Recombinant Human GLUD1 protein (denatured) (His tag N-Terminus)
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Recombinant Human GLUD1 protein (denatured) (His tag N-Terminus) is a Human Full Length protein, in the 54 to 558 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.
View Alternative Names
GLUD, GLUD1, GDH 1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human GLUD1 protein (denatured) (His tag N-Terminus) (AB180318)
15% SDS-PAGE analysis of ab180318 (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
GLUD1 facilitates nitrogen and carbon homeostasis through its role in amino acid breakdown and energy metabolism. Although not part of a complex GLUD1's activity impacts central metabolic processes influencing cellular energy status and neurotransmitter regulation. The enzyme contributes to the glutamate-glutamine cycle which is important for neurotransmission in the brain. Its regulation by ADP GDP and other molecules enables cells to adapt to energetic demands.
Pathways
GLUD1 is integral to the tricarboxylic acid (TCA) cycle and urea cycle impacting both energy production and detoxification of ammonia. In the TCA cycle GLUD1 influences the availability of α-ketoglutarate interfacing with enzymes such as isocitrate dehydrogenase. In the urea cycle it aids in converting ammonia to urea in the liver. Additionally GLUD1's function connects with glutamine synthetase in managing amino acid synthesis and degradation.
Specifications
Form
Liquid
General info
Function
Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed : 11032875, PubMed : 11254391, PubMed : 16023112, PubMed : 16959573). Plays a role in insulin homeostasis (PubMed : 11297618, PubMed : 9571255). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).
Sequence similarities
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Post-translational modifications
ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity (PubMed:16959573). Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer (PubMed:16023112).
Subcellular localisation
Mitochondrion
Target data
Product promise
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