Analytical Data
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Gene name
GK2
- Application
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Alternative Names
GK2；GK2；N-acetylgalactosamine kinase
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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
Q14410
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Expression Region
2-553aa
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AA Sequence
AAPKTAAVGPLVGAVVQGTNSTRFLVFNSKTAELLSHHKVELTQEFPKEGWVEQDPKEILQSVYECIARTCEKLDELNIDISNIKAVGVSNQRETTVIWDKLTGEPLYNAVVWLDLRTQTTVEDLSKKIPGNSNFVKSKTGLPLSTYFSAVKLRWMLDNVRNVQKAVEEGRALFGTIDSWLIWSLTGGVNGGVHCTDVTNASRTMLFNIHSLEWDKELCDFFEIPMDLLPNVFSSSEIYGLIKTGALEGVPISGCLGDQCAALVGQMCFQEGQAKNTYGTGCFLLCNTGRKCVFSEHGLLTTVAYKLGREKPAYYALEGSVAIAGAVIRWLRDNLGIIETSGDIERLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGILCGLTQFTNKCHIAFAALEAVCFQTREILEAMNRDCGIPLRHLQVDGGMTNNKVLMQLQADILHIPVIKPFMPETTALGAAMAAGAAEGVSVWSLEPQALSVLRMERFEPQIQATESEIRYATWKKAVMKSMGWVTSQSPEGGDPSIFSSLPLGFFIVSSMVMLIGARYISGVP
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Molecular Weight
76.5 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
The study of GK2 (Glycine Kinase 2) recombinant protein originates from the need to better understand its role in various biological processes, particularly in energy metabolism and neurotransmitter synthesis. GK2 is an enzyme involved in the phosphorylation of glycine to form phosphoglycine, a crucial step that influences cellular energy balance and signaling pathways. Research has indicated that altered GK2 activity may be linked to metabolic disorders and neurological diseases, prompting a closer examination of its biochemical properties and regulatory mechanisms. The ability to produce recombinant GK2 in vitro has enabled scientists to investigate its structure, function, and interaction with other cellular components, providing insights into its physiological roles and potential implications in disease states. Additionally, exploring GK2 as a therapeutic target could pave the way for novel treatments, as its modulation may offer a means to restore normal metabolic functions. As a result, the production and study of GK2 recombinant protein have become a significant focus in biochemistry and molecular biology, aiming to uncover the complexities of this enzyme and its contributions to health and disease. By harnessing advanced techniques in protein expression and purification, researchers are poised to elucidate the intricate mechanisms through which GK2 operates, establishing a foundation for future experimental and clinical applications.
