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SYVN1 (HRD1) Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 3
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q86TM6 |
| Other Accession | Q5XHH7, Q6NRL6, Q9DBY1, Q8N6E8 |
| Reactivity | Human |
| Predicted | Mouse, Xenopus |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 67685 Da |
| Antigen Region | 58-88 aa |
| 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 58-88 amino acids from the N-terminal region of human SYVN1 (HRD1). |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain 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. |
| Precautions | SYVN1 (HRD1) Antibody (N-term) 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) |
Provided below are standard protocols that you may find useful for product applications.
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. Synoviolin/Hrd1 (expressed in rheumatoid synovium) is reported to be a novel causative factor for arthropathy by triggering synovial cell outgrowth through its antiapoptotic effects. HRD1 contains one ring-type zinc finger.
References
Kikkert, M., et al., J. Biol. Chem. 279(5):3525-3534 (2004). Amano, T., et al., Genes Dev. 17(19):2436-2449 (2003). Nadav, E., et al., Biochem. Biophys. Res. Commun. 303(1):91-97 (2003). Kaneko, M., et al., FEBS Lett. 532 (1-2), 147-152 (2002) (): ().
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