Analytical Data
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Gene name
metalloendopeptidase
- Application
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Alternative Names
Beta-lytic protease
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Species
Lysobacter enzymogenes
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00801
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Expression Region
1-178aa
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Molecular Weight
35.1 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
Metalloendopeptidases are a class of zinc-dependent enzymes that play crucial roles in various biological processes by cleaving peptide bonds in protein substrates. These enzymes are involved in protein degradation, cellular signaling, and the processing of hormones and neurotransmitters. The relevance of metalloendopeptidases extends to several physiological and pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders. Given their significant roles, there is substantial interest in understanding their structure, function, and mechanisms of action. Recombinant protein technology has emerged as a powerful tool to study metalloendopeptidases, enabling the production of these enzymes in a controlled environment. By utilizing techniques such as molecular cloning and expression in host systems like bacteria or yeast, researchers can obtain large quantities of purified enzymes for detailed biochemical analyses. Moreover, recombinant metalloendopeptidases can be engineered to enhance their stability, activity, or specificity, facilitating the development of novel therapeutic agents or diagnostic tools. Overall, the study of recombinant metalloendopeptidases is pivotal for advancing our knowledge of their biological functions and for exploring their potential applications in biotechnology and medicine.
