Analytical Data
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Gene name
PRKAg3
- Application
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Alternative Names
PRKAg3；AMPKG3；5'-AMP-activated Protein kinase subunit gamma-3
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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
Q9UGI9
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Expression Region
1-489aa
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AA Sequence
MEPGLEHALR RTPSWSSLGG SEHQEMSFLE QENSSSWPSP AVTSSSERIR GKRRAKALRW TRQKSVEEGE PPGQGEGPRS RPAAESTGLE ATFPKTTPLA QADPAGVGTP PTGWDCLPSD CTASAAGSST DDVELATEFP ATEAWECELE GLLEERPALC LSPQAPFPKL GWDDELRKPG AQIYMRFMQE HTCYDAMATS SKLVIFDTML EIKKAFFALV ANGVRAAPLW DSKKQSFVGM LTITDFILVL HRYYRSPLVQ IYEIEQHKIE TWREIYLQGC FKPLVSISPN DSLFEAVYTL IKNRIHRLPV LDPVSGNVLH ILTHKRLLKF LHIFGSLLPR PSFLYRTIQD LGIGTFRDLA VVLETAPILT ALDIFVDRRV SALPVVNECG QVVGLYSRFD VIHLAAQQTY NHLDMSVGEA LRQRTLCLEG VLSCQPHESL GEVIDRIARE QVHRLVLVDE TQHLLGVVSL SDILQALVLS PAGIDALGA
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Molecular Weight
54.2 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
PRKAg3, a member of the amine oxidase family, has garnered attention in the field of biochemical research due to its potential role in various physiological and pathological processes. This recombinant protein plays a crucial role in catalyzing the oxidative deamination of primary amines, which is vital for the regulation of polyamine metabolism and the modulation of cellular signaling pathways. Studies have suggested that alterations in PRKAg3 activity may be linked to several diseases, including cardiovascular disorders and cancer, making it a target of interest for potential therapeutic interventions. The production of PRKAg3 as a recombinant protein allows for detailed investigations into its enzymatic properties, structure-function relationships, and physiological relevance. Researchers aim to elucidate its mechanism of action and its interactions with other biomolecules through advanced techniques such as crystallography and mass spectrometry. Furthermore, the exploration of PRKAg3's substrate specificity may reveal novel insights into its biological roles, paving the way for the development of drug candidates that could modulate its activity. Understanding PRKAg3’s function could ultimately contribute to the advancement of targeted therapies and improve our knowledge of its involvement in metabolic regulation and disease progression.
