Analytical Data
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Gene name
Animal-Free MMP-2
- Application
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Alternative Names
CLG4; CLG4A; MMP-II; MONA; TBE-1; PEX; Gelatinase A; 72kDa Gelatinase; 72kDa Type IV Collagenase
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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 95% as determined by SDS-PAGE.
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Uniprot
P08253
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Expression Region
Ala30~Cys660
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Molecular Weight
75kDa
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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-2 (MMP-2) is a key enzyme involved in the remodeling of the extracellular matrix, playing a critical role in various physiological processes, such as tissue repair, angiogenesis, and cell migration, as well as pathological conditions, including cancer metastasis and fibrosis. Traditionally, MMP-2 has been sourced from animal tissues, posing ethical concerns, variability in yield, and risks of contamination with pathogens. The development of animal-free recombinant proteins has emerged as a pioneering approach to overcome these limitations. Through biotechnological advancements, researchers can now utilize expression systems such as yeast, bacteria, or plant cells to produce MMP-2 in a controlled, reproducible manner. This not only ensures higher purity and consistency but also addresses ethical issues associated with animal use. Additionally, animal-free production methods facilitate easier scalability and enable the potential for post-translational modifications that enhance the enzymatic activity and stability of the protein. The growing interest in recombinant MMP-2 is underscored by its therapeutic potential in treating fibrotic diseases, cardiovascular disorders, and cancer, making it a valuable focus of research in biomedicine and biotechnology. The shift towards animal-free methods marks a significant advancement in the production of biopharmaceuticals, aligned with global trends toward sustainability and ethical responsibility in scientific research.
