Recombinant Human MMP3 Protein (His Tag) supplied by Elabscience with collaborator-provided technical specifications.
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Recombinant Human MMP3 Protein (His Tag) is a research-use recombinant protein from Elabscience preparation representing MMP3 supplied as Lyophilized. Review the expression, purity, formulation and storage specifications below before selecting it for an assay or functional workflow.
Fully tested in-house by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species | Bioactivity | Binding | Cell-Based | In Vivo | ELISA Capture |
|---|---|---|---|---|---|
| Human |
This product is manufactured by Elabscience and sold through ABMIUM without relabelling.
ABMIUM supports global orders. Availability, shipping requirements and applicable import arrangements are confirmed before fulfilment where required.
Yes. Send your target, sample, application and experimental conditions through ABMIUM MATCH or technical support.
Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
Matrix metallopeptidase 3 (MMP3), also known as matrix metalloproteinase-3 or stromelysin-1, is a secreted extracellular-matrix protease. This ABMIUM record connects NCBI Gene 4314 and UniProtKB P08254 to catalogue-backed research products.
Biological function: Matrix metallopeptidase 3 (MMP3/stromelysin-1) is a zinc-dependent extracellular protease with broad substrate specificity. It can degrade multiple extracellular-matrix components, including fibronectin and laminin, and can process or activate other proteins including matrix metalloproteinases.
