Analytical Data
-
Gene name
Q6P4F1
-
简介
The FUT10 protein plays a key role in glycosylation, primarily fucosylating the innermost GlcNAc residues in biantennary N-glycans. This activity generates a core α(1->3)-fucose epitope that serves as a recognition signal for targeted degradation of misfolded glycoproteins. FUT10 Protein, Human (HEK293, His) is the recombinant human-derived FUT10 protein, expressed by HEK293 , with N-His labeled tag.
- Application
-
Alternative Names
Alpha-(1,3)-fucosyltransferase 10; Fucosyltransferase X; Fuc-TX; Fucosyltransferase 10
-
Species
Human
-
Source
HEK293
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6P4F1-1
-
Expression Region
L32-D479
-
Protein Length
Lumenal Domain
-
Molecular Weight
55-65 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
Q6P4F1 is a hypothetical protein encoded by the gene with the UniProt accession number Q6P4F1, which is of particular interest in the field of molecular biology due to its potential roles in various cellular processes. Despite its designation as "hypothetical," studies suggest that Q6P4F1 might be involved in critical pathways such as stress response, signal transduction, and cellular metabolism. Researchers have been increasingly focused on characterizing this protein to elucidate its structure-function relationships and understand its biological significance. Preliminary investigations utilizing bioinformatics tools have highlighted conserved domains and potential interaction partners, hinting at a broader functional network. Furthermore, recombinant expression of Q6P4F1 in model organisms, such as E. coli or yeast, is being explored to facilitate functional studies and high-throughput screening for biochemical assays. As the understanding of Q6P4F1 evolves, it may reveal insights into disease mechanisms and contribute to the development of novel therapeutic strategies, particularly in conditions where this protein may act as a biomarker or therapeutic target. The ongoing research aims to fill gaps in knowledge regarding the proteomic landscape and the specific roles of lesser-studied proteins like Q6P4F1, ultimately advancing our comprehension of cellular dynamics and potential applications in biotechnology and medicine.
