Analytical Data
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Gene name
GYG2
- Application
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Alternative Names
Glycogenin 2; Glycogenin glucosyltransferase; Glycogenin-2; Glycogenin2; GLYG2_HUMAN; GN 2; GN-2; GN2; GYG 2; GYG2; OTTHUMP00000022855
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15488
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Expression Region
1-470aa
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AA Sequence
MSVTDQAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSVSSSQHQAAFLHLWWTVYQNNVLPLYKSVQAGEARASPGHTLCRSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPTQIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILQPANKVESVSSEETFEPSQELPAEALRDPSLQDALEVDLAVSVSQISIEEKVKELSPEEERRKWEEGRIDYMGKDAFARIQEKLDRFLQ
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Molecular Weight
78.4 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
Related Products
Protein Description
The GYG2 protein, a member of the glycogenin family, plays a pivotal role in glycogen metabolism, specifically in the initiation of glycogen synthesis. Research into GYG2 has gained momentum due to its crucial function in maintaining glucose homeostasis and contributing to energy storage in muscle and liver tissues. Mutations in the GYG2 gene have been associated with glycogen storage diseases, particularly those characterized by impaired glycogen accumulation and resultant muscle weakness and myopathy. This has propelled interest in understanding the structural and functional properties of GYG2, including its enzymatic mechanisms and interaction with other proteins involved in glycogen metabolism. Furthermore, as the prevalence of metabolic syndromes and diabetes rises, studying GYG2 could provide insights into potential therapeutic targets for these conditions. Current research focuses on elucidating the biochemical pathways in which GYG2 operates, exploring its regulatory mechanisms, and assessing its potential as a biomarker for metabolic health. Investigations into the recombinant expression of GYG2 protein and its functional assays are being conducted to better appreciate its role in glycogen biosynthesis and to inform future strategies for treating glycogen-related disorders. Overall, GYG2 represents a significant molecular target in the fields of biochemistry and metabolic biology, with implications for understanding both fundamental biological processes and potential clinical applications.
