Analytical Data
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Gene name
amiF
- Application
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Alternative Names
amiF；Formamidase
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Species
Bradyrhizobium
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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
A4Z3G9
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Expression Region
1-337aa
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AA Sequence
MNGLGGLNKSEHGVVIGLVQLQLPVVVTKEDLAKQTEKIVWMVGKARRNLGTMDLVVFPEYSLHGLSMDTNPEIMCRLDGPEVAAFKQACIDNKIWGCFSIMEYNPDGNPYNSGLIIDSNGEIKLYYRKLHPWIPVEPWEPGDLGIPVIEGPRGAKIALIICHDGMFPEMARECAYKGAEIMIRTAGYTAPIRDSWRFTNQANAFQNLMVTANVCMCGSDGSFDSMGEGMIVNFDGSILAHGTTGRADEIITAEVRPDLVREARIGWGVENNIYQLWHRGYVAVKGGAMDCPYTFMHDMVAGTYRLPWEDQVKITDGTSCGFPAPTRVFGKMAKAAE
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Molecular Weight
53.2 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 amiF recombinant proteins has gained significant attention due to their potential applications in various biotechnological and pharmaceutical fields. amiF, a gene encoding for an amidohydrolase enzyme, is involved in the hydrolysis of amides, playing a crucial role in metabolic pathways across different organisms. Understanding the structure and function of amiF can provide insights into its catalytic mechanisms, which are essential for designing enzyme inhibitors or enhancing enzyme activity for industrial applications. Furthermore, the production of amiF recombinant proteins allows for the exploration of their properties in controlled environments, facilitating the development of improved biocatalysts. As industries increasingly seek sustainable and efficient processes, the ability to harness and modify these enzymes can lead to breakthroughs in bioprocessing and drug development. The exploration of amiF in therapeutic contexts, particularly for its potential use in treating conditions linked to amide metabolism, illustrates the relevance of this research. Overall, the investigation of amiF recombinant proteins holds promise for advancing our understanding of enzymatic functions and developing innovative solutions for pressing challenges in health and biotechnology.
