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。
Anti-TRIF Antibody
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Application 
| WB |
|---|---|
| Primary Accession | Q80UF7 |
| Host | Rabbit |
| Reactivity | Mouse |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for TIR domain-containing adapter molecule 1(TICAM1) detection. Tested with WB in Mouse. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 106759 |
|---|---|
| Other Names | TIR domain-containing adapter molecule 1, TICAM-1, Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta, TIR domain-containing adapter protein inducing IFN-beta, Ticam1, Trif |
| Calculated MW | 79230 Da |
| Application Details | Western blot, 0.1-0.5 µg/ml, Mouse |
| Subcellular Localization | Cytoplasmic vesicle, autophagosome . Colocalizes with UBQLN1 in the autophagosome. . |
| Source | Eukaryota |
| Protein Name | TIR domain-containing adapter molecule 1 |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of mouse TRIF(693-708aa NNHMWGHTGAQSSDDK). |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| Sequence Similarities | Contains 1 TIR domain. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | Ticam1 |
|---|---|
| Synonyms | Trif |
| Function | Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF- kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis (PubMed:12855817, PubMed:16002681, PubMed:21703541). Ligand binding to these receptors results in TRIF recruitment through its TIR domain (PubMed:12855817, PubMed:16002681, PubMed:21703541). Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively (PubMed:12855817, PubMed:16002681, PubMed:21703541). Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens (By similarity). Component of a multi-helicase- TICAM1 complex that acts as a cytoplasmic sensor of viral double- stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines (PubMed:21703541). |
| Cellular Location | Cytoplasm, cytosol. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8IUC6} Mitochondrion. Note=Colocalizes with UBQLN1 in the autophagosome. Colocalizes in the cytosol with DDX1, DDX21 and DHX36 (PubMed:21703541). Colocalizes in the mitochondria with DDX1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-helicase- TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA ligand stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q8IUC6, ECO:0000269|PubMed:21703541} |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
TICAM1(TIR DOMAIN-CONTAINING ADAPTOR MOLECULE 1), also known as TRIF, is an adapter in responding to activation of toll-like receptors(TLRs). It mediates the rather delayed cascade of two TLR-associated signaling cascades, where the other one is dependent upon a MyD88 adapter. By genomic sequence analysis, Oshiumi et al.(2003) mapped the TICAM1 gene to chromosome 19p13.3. By coimmunoprecipitation analysis, Oshiumi et al.(2003) showed that TICAM1 interacts specifically with TLR3, but not with other TLRs. Functional analysis showed that the association of TLR3 and TICAM1 mediates dsRNA activation of IFNB, through either NFKB, AP1, or IRF3. TICAM1 activation of NFKB was found to occur predominantly through IRAK1 rather than IRAK2 . Small interfering(si)RNA blockage of TICAM1, just upstream of the TIR domain, reduced IFNB production in response to dsRNA.
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