Analytical Data
-
Gene name
GYG
- Application
-
Alternative Names
Glycogenin; Glycogenin-1; Glycogenin1; GLYG_HUMAN; GN-1; GN1; GYG 1; GYG; GYG1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P46976
-
Expression Region
2-350aa
-
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
-
Molecular Weight
39.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
GYG (glycogenin-like protein) is a key player in glycogen metabolism, primarily functioning as a primer for glycogen synthesis. Research into GYG has gained momentum due to its crucial role in regulating glucose homeostasis and its implications in metabolic diseases such as diabetes and obesity. Glycogen synthesis is vital for energy storage, and GYG facilitates the initiation of this process by catalyzing the formation of glycogen from glucose molecules. Understanding the structure and function of GYG can provide insights into the mechanisms of glycogen metabolism and its dysregulation in various pathologies. Additionally, studies have highlighted the potential of targeting GYG for therapeutic interventions aimed at enhancing glycogen storage and improving metabolic health. Advances in biophysical and biochemical techniques have enabled researchers to explore the functional characteristics of GYG, including its interaction with other proteins and regulatory pathways. Given its significant impact on energy balance and metabolic regulation, continued research on GYG is essential for developing strategies to combat metabolic disorders and improve overall health outcomes.
