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。
RB1 Antibody (Center S249)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- 背景知识
Application 
| WB, E |
|---|---|
| Primary Accession | P06400 |
| Other Accession | NP_000312.2 |
| Reactivity | Human, Rat, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 106159 Da |
| Antigen Region | 227-256 aa |
| Gene ID | 5925 |
|---|---|
| Other Names | Retinoblastoma-associated protein, p105-Rb, pRb, Rb, pp110, RB1 |
| Target/Specificity | This RB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 227-256 amino acids from the Central region of human RB1. |
| 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 | RB1 Antibody (Center S249) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | RB1 |
|---|---|
| Function | Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin- modifying enzymes that actively repress transcription (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed:10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1- dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). |
| Cellular Location | Nucleus. Cytoplasm {ECO:0000250|UniProtKB:P13405}. Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization (PubMed:20940255). Localizes to the cytoplasm when hyperphosphorylated (By similarity). {ECO:0000250|UniProtKB:P13405, ECO:0000269|PubMed:20940255} |
| Tissue Location | Expressed in the retina. Expressed in foreskin keratinocytes (at protein level) (PubMed:20940255) |
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 negative regulator of the cell cycle and was the first tumor suppressor gene found. The encoded protein also stabilizes constitutive heterochromatin to maintain the overall chromatin structure. The active, hypophosphorylated form of the protein binds transcription factor E2F1. Defects in this gene are a cause of childhood cancer retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.
REFERENCES
Liao, C.C., et al. J. Biol. Chem. 285(43):33134-33143(2010)
Kim, T.R., et al. Biochem. Biophys. Res. Commun. 400(1):100-105(2010)
Hirschi, A., et al. Nat. Struct. Mol. Biol. 17(9):1051-1057(2010)
Tooley, C.E., et al. Nature 466(7310):1125-1128(2010)
Dimaras, H., et al. Transl Res 156(2):91-97(2010)
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