Analytical Data
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Gene name
metalloproteinase
- Application
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Alternative Names
PEP1 PRO A
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Species
Legionella pneumophila
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21347
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Expression Region
208-543aa
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Molecular Weight
41.8 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
Metalloproteinases, particularly matrix metalloproteinases (MMPs), are a family of zinc-dependent endopeptidases that play crucial roles in various physiological and pathological processes, including tissue remodeling, wound healing, and inflammation. They are involved in the degradation of extracellular matrix (ECM) components, which is essential for normal cellular functions as well as in disease states such as cancer metastasis and arthritis. Given their significant roles, MMPs have garnered considerable interest as potential therapeutic targets. However, studying their functions and mechanisms has been challenging due to difficulties in obtaining pure and active forms of these enzymes. The advent of recombinant DNA technology has facilitated the production of metalloproteinases through expression systems, allowing for the generation of high-quality recombinant proteins. This advancement has enabled researchers to delve deeper into the biochemistry of these enzymes, investigate their substrate specificities, and explore their interactions with inhibitors. Furthermore, recombinant metalloproteinases are valuable tools for drug development and therapeutic interventions aimed at modulating their activity in disease contexts. Overall, recombinant metalloproteinase research is critical for understanding their biological roles and developing novel strategies for treating MMP-related diseases.
