Analytical Data
-
Gene name
GLG1
- Application
-
Alternative Names
CFR-1; ESL-1; MG160; Golgi Apparatus Protein 1; E-selectin ligand 1; Cysteine-rich fibroblast growth factor receptor
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q92896
-
Expression Region
Lys1048~Asn1145
-
Molecular Weight
15kDa
-
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
GLG1, also known as glucan biosynthesis protein 1, plays a crucial role in the synthesis of glycogen in eukaryotic organisms. Research into GLG1 recombinant proteins has gained momentum due to their importance in understanding carbohydrate metabolism and storage, which has implications for various physiological processes and metabolic disorders. Glycogen, as a vital energy reserve, is intricately linked to conditions such as diabetes and glycogen storage diseases. Investigating GLG1 at a molecular level provides insights into its enzymatic functions and interactions within metabolic pathways, enhancing our understanding of how energy is regulated in cells. The recombinant production of GLG1 allows for detailed biochemical studies and the exploration of its structural properties, which can aid in the development of potential therapeutic strategies. Moreover, recombinant GLG1 proteins can serve as valuable tools for screening compounds that may modulate its activity, offering a pathway for novel treatments targeting glycogen metabolism. Understanding GLG1’s role could also have broader implications in biotechnology, such as improving yeast strains for bioethanol production or enhancing glycogen accumulation in crops. Thus, the research surrounding GLG1 recombinant proteins is pivotal not only for fundamental science but also for applied biomedicine and agriculture.
