Analytical Data
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Gene name
GLN
- Application
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Alternative Names
GLN；15E1.2；Glutamyl-tRNA(Gln) amidotransferase subunit C. mitochondrial
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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
O43716
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Expression Region
1-136aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMWSRLVW LGLRAPLGGR QGFTSKADPQ GSGRITAAVI EHLERLALVD FGSREAVARL EKAIAFADRL RAVDTDGVEP MESVLEDRCL YLRSDNVVEG NCADELLQNS HRVVEEYFVA PPGNISLPKL DEQEPFPHS
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Molecular Weight
18 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
GLN recombinant proteins have garnered significant attention in recent years due to their promising applications in biotechnology and medicine. Glutamine (GLN) is a vital amino acid involved in various metabolic processes and plays essential roles in protein synthesis, cell signaling, and immune response. The development of recombinant proteins allows for the production of GLN and its derivatives in a more efficient and controlled manner compared to traditional extraction methods from natural sources. Researchers have focused on the use of genetic engineering techniques to produce GLN proteins in various host systems, including bacteria, yeast, and mammalian cells. This approach not only enhances the yield and purity of the proteins but also facilitates the incorporation of post-translational modifications that are crucial for their biological activity. The insights gained from GLN recombinant protein studies have significant implications for therapeutic applications, such as in the formulation of nutraceuticals, development of targeted therapies for metabolic disorders, and enhancement of immune function. Moreover, understanding the structure-function relationships of GLN proteins contributes to the broader field of protein design and engineering, paving the way for innovative strategies in drug development and disease management. As research continues to evolve, the potential for GLN recombinant proteins to address various biological challenges holds promise for future advancements in health and medicine.
