Analytical Data
-
Gene name
ASS
- Application
-
Alternative Names
ASS ; Ass-1; ass1; ASSA; ASSY_HUMAN
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P00966
-
Expression Region
1-412aa
-
AA Sequence
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK
-
Molecular Weight
46 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of ASS (argininosuccinate synthase) recombinant protein has gained significant attention due to its critical role in the urea cycle, a fundamental metabolic pathway responsible for detoxifying ammonia in the liver. ASS catalyzes the conversion of citrulline and aspartate into argininosuccinate, playing a vital role in arginine biosynthesis and nitrogen metabolism. Deficiencies in ASS can lead to argininosuccinic aciduria, a rare genetic disorder associated with elevated ammonia levels, neurological impairment, and a decreased quality of life. Recent advancements in recombinant DNA technology have enabled the production of ASS in heterologous systems, allowing for in-depth functional studies and the exploration of its structural properties. Understanding the molecular characteristics and kinetic properties of ASS through recombinant protein approaches can provide insights into its mechanisms of action and potential therapeutic applications. Moreover, these studies can facilitate the development of novel treatments for metabolic disorders associated with impaired urea cycle function. The exploration of ASS recombinant protein not only contributes to the fundamental understanding of metabolic pathways but also opens avenues for innovative biotechnological applications, including gene therapy and enzyme replacement therapies. As such, the research on ASS recombinant protein serves as a pivotal avenue in addressing metabolic disorders and enhancing our understanding of human physiology.











