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。
TRIM26 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- 背景知识
Application 
| WB, E |
|---|---|
| Primary Accession | Q12899 |
| Other Accession | P62603, O77666, Q99PN3, NP_003440.1 |
| Reactivity | Human |
| Predicted | Mouse, Pig, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 62166 Da |
| Antigen Region | 141-169 aa |
| Gene ID | 7726 |
|---|---|
| Other Names | Tripartite motif-containing protein 26, Acid finger protein, AFP, RING finger protein 95, Zinc finger protein 173, TRIM26, RNF95, ZNF173 |
| Target/Specificity | This TRIM26 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 141-169 amino acids from the N-terminal region of human TRIM26. |
| 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 | TRIM26 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TRIM26 |
|---|---|
| Synonyms | RNF95, ZNF173 |
| Function | E3 ubiquitin-protein ligase which regulates the IFN-beta production and antiviral response downstream of various DNA-encoded pattern-recognition receptors (PRRs). Also plays a central role in determining the response to different forms of oxidative stress by controlling levels of DNA glycosylases NEIL1, NEIL3 and NTH1 that are involved in repair of damaged DNA (PubMed:29610152, PubMed:36232914). Promotes nuclear IRF3 ubiquitination and proteasomal degradation (PubMed:25763818). Bridges together TBK1 and NEMO during the innate response to viral infection leading to the activation of TBK1. Positively regulates LPS-mediated inflammatory innate immune response by catalyzing the 'Lys-11'-linked polyubiquitination of TAB1 to enhance its activation and subsequent NF-kappa-B and MAPK signaling (PubMed:34017102). In a manner independent of its catalytic activity, inhibits WWP2, a SOX2-directed E3 ubiquitin ligase, and thus protects SOX2 from polyubiquitination and proteasomal degradation (PubMed:34732716). Ubiquitinates the histone acetyltransferase protein complex component PHF20 and thereby triggers its degradation in the nucleus after its recruitment by the histone demethylase KDM6B, serving as a scaffold protein (PubMed:23452852). Upon induction by TGF-beta, ubiquitinates the TFIID component TAF7 for proteasomal degradation (PubMed:29203640). Induces ferroptosis by ubiquitinating SLC7A11, a critical protein for lipid reactive oxygen species (ROS) scavenging (By similarity). Inhibits directly hepatitis B virus replication by mediating HBX ubiquitination and subsequent degradation (PubMed:35872575). |
| Cellular Location | Cytoplasm. Nucleus. Note=Viral infection mediates TRIM26 nuclear translocation |
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 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Although the function of the protein is unknown, the RING domain suggests that the protein may have DNA-binding activity. The gene localizes to the major histocompatibility complex (MHC) class I region on chromosome 6.
REFERENCES
Cree, B.A., et al. PLoS ONE 5 (6), E11296 (2010) :
Barcellos, L.F., et al. PLoS Genet. 5 (10), E1000696 (2009) :
Males, S., et al. Antivir. Ther. (Lond.) 12(5):797-803(2007)
Reymond, A., et al. EMBO J. 20(9):2140-2151(2001)
Rahman, A., et al. J. Biol. Chem. 273(25):15395-15403(1998)
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