Analytical Data
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Gene name
KYNA
- Application
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Alternative Names
KYNA;G-Protein coupled receptor 35
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HC97
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Expression Region
1-309aa
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AA Sequence
MNGTYNTCGSSDLTWPPAIKLGFYAYLGVLLVLGLLLNSLALWVFCCRMQQWTETRIYMTNLAVADLCLLCTLPFVLHSLRDTSDTPLCQLSQGIYLTNRYMSISLVTAIAVDRYVAVRHPLRARGLRSPRQAAAVCAVLWVLVIGSLVARWLLGIQEGGFCFRSTRHNFNSMAFPLLGFYLPLAVVVFCSLKVVTALAQRPPTDVGQAEATRKAARMVWANLLVFVVCFLPLHVGLTVRLAVGWNACALLETIRRALYITSKLSDANCCLDAICYYYMAKEFQEASALAVAPSAKAHKSQDSLCVTLA
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Molecular Weight
34 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
Kynurenine (KYNA) is a significant metabolite in the kynurenine pathway, which is involved in the metabolism of tryptophan. This pathway plays a crucial role in various physiological and pathological processes, including neurodegeneration, cancer, and immune responses. Recent studies have highlighted the importance of KYNA as a neuroprotective agent due to its ability to modulate glutamate receptor activity and reduce excitotoxicity, a key factor in neurological disorders such as Alzheimer’s disease and schizophrenia. The exploration of KYNA's structure and function has led to interest in the development of recombinant proteins that can mimic or enhance its activity. Researchers aim to produce KYNA in a more controlled and scalable manner using recombinant DNA technology, which allows for the precise modification of KYNA’s biochemical properties. This approach seeks to improve our understanding of KYNA's mechanisms of action and develop therapeutic applications targeting various diseases associated with altered tryptophan metabolism. The study of KYNA as a recombinant protein is still in its early stages, but it holds promise for advancing our knowledge of its role in health and disease, potentially paving the way for novel treatments that leverage its neuroprotective characteristics while addressing challenges such as specificity and bioavailability in therapeutic contexts.











