pael-R from the endoplasmic reticulum (ER) to the cytosol. PMID: 18344614
- XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP PMID: 18502753
- The promoter of human HRD1, which encodes an E3 ubiquitin ligase, an important component of ERAD, was analyzed PMID: 18664523
Database Links
Protein Families
HRD1 family
Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue Specificity
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).
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