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Brand: ProteoGenix

Recombinant Human KYAT1 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
44.71 kDa

$392.00

100ug + 392 loyalty points
Met1–Leu372
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Recombinant Human KYAT1 Protein, N-His

Recombinant Human KYAT1 Protein, N-His

Product name Recombinant Human KYAT1 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 44.71 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Met1-Leu372
Aliases /Synonyms Kynurenine--oxoglutarate transaminase 1; 2.6.1.7; Cysteine-S-conjugate beta-lyase; 4.4.1.13; Glutamine transaminase K; GTK; Glutamine--phenylpyruvate transaminase; 2.6.1.64; Kynurenine aminotransferase 1; Kynurenine aminotransferase I; KATI; Kynurenine--oxoglutarate transaminase I; KYAT1; CCBL1
Reference ARO-P12343
Note For research use only.
Molecular Constructor
Met1–Leu372

Introduction

Recombinant proteins are proteins that are produced through genetic engineering techniques, where the DNA sequence of a specific protein is inserted into a host organism, such as bacteria or yeast, to produce large quantities of the desired protein. One such recombinant protein is the Recombinant Human KYAT1 Protein, which has gained significant attention in the scientific community due to its unique structure, activity, and potential applications.

Structure of Recombinant Human KYAT1 Protein

The Recombinant Human KYAT1 Protein, also known as Kynurenine aminotransferase 1, is a 48-kDa protein that consists of 422 amino acids. It is a member of the aminotransferase family and is highly conserved among different species, including humans, mice, and rats. The protein has a pyridoxal phosphate (PLP) binding site, which is essential for its enzymatic activity.

Activity of Recombinant Human KYAT1 Protein

The primary function of Recombinant Human KYAT1 Protein is to catalyze the conversion of kynurenine, an amino acid derived from tryptophan, to kynurenic acid. This reaction is a crucial step in the kynurenine pathway, which is involved in the metabolism of tryptophan and plays a significant role in immune regulation, neuroprotection, and neurotransmission. The activity of KYAT1 protein is dependent on the presence of PLP, which acts as a cofactor and is required for the proper folding and stability of the protein.

Applications of Recombinant Human KYAT1 Protein

Recombinant Human KYAT1 Protein has a wide range of potential applications in various fields, including biomedical research and drug development. One of the significant applications of this protein is in studying the kynurenine pathway and its role in various diseases, such as cancer, neurodegenerative disorders, and autoimmune diseases. The overexpression or inhibition of KYAT1 protein can provide valuable insights into the mechanisms underlying these diseases and help in the development of potential therapeutic strategies.

Another potential application of Recombinant Human KYAT1 Protein is in the production of kynurenic acid, which has been shown to have neuroprotective and anti-inflammatory properties. Kynurenic acid has been studied for its potential use in the treatment of neurological disorders, such as Alzheimer’s disease and Parkinson’s disease. The use of KYAT1 protein for the large-scale production of kynurenic acid can provide a cost-effective and efficient method for obtaining this valuable compound.

Conclusion

In summary, Recombinant Human KYAT1 Protein is a unique protein with a specific structure and activity that plays a crucial role in the kynurenine pathway. Its potential applications in biomedical research and drug development make it a valuable tool for studying and understanding various diseases. With further research and development, this protein has the potential to contribute significantly to the advancement of medicine and improve human health.

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