癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
RNF34 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, E |
|---|---|
| Primary Accession | Q969K3 |
| Other Accession | Q6AYH3, Q99KR6, Q5E9J6, NP_079402.2, NP_919247.1 |
| Reactivity | Human |
| Predicted | Bovine, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 41641 Da |
| Antigen Region | 283-311 aa |
| Gene ID | 80196 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase RNF34, 632- {ECO:0000269|PubMed:25012219, ECO:0000269|Ref13}, Caspase regulator CARP1, Caspases-8 and -10-associated RING finger protein 1, CARP-1, FYVE-RING finger protein Momo, RNF34 (HGNC:17297) |
| Target/Specificity | This RNF34 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 283-311 amino acids from the C-terminal region of human RNF34. |
| Dilution | WB~~1:1000 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 | RNF34 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | RNF34 (HGNC:17297) |
|---|---|
| Function | E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed:25012219). |
| Cellular Location | Cell membrane; Peripheral membrane protein. Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus Nucleus speckle. Cytoplasm, cytosol |
| Tissue Location | Ubiquitous. Detected in heart, brain, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, colon and leukocytes. |
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 RINF finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein interacts with DNAJA3/hTid-1, which is a DnaJ protein reported to function as a modulator of apoptosis. Overexpression of this gene in Hela cells was shown to confer the resistance to TNF-alpha induced apoptosis, suggesting an anti-apoptotic function of this protein. This protein can be cleaved by caspase-3 during the induction of apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
REFERENCES
Erlbruch, A., et al. Proteomics 10(16):2890-2900(2010)
Yang, W., et al. Cell Cycle 7(5):670-682(2008)
Yang, W., et al. J. Biol. Chem. 282(5):3273-3281(2007)
Konishi, T., et al. Mol. Cancer Ther. 4(5):743-750(2005)
Sasaki, S., et al. J. Exp. Clin. Cancer Res. 23(3):507-512(2004)
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