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。
UBE4B Antibody (N-term) 精选
Purified Rabbit Polyclonal Antibody (Pab)
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- 背景知识
Application 
| WB, IHC-P-Leica, E |
|---|---|
| Primary Accession | O95155 |
| Other Accession | Q9ES00 |
| Reactivity | Human, Mouse |
| Predicted | Rat, Bovine, Canine, Rabbit, Chicken |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 146185 Da |
| Antigen Region | 112-142 aa |
| Gene ID | 10277 |
|---|---|
| Other Names | Ubiquitin conjugation factor E4 B, 632-, UBE4B (HGNC:12500) |
| Target/Specificity | This UBE4B antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 112-142 amino acids from the N-terminal region of human UBE4B. |
| Dilution | WB~~1:1000 IHC-P-Leica~~1:500 E~~Use at an assay dependent concentration. |
| 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 | UBE4B Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | UBE4B (HGNC:12500) |
|---|---|
| Function | Acts as an E3 ubiquitin ligase and E4 ubiquitin chain elongation enzyme specifically involved in polyubiquitin chain assembly (PubMed:21317885). Plays an essential role in cardiac development and in the protection of neurons from degeneration evoked by ER stress (By similarity). Is recruited to early endosomes via interaction with the ESCRT-0 component HGS, where it ubiquitinates membrane protein cargo such as EGFR and APP to promote their sorting into multivesicular bodies and subsequent lysosomal degradation (PubMed:24344129, PubMed:32841720). Promotes MDM2-mediated polyubiquitination and subsequent degradation of the tumor suppressor TP53 (PubMed:21317885). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates the formation of 'Lys-11'- or 'Lys-48'-linked polyubiquitin chains on TRA2A and PYCR2 and induces their degradation by the proteasome (PubMed:35669517). Thereby regulates the alternative splicing function of TRA2A (PubMed:35669517). Also regulates the mTOR signaling pathway by polyubiquitinating KLHL22, an E3 ligase that degrades the GATOR1 complex protein DEPDC5 (By similarity). Under mitochondrial depolarization, mediates the ubiquitination of NIPSNAP1, thereby promoting its interaction with autophagy receptors NDP52 and p62/SQSTM1 and its subsequent degradation via the lysosome-dependent pathway (PubMed:41596759). |
| Cellular Location | Early endosome. Cytoplasm Nucleus {ECO:0000250|UniProtKB:Q9ES00} |
| Tissue Location | Expressed in differentiated myotubes (at protein level) (PubMed:17369820). Highest expression in ovary, testis, heart and skeletal muscle (PubMed:11802788). Expression is low in colon, thymus and peripheral blood leukocytes (PubMed:11802788). Almost undetectable in lung and spleen (PubMed:11802788) |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE4B represents an additional conjugation factor, E4, which is involved in multiubiquitin chain assembly. UBE4B also the strongest candidate among the neuroblastoma tumor suppressors.
REFERENCES
Ishikawa, K., et al., DNA Res. 5(3):169-176 (1998).
Mahoney, J.A., et al., Biochem. J. 361 (Pt 3), 587-595 (2002).
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