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。
Phospho-mouse TSC1(S387) Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- 背景知识
Application 
| DB, E |
|---|---|
| Primary Accession | Q9EP53 |
| Other Accession | Q9Z136, NP_075025.2 |
| Reactivity | Mouse |
| Predicted | Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 128746 Da |
| Gene ID | 64930 |
|---|---|
| Other Names | Hamartin, Tuberous sclerosis 1 protein homolog, Tsc1, Kiaa0243 |
| Target/Specificity | This mouse TSC1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S387 of mouse TSC1. |
| Dilution | DB~~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 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 | Phospho-mouse TSC1(S387) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | Tsc1 {ECO:0000303|PubMed:11130985, ECO:0000312|MGI:MGI:1929183} |
|---|---|
| Function | Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12820960). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12820960). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12820960). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (By similarity). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (By similarity). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (PubMed:16707451). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (By similarity). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (By similarity). |
| Cellular Location | Lysosome membrane {ECO:0000250|UniProtKB:Q92574}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92574}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92574}. Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients. In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol. {ECO:0000250|UniProtKB:Q92574} |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling (By similarity). Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling (By similarity).
REFERENCES
Kladney, R.D., et al. Cancer Res. 70(21):8937-8947(2010)
Sathaliyawala, T., et al. Immunity 33(4):597-606(2010)
Scott, C.L., et al. Am. J. Physiol. Lung Cell Mol. Physiol. 299 (4), L455-L471 (2010) :
Bartolome, A., et al. Endocrinology 151(7):3084-3094(2010)
Squarize, C.H., et al. PLoS ONE 5 (5), E10643 (2010) :
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