Analytical Data
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Gene name
mtnN
- Application
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Alternative Names
mtnN；mtn；pfs；yadA；5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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Species
Human
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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
A7ZWA7
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Expression Region
1-232aa
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AA Sequence
MKIGIIGAMEEEVTLLRDKIEKRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
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Molecular Weight
31.8 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 mtnN recombinant proteins is grounded in the quest to understand the biosynthetic pathways of microbial natural products, particularly in the context of antibiotics and other bioactive compounds. mtnN encodes a key enzyme involved in the biosynthesis of nocardicin, a potent antibiotic derived from the actinomycete Nocardia lactamdurans. Research has shown that mtnN plays a crucial role in the enzymatic processes that modify and assemble amino acid precursors into nocardicin, thereby influencing the compound's biological activity. Given the rising issue of antibiotic resistance, exploring such biosynthetic pathways not only enhances our fundamental understanding of microbial metabolism but also holds the potential for discovering novel antibiotics. By producing mtnN recombinant proteins in laboratory settings, researchers aim to elucidate the function and mechanism of this enzyme, paving the way for genetic manipulation and biotechnological applications that could lead to the development of new therapeutic agents. Overall, the investigation of mtnN and its resultant protein products represents a significant step toward harnessing microbial diversity for drug discovery and addressing pressing public health challenges.
