Analytical Data
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Gene name
ctfB
- Application
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Alternative Names
Acetoacetyl-CoA:acetate/butyrate CoA-transferase subunit B (Coat B)
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Species
Clostridium acetobutylicum
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23673
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Expression Region
1-221aa
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Molecular Weight
30.6 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
CTFB (C-Terminal Fragment of B) recombinant protein has gained significant attention in recent years due to its potential applications in various fields, including biotechnology, medicine, and molecular biology. CTFB is derived from larger proteins and often retains functional domains that play critical roles in cellular processes. Research into CTFB focuses on its mechanisms of action, its interaction with other biomolecules, and its influence on signal transduction pathways. Studies have shown that CTFB can be involved in modulating gene expression, influencing stress responses, and participating in cellular signaling cascades. Furthermore, its stability and ease of production as a recombinant protein make it a valuable tool for investigating protein function and for developing therapeutic strategies. The ongoing exploration of CTFB's properties may lead to novel insights into cellular dynamics and pathways involved in diseases, ultimately paving the way for innovative treatments in areas such as cancer therapy and regenerative medicine. Overall, the study of CTFB recombinant protein presents a promising frontier in the pursuit of understanding intricate biological systems and developing cutting-edge biotechnological solutions.
