Recombinant Mouse 5-Amp-Activated Protein Kinase Subunit Gamma-1 (PRKAG1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04952P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse 5-Amp-Activated Protein Kinase Subunit Gamma-1 (PRKAG1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04952P
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Product Overview

Description Recombinant Mouse 5-Amp-Activated Protein Kinase Subunit Gamma-1 (PRKAG1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb O54950
Target Symbol PRKAG1
Synonyms Prkag1; Prkaac5'-AMP-activated protein kinase subunit gamma-1; AMPK gamma1; AMPK subunit gamma-1; AMPKg
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence MESVAAESSPALENEHFQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLQELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALVLTGGEKKP
Expression Range 1-330aa
Protein Length Full Length
Mol. Weight 41.6 kDa
Research Area Metabolism
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Protein Families 5'-AMP-activated protein kinase gamma subunit family
Database References

KEGG: mmu:19082

STRING: 10090.ENSMUSP00000132499

UniGene: PMID: 28355557

  • Transgenic activation of skeletal muscle AMPKgamma1 in this model plays an important sex-specific role in skeletal muscle metabolism and whole body energy homeostasis. PMID: 26306597
  • Data indicate that a diet high in iron improves glucose tolerance by activating AMPK through mechanisms that include deacetylation. PMID: 23515442
  • Results demonstrate that AMPKgamma1 subunit is required for the maintenance of erythrocyte membrane elasticity. PMID: 20881209
  • In R70Qgamma1-expressing mice, there is an increase in muscle glycogen synthase activity associated with an increase in exercise capacity. PMID: 17106064
  • AMPK is not necessary for exercise training-induced increases in mitochondrial markers, but it is essential for fiber type IIb to IIa/x transformation and increases in hexokinase II protein[AMP-activated protein kinase gamma1] PMID: 17513699

    • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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