Analytical Data
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Gene name
ACB1
- Application
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Alternative Names
ACB1；Acyl-CoA-binding domain-containing Protein 4
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31787
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Expression Region
1-87aa
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AA Sequence
MVSQLFEEKAKAVNELPTKPSTDELLELYALYKQATVGDNDKEKPGIFNMKDRYKWEAWENLKGKSQEDAEKEYIALVDQLIAKYSS
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Molecular Weight
12.1 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
ACB1 (Aspergillus cellobiohydrolase B1) is a crucial enzyme involved in cellulose degradation, playing a significant role in the bioconversion of lignocellulosic biomass to fermentable sugars. With the rising demand for sustainable energy sources, research into ACB1 recombinant proteins has garnered considerable attention due to their potential applications in biofuel production and bioremediation. The ability of ACB1 to efficiently hydrolyze cellulosic materials is vital for improving the efficiency of enzymatic biomass conversion processes. Moreover, advancements in genetic engineering techniques allow for the optimization of ACB1 expression and activity, enhancing its properties for industrial applications. Studies have focused on various expression systems, including heterologous organisms, to produce ACB1 in large quantities with desired modifications that can improve its stability and activity under industrial conditions. Overall, ACB1 recombinant protein research not only strengthens our understanding of cellulase enzymes but also paves the way for innovative solutions in waste management and renewable energy sectors, aligning with global sustainability goals.
