Analytical Data
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Gene name
acm
- Application
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Alternative Names
1,4-beta-N-acetylmuramidase M1
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Species
Streptomyces globisporus
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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
P25310
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Expression Region
78-294aa
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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
The study of acyl-CoA-binding proteins (ACBP) and their restructured variants has gained significant attention in recent years due to their essential roles in lipid metabolism and cellular energy homeostasis. ACBP is known to facilitate the transport of acyl-CoA esters, which are vital intermediates in fatty acid metabolism, thereby influencing various physiological processes including energy production, signaling pathways, and membrane synthesis. Restructuring these proteins through techniques such as site-directed mutagenesis or protein engineering aims to enhance their stability, binding affinity, and specificity for different acyl-CoA substrates. This can lead to a better understanding of the molecular mechanisms underlying lipid-related diseases, including obesity, diabetes, and cardiovascular disorders. Furthermore, engineered ACBP variants could serve as valuable tools in metabolic engineering and synthetic biology, potentially aiding in the development of novel therapeutic strategies. As research progresses, the implications of ACBP manipulation extend beyond basic biology, presenting opportunities for biotechnological applications in health and disease management.
