Analytical Data
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Gene name
ID2
- Application
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Alternative Names
Class B basic helix-loop-helix protein 26 ;bHLHb26Inhibitor of DNA binding 2Inhibitor of differentiation 2
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q02363
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Expression Region
1-134aa
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Molecular Weight
30.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of ID2 (Inhibitor of DNA Binding 2) recombinant proteins has gained significant attention in recent years due to ID2's crucial role in cellular processes such as differentiation, proliferation, and tumorigenesis. ID2, a member of the ID (inhibitor of differentiation) family, acts as a dominant-negative regulator of basic helix-loop-helix (bHLH) transcription factors, thereby influencing gene expression patterns essential for development and cell identity. Abnormal expression of ID2 is associated with various cancers, making it a potential biomarker and therapeutic target. Researchers are increasingly utilizing recombinant DNA technology to produce ID2 proteins, allowing for detailed biophysical characterization, functional analyses, and exploration of its interactions with other proteins. Understanding the structure and function of ID2 at a molecular level can facilitate the development of targeted therapies aimed at modulating its activity in disease contexts. Overall, the investigation of ID2 recombinant proteins is poised to provide valuable insights into the molecular mechanisms of cell fate decisions and offer new avenues for cancer treatment strategies.
