Recombinant Human ALPP Protein(His Tag) supplied by Elabscience with collaborator-provided technical specifications.
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Recombinant Human ALPP Protein(His Tag) is a research-use recombinant protein from Elabscience preparation representing ALPP 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.
ALPP (alkaline phosphatase, placental), commonly called placental alkaline phosphatase (PLAP), encodes a placental-type alkaline phosphatase studied in phosphomonoesterase activity, placental biology and lineage-associated expression.
Biological function: Placental alkaline phosphatase is a metalloenzyme that hydrolyses phosphate monoesters. The mature ALPP/PLAP enzyme functions as a homodimer and uses metal cofactors at its catalytic site, making it a useful target for studying extracellular alkaline-phosphatase activity and placental-type phosphatase biology.
