Name :
Recombinant Human Aspartate Aminotransferase Protein (His Tag), HPLC-verified
Biological Activity :
Background :
GOT1 (Glutamic-Oxaloacetic Transaminase 1) is a Protein Coding gene. GOT1 belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme that exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology. GOT1 is an important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. GOT1 is broadly expressed in the heart, liver, and other tissues. Diseases associated with GOT1 include Aspartate Aminotransferase, Serum Level Of, Quantitative Trait Locus 1, and Lujo Hemorrhagic Fever.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
P17174
NCBI Gene ID :
Synonyms :
Synonyms :
glutamic-oxaloacetic transaminase 1, soluble
Amino Acid Sequence :
Molecular Weight :
The recombinant human GOT1 consists of 428 amino acids and predicts a molecular mass of 48.1 KDa. It migrates as an approximately 36-45 KDa band in SDS-PAGE under reducing conditions.
Purity :
≥ 90 % as determined by SDS-PAGE. ≥ 95 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
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.
Endotoxin Level :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the mature form of human GOT1 (P17174) (Met1-Gln413) was expressed with a polyhistidine tag at the N-terminus.
Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
ASTQTL1 Protein, Human; cAspAT Protein, Human; cCAT Protein, Human; GIG18 Protein, Human Aspartate Aminotransferase 背景信息 GOT1 (Glutamic-Oxaloacetic Transaminase 1) is a Protein Coding gene. GOT1 belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Glutamic-oxaloacetic transaminase is a pyridoxal phosphate-dependent enzyme that exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, respectively. GOT plays a role in amino acid metabolism and the urea and tricarboxylic acid cycles. The two enzymes are homodimeric and show close homology. GOT1 is an important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. GOT1 is broadly expressed in the heart, liver, and other tissues. Diseases associated with GOT1 include Aspartate Aminotransferase, Serum Level Of, Quantitative Trait Locus 1, and Lujo Hemorrhagic Fever.
References & Citations :
Shen H, et al. (2011) Genome-wide association study identifies genetic variants in GOT1 determining serum aspartate aminotransferase levels. J Hum Genet. 56(11):801-5. Doonan S, et al. (1985) Structural and genetic relationships between cytosolic and mitochondrial isoenzymes. Int J Biochem. 16(12):1193-9. Panteghini M. (1990) Aspartate aminotransferase isoenzymes. Clin Biochem. 23(4):311-9. Bousquet-Lemercier B, et al. (1990) Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 29(22):5293-9.
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