Recombinant Human ASS1 Protein (His Tag) supplied by Elabscience with collaborator-provided technical specifications.
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Recombinant Human ASS1 Protein (His Tag) is a research-use recombinant protein from Elabscience preparation representing ASS1 supplied as Liquid. 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.
Argininosuccinate synthase 1 (ASS1; argininosuccinate synthase) is a cytosolic urea-cycle enzyme that catalyzes ATP-dependent formation of argininosuccinate from citrulline and aspartate. This catalogue-backed ABMIUM record links human ASS1 (NCBI Gene 445; UniProt P00966) to research reagents.
Biological function: ASS1 catalyzes the ATP-dependent condensation of citrulline and aspartate to form argininosuccinate. This reaction is a core urea-cycle step and, together with argininosuccinate lyase, contributes to endogenous arginine biosynthesis.
