Analytical Data
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Gene name
CMAHP
- Application
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Alternative Names
(CMP-NeuAc hydroxylase-like protein)(Cytidine monophosphate-N-acetylneuraminic acid hydroxylase pseudogene)
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Species
Human
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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
Q9Y471
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Expression Region
1-501aa
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Molecular Weight
63.4 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
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Protein Description
CMAHP (Cyanobacterial Mycobacterial Alpha-Helical Protein) is a protein of significant interest in the field of synthetic biology and biochemistry due to its unique structural properties and functional roles. Originally identified in cyanobacteria, CMAHP exhibits an alpha-helical structure that is believed to play a crucial role in cellular processes and interactions. The study of CMAHP is driven by its potential applications in various industrial and medical fields, including drug delivery systems, enzyme design, and biocatalysis. The ability to recombine and express CMAHP in heterologous systems enhances its availability for detailed functional studies, enabling researchers to explore its biochemical pathways and interactions with other proteins. Moreover, understanding the mechanisms that govern CMAHP’s stability and activity can lead to the development of innovative biotechnological applications. With advances in molecular cloning techniques and expression systems, the re-engineering of CMAHP for enhanced performance is becoming increasingly feasible. This research not only contributes to the fundamental understanding of protein folding and function but also paves the way for the development of novel biomaterials and therapeutic agents. The ongoing exploration of CMAHP represents a promising frontier in protein science, highlighting the importance of natural proteins in the advancement of biotechnological applications.
