Analytical Data
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Gene name
GYG1
- Application
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Alternative Names
GYG1；GYG;Glycogenin-1
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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
P46976
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Expression Region
2-350aa
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AA Sequence
TDQAFVTLT TNDAYAKGAL VLGSSLKQHR TTRRLVVLAT PQVSDSMRKV LETVFDEVIM VDVLDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFDREEL SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HLASEQGSFD GGDQGILNTF FSSWATTDIR KHLPFIYNLS SISIYSYLPA FKVFGASAKV VHFLGRVKPW NYTYDPKTKS VKSEAHDPNM THPEFLILWW NIFTTNVLPL LQQFGLVKDT CSYVNVLSDL VYTLAFSCGF CRKEDVSGAI SHLSLGEIPA MAQPFVSSEE RKERWEQGQA DYMGADSFDN IKRKLDTYLQ
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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 GYG1 protein, a glycogenin family member, plays a critical role in glycogen biosynthesis, serving as a primer for glycogen particles in eukaryotic organisms. Research into GYG1 has gained traction due to its essential function in carbohydrate metabolism and its implications for various metabolic disorders. Mutations or dysfunctions in GYG1 can lead to glycogen storage diseases, which are characterized by abnormal glycogen accumulation in tissues, resulting in a range of clinical symptoms. As physical activity, diet, and metabolic health gain increasing importance in the context of obesity and diabetes, understanding the molecular mechanisms governing glycogen synthesis via GYG1 is crucial. Recent studies have focused on elucidating the structural characteristics of GYG1 and how they relate to its enzymatic activity. Advances in techniques, such as X-ray crystallography and cryo-electron microscopy, have been instrumental in revealing the intricate workings of GYG1. Furthermore, the exploration of GYG1's interactions with other metabolic regulators and enzymes offers valuable insights into not only glycogen metabolism but also broader metabolic pathways. As we strive to develop targeted therapeutic strategies for glycogen-related disorders, a deeper understanding of GYG1's structure and function will be essential for unraveling its role in health and disease.
