Analytical Data
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Gene name
4hbD
- Application
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Alternative Names
/
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Species
Clostridium kluyveri
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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
P38945
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Expression Region
1-371aa
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Molecular Weight
49.2 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 4hbD recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology, medicine, and structural biology. 4hbD, or four-helix bundle domain, is a type of protein motif characterized by a stable structure formed by four alpha-helices. These proteins are notable for their ability to serve as scaffolds for engineering novel biomolecules, enabling the design of proteins with specific functions or properties. The research background of 4hbD recombinant proteins encompasses the exploration of their stability, folding mechanisms, and interaction dynamics, thereby providing insights into protein design principles. Furthermore, advancements in techniques such as synthetic biology and protein engineering have facilitated the production of these proteins with enhanced functionalities, making them valuable in therapeutic applications, including targeted drug delivery and vaccine development. Overall, the investigation of 4hbD recombinant proteins represents a promising frontier in understanding protein structure and function while paving the way for innovative solutions in medicine and biotechnology.
