RNF31 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- 实验流程
- 背景知识
Application ![]()
| WB, E |
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Primary Accession | Q96EP0 |
Other Accession | NP_060469.4 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 119652 Da |
Antigen Region | 955-983 aa |
Gene ID | 55072 |
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Other Names | E3 ubiquitin-protein ligase RNF31, 632-, HOIL-1-interacting protein, HOIP, RING finger protein 31, Zinc in-between-RING-finger ubiquitin-associated domain protein, RNF31, ZIBRA |
Target/Specificity | This RNF31 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 955-983 amino acids from the C-terminal region of human RNF31. |
Dilution | WB~~1:2000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
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 | RNF31 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | RNF31 (HGNC:16031) |
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Function | E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684, PubMed:28481331). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684). Linear ubiquitination mediated by the LUBAC complex interferes with TNF- induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:28189684). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:20005846, PubMed:27458237). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331, PubMed:34012115). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331). Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed:34012115). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331, PubMed:34012115). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998). RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa- B activation (PubMed:27777308). Binds polyubiquitin of different linkage types (PubMed:23708998). |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q924T7}. |
Tissue Location | Expressed in both normal and transformed breast epithelial cell lines. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The protein encoded by this gene contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions.
REFERENCES
Silva, L.K., et al. Eur. J. Hum. Genet. (2010) In press : Ehrlund, A., et al. Mol. Cell. Biol. 29(8):2230-2242(2009) Tokunaga, F., et al. Nat. Cell Biol. 11(2):123-132(2009) Kirisako, T., et al. EMBO J. 25(20):4877-4887(2006) Lim, J., et al. Cell 125(4):801-814(2006)

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