Recombinant Human ASS1 protein (His tag N-Terminus)
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Recombinant Human ASS1 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 412 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
ASS, ASS1, Argininosuccinate synthase, Citrulline--aspartate ligase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human ASS1 protein (His tag N-Terminus) (AB98084)
15% SDS-PAGE analysis of ab98084 (3μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Argininosuccinate synthase 1 contributes significantly to the synthesis of arginine an essential amino acid through its conversion activities. The enzyme operates as a homotrimer a complex consisting of three identical subunits. This enzymatic activity is indispensable in maintaining the balance of nitrogen and ammonia within the body particularly important for liver and kidney functions.
Pathways
ASS1 is a critical component of both the urea cycle and the nitric oxide metabolism pathway. The urea cycle helps in detoxifying ammonia by converting it into urea which is excreted in urine. In nitric oxide metabolism ASS1 links with nitric oxide synthase to facilitate the use of arginine in producing nitric oxide a vital signaling molecule. The pathway engagement partners include proteins like citrin which supplies aspartate for the reaction.
Specifications
Form
Liquid
Additional notes
ab98084 was purified using conventional chromatography techniques.
General info
Function
One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.
Sequence similarities
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Post-translational modifications
Acetylated by CLOCK in a circadian manner which negatively regulates its enzyme activity. Deacetylated by histone deacetylases.
Target data
Product promise
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