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SYVN1 / HRD1 Antibody (Internal)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P |
|---|---|
| Primary Accession | Q86TM6 |
| Reactivity | Human, Mouse, Rabbit, Zebrafish, Hamster, Monkey, Horse, Xenopus, Bovine, Dog |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 68kDa |
| Dilution | IHC-P (5-10 µg/ml) |
| Gene ID | 84447 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase synoviolin, 6.3.2.-, Synovial apoptosis inhibitor 1, SYVN1, HRD1, KIAA1810 |
| Target/Specificity | Human SYVN1 / HRD1. BLAST analysis of the peptide immunogen showed no homology with other human proteins. |
| Reconstitution & Storage | Long term: -70°C; Short term: +4°C |
| Precautions | SYVN1 / HRD1 Antibody (Internal) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SYVN1 |
|---|---|
| Synonyms | HRD1, KIAA1810 |
| Function | 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, PubMed:28827405). 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, PubMed:28842558). 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). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (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) |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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. 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. 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. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis.
References
Kaneko M.,et al.FEBS Lett. 532:147-152(2002).
Nadav E.,et al.Biochem. Biophys. Res. Commun. 303:91-97(2003).
Amano T.,et al.Genes Dev. 17:2436-2449(2003).
Kikkert M.,et al.J. Biol. Chem. 279:3525-3534(2004).
Nagase T.,et al.DNA Res. 8:85-95(2001).
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