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。
RFWD2 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, E |
|---|---|
| Primary Accession | Q8NHY2 |
| Other Accession | Q9R1A8, NP_071902.2 |
| Reactivity | Human |
| Predicted | Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 80474 Da |
| Antigen Region | 672-701 aa |
| Gene ID | 64326 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase RFWD2, 632-, Constitutive photomorphogenesis protein 1 homolog, hCOP1, RING finger and WD repeat domain protein 2, RING finger protein 200, RFWD2, COP1, RNF200 |
| Target/Specificity | This RFWD2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 672-701 amino acids from the C-terminal region of human RFWD2. |
| 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 | RFWD2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | COP1 (HGNC:17440) |
|---|---|
| Function | E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable). |
| Cellular Location | Nucleus speckle. Cytoplasm. Note=In the nucleus, it forms nuclear speckles |
| Tissue Location | Ubiquitously expressed at low level. Expressed at higher level in testis, placenta, skeletal muscle and heart |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1.
REFERENCES
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Kinyo, A., et al. J. Invest. Dermatol. 130(2):541-545(2010)
Li, D.Q., et al. Proc. Natl. Acad. Sci. U.S.A. 106(41):17493-17498(2009)
Kato, S., et al. J. Biol. Chem. 283(51):35464-35473(2008)
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