Rekombinantes humanes ADAM12-Protein (His-Tag) von Elabscience, geliefert mit vom Kooperationspartner bereitgestellten technischen Spezifikationen.
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Recombinant Human ADAM12 Protein (His Tag) is a research-use recombinant protein from Elabscience preparation representing ADAM12 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 | Bioaktivität | Bindung | Zellbasiert | 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.
ADAM metallopeptidase domain 12 (ADAM12), also known as meltrin-alpha/MLTN, is a disintegrin and metalloprotease-family protein with membrane-bound and secreted isoforms. This ABMIUM record links verified ADAM12 biology with catalogue-backed research products.
Biological function: ADAM12 is a zinc-dependent metalloprotease/disintegrin associated with cell adhesion and proteolysis. Reviewed UniProt annotation supports roles in skeletal-muscle regeneration and cell fusion and, by similarity, formation of osteoclasts and macrophage-derived giant cells.
