Analytical Data
-
Gene name
GbL
- Application
-
Alternative Names
MLST8; Pop3; GbetaL; MTOR Associated Protein,LST8 Homolog; Mammalian lethal with SEC13 protein 8; Target of rapamycin complex subunit LST8
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BVC4
-
Expression Region
Asp69~Trp247
-
Molecular Weight
28kDa
-
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
GbL, or glucan-binding lectin, is a type of recombinant protein that has gained significant interest in the fields of biochemistry and molecular biology due to its potential applications in various medical and agricultural domains. Initially discovered in certain fungal species, GbL exhibits a unique ability to bind to specific polysaccharides, particularly beta-glucans, which are essential components of the cell walls of many fungi and plants. This binding activity has led researchers to explore GbL's roles in immune response modulation, pathogen recognition, and as a potential therapeutic agent. The ability to produce GbL through recombinant DNA technology has enabled scientists to study its properties in detail and increase its availability for experimental and commercial applications. Moreover, understanding the structure-function relationship of GbL can illuminate mechanisms of pathogen-host interactions, thus providing insights into developing novel strategies for disease prevention and treatment. Additionally, as a lectin, GbL's interactions with glycosylated molecules are of great relevance in glycomics research, making it a valuable tool for studying carbohydrate-protein interactions. Overall, the study of GbL and its recombinant forms is paving the way for advancements in biotechnology, with implications that extend from immunology to agricultural pest control.
