Analytical Data
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Gene name
Bcl11A
- Application
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Alternative Names
BCL11A-L; BCL11A-S; BCL11A-XL; CTIP1; EVI9; Ecotropic Viral Integration Site 9; COUP-TF-interacting protein 1; Ecotropic viral integration site 9 homolog; Zinc finger protein 856
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H165
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Expression Region
Met1~Arg210
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Molecular Weight
32kDa
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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
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Protein Description
Bcl11A, a protein encoded by the BCL11A gene, plays a crucial role in various biological processes, particularly in hematopoiesis and the development of the nervous system. Initially identified for its involvement in the regulation of the transcription of beta-globin genes, Bcl11A has gained attention for its significant role in the suppression of fetal gamma-globin expression and the promotion of adult beta-globin expression, making it a potential target for therapeutic strategies in sickle cell disease and beta-thalassemia. Moreover, studies have shown that Bcl11A is essential for lymphoid cell development and has implications in the progression of certain cancers, including leukemias. Recent research has focused on characterizing Bcl11A as a transcription factor, elucidating its interactions with other proteins and understanding its regulatory networks. The generation of Bcl11A recombinant proteins facilitates structural and functional studies, offering insights into its mechanistic roles in gene regulation. Researchers are particularly interested in the development of small molecules or genetic interventions that can modulate Bcl11A activity, potentially leading to novel treatments for blood disorders and malignancies. Overall, the study of Bcl11A and its recombinant proteins is vital for unlocking new therapeutic avenues and enhancing our understanding of gene regulation in health and disease.
