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。
UBA52 Antibody (C-Term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IHC-P, FC, E |
|---|---|
| Primary Accession | P62987 |
| Other Accession | P62986, P63053, P62984, P0C273, P62985, P63048, NP_001029102.1, NP_003324.1 |
| Reactivity | Human |
| Predicted | Bovine, Chicken, Monkey, Mouse, Pig, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 14728 Da |
| Antigen Region | 100-128 aa |
| Gene ID | 7311 |
|---|---|
| Other Names | Ubiquitin-60S ribosomal protein L40, CEP52, Ubiquitin A-52 residue ribosomal protein fusion product 1, Ubiquitin, 60S ribosomal protein L40, UBA52, UBCEP2 |
| Target/Specificity | This UBA52 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 100-128 amino acids from the C-terminal region of human UBA52. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 FC~~1:10~50 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 | UBA52 Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | UBA52 |
|---|---|
| Synonyms | UBCEP2 |
| Function | [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. |
| Cellular Location | [Ubiquitin]: Cytoplasm. Nucleus |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Ubiquitin is a highly conserved nuclear and cytoplasmic protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein L40 at the C terminus, a C-terminal extension protein (CEP). Multiple processed pseudogenes derived from this gene are present in the genome.
REFERENCES
Memet, S. Biochem. Pharmacol. 72(9):1180-1195(2006)
Wang, A.G., et al. Biochem. Biophys. Res. Commun. 345(3):1022-1032(2006)
Foster, L.J., et al. J. Proteome Res. 5(1):64-75(2006)
Hu, Y., et al. Mol. Cell Proteomics 4(12):2000-2009(2005)
Westhoff, B., et al. Curr. Biol. 15(11):1058-1064(2005)
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