Analytical Data
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Gene name
MMP-10
- Application
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Alternative Names
STMY2; SL2; Stromelysin 2; Transin-2
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
O55123
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Expression Region
Glu154~Ser472
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Molecular Weight
40kDa
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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
Matrix metalloproteinase-10 (MMP-10), also known as stromelysin-2, is a crucial enzyme involved in the degradation of extracellular matrix components and plays a significant role in various physiological and pathological processes, including tissue remodeling, wound healing, and inflammatory responses. Overexpression of MMP-10 has been implicated in several diseases, such as cancer metastasis, cardiovascular diseases, and chronic inflammatory conditions. Research into MMP-10 has garnered attention due to its potential as a biomarker for disease progression and its viability as a therapeutic target. Recombinant MMP-10 protein production has facilitated detailed studies of its structure, function, and interaction with other molecules, providing valuable insights into its regulatory mechanisms. Understanding the role of MMP-10 in disease processes could lead to innovative strategies for treatment and prevention. Moreover, the development of MMP-10 inhibitors might offer novel therapeutic options for conditions characterized by excessive matrix degradation. The ongoing exploration of MMP-10's functions through recombinant technologies emphasizes its relevance in biomedical research, paving the way for new interventions that leverage this enzyme's unique properties.
