Preparation and Storage
推奨アッセイ手順
Western blot: Please refer to http://www.bdbiosciences.com/support/resources/cell_biology/index.jsp
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Id proteins were originally characterized as inhibitors of DNA binding and cell differentiation. Id1 through 4 contain an evolutionarily conserved helix-loop-helix (HLH) sequence which is critical for protein-protein interaction(s). Most HLH transcription factors contain a basic amino acid region adjacent to the HLH sequence, the bHLH sequence, which is responsible for DNA binding. bHLH transcription factors fall into 2 major groups designated class A factors, e.g., E2.2 and E47, and class B factors, e.g., MyoD, myogenin. In vitro studies demonstrate distinct interaction(s) between Id proteins and bHLH transcription factors. While Id proteins contain an HLH domain, they lack the basic region which is required for DNA binding. Therefore, Id proteins are negative regulators of transcription since complexes which contain them do not bind DNA. Id proteins are variably expressed throughout the cell cycle and are regulated by phosphorylation by cyclin-cdk complexes. Thus, Id proteins play an important role in transcriptional regulation of cell cycle related genes. Overexpression of Id1 can induce apoptosis in serum-starved fibroblasts and is correlated with cell cycle progression promoted by Id family members. For example, Id2 can reverse the cell cycle block provided by retinoblastoma protein (Rb) via direct interaction between Id2 and Rb. Clone B31.1 has been reported to recognize mouse Id2, but does not crossreact with mouse Id1 or mouse Id3.
Development References (8)
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Cooper CL, Brady G, Bilia F, Iscove NN, Quesenberry PJ. Expression of the Id family helix-loop-helix regulators during growth and development in the hematopoietic system. Blood. 1997; 89(9):3155-3165. (Biology). View Reference
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Hara E, Hall M, Peters G. Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors. EMBO J. 1997; 16(2):332-342. (Biology). View Reference
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Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA. The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein. Genes Dev. 1994; 8(11):1270-1284. (Biology). View Reference
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Kadesch T. Consequences of heteromeric interactions among helix-loop-helix proteins. Cell Growth Differ. 1993; 4(1):49-55. (Biology). View Reference
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Langlands K, Yin X, Anand G, Prochownik EV. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J Biol Chem. 1997; 272(32):19785-19793. (Biology). View Reference
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Norton JD, Atherton GT. Coupling of cell growth control and apoptosis functions of Id proteins. Mol Cell Biol. 1998; 18(4):2371-2381. (Biology). View Reference
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Norton JD, Deed RW, Craggs G, Sablitzky F. Id helix-loop-helix proteins in cell growth and differentiation. Trends Cell Biol. 1998; 8(2):58-65. (Biology). View Reference
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Riechmann V, van Crüchten I, Sablitzky F. The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3. Nucleic Acids Res. 1994; 22(5):749-755. (Biology). View Reference
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