Analytical Data
-
Gene name
Stromelysin-1/MMP-3
- Application
-
Alternative Names
SL1; STMY; STMY1; STR1; Progelatinase; Stromelysin 1; Transin-1
-
Species
Pig
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
F1SV58
-
Expression Region
Tyr18~Cys477
-
Molecular Weight
56kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Stromelysin-1, also known as matrix metalloproteinase-3 (MMP-3), is a key enzyme involved in the degradation of extracellular matrix components, playing a critical role in tissue remodeling and repair. Research on MMP-3 has gained substantial attention due to its implications in various pathological conditions, including arthritis, cancer metastasis, and cardiovascular diseases. MMP-3 is produced as an inactive proenzyme and requires activation to exert its proteolytic functions. Recombinant protein technology has facilitated the production of MMP-3 for both functional studies and therapeutic applications. Understanding the structure and activity of recombinant Stromelysin-1 is crucial for investigating its biological roles and regulatory mechanisms in health and disease. Enhanced levels of MMP-3 have been associated with inflammatory processes and the progression of tissue degeneration, making it a potential biomarker for disease monitoring and a target for developing novel therapeutic strategies. Furthermore, the availability of purified recombinant MMP-3 allows for high-throughput screening of inhibitors and the study of its interactions with various substrates. Given the significance of MMP-3 in maintaining tissue homeostasis and its involvement in pathological states, ongoing research endeavors aim to elucidate its precise functions, regulation, and potential as a target for intervention in disease.
