Analytical Data
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Gene name
MMP-7
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简介
MMP-7 proteins enzymatically degrade a variety of substrates, including casein, gelatin (types I, III, IV, and V), and fibronectin. Its proteolytic effect activates procollagenase, indicating its role in the regulation of collagen metabolism. MMP-7 Protein, Human (HEK293, His) is the recombinant human-derived MMP-7 protein, expressed by HEK293, with N-His labeled tag.
- Application
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Alternative Names
Matrilysin; Matrin; Matrix metalloproteinase-7; Pump-1 protease; MPSL1; PUMP1
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Species
Human
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Source
HEK293
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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
P09237
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Expression Region
L18-K267
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Protein Length
Full Length of Mature Protein
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Molecular Weight
30 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
MMP-7, or Matrix Metalloproteinase-7, is a crucial enzyme belonging to the matrix metalloproteinase (MMP) family, which plays a significant role in the degradation of extracellular matrix components. This enzyme has garnered considerable interest in biomedical research due to its involvement in various physiological and pathological processes, including tissue remodeling, wound healing, and inflammation. Dysregulation of MMP-7 expression has been linked to several diseases, particularly cancer, where it contributes to tumor progression and metastasis by facilitating the degradation of the extracellular matrix and influencing cell migration. Additionally, MMP-7 has been implicated in degenerative diseases, cardiovascular conditions, and inflammatory disorders. As a result, researchers are focusing on the development of MMP-7 reprogrammed proteins for potential therapeutic applications, including drug design and gene therapy. By understanding the structure, function, and regulatory mechanisms of MMP-7, scientists aim to uncover novel targets for intervention, improving treatment strategies for diseases associated with abnormal MMP activity. Overall, the study of MMP-7 recombinant proteins is essential for advancing our knowledge of matrix biology and the development of innovative therapeutic approaches.
