Analytical Data
-
Gene name
B3GALT5
-
简介
B3GALT5 protein plays a pivotal role in catalyzing the transfer of galactose (Gal) to GlcNAc-based acceptors, exhibiting a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Additionally, it demonstrates efficient acceptor activity with glycolipid LC3Cer. B3GALT5 Protein, Human (HEK293, Fc) is the recombinant human-derived B3GALT5 protein, expressed by HEK293 , with N-hFc labeled tag.
- Application
-
Alternative Names
Beta-1,3-galactosyltransferase 5; Beta3Gal-T5; Beta-3-Gx-T5
-
Species
Human
-
Source
HEK293
-
Tag
N-hFc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y2C3
-
Expression Region
N29-V310
-
Protein Length
Lumenal Domain
-
Molecular Weight
62 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
B3GALT5, a member of the beta-1,3-galactosyltransferase family, plays a crucial role in glycoprotein and glycolipid biosynthesis by transferring galactose residues to certain acceptor molecules, thereby influencing various biological processes. This enzyme is particularly significant in the formation of glycosaminoglycans, which are essential components of the extracellular matrix and are involved in cell signaling, proliferation, and differentiation. Dysregulation of B3GALT5 has been implicated in multiple pathological conditions, including cancer and genetic disorders, highlighting its potential as a therapeutic target. Recent research has focused on the structural characterization and functional analysis of B3GALT5, using recombinant protein techniques to produce the enzyme in vitro. This approach allows for detailed studies on its enzymatic activity, substrate specificity, and regulatory mechanisms. Understanding the biochemical properties of B3GALT5 is critical for uncovering its roles in health and disease, paving the way for the development of novel diagnostic and therapeutic strategies that leverage its unique functions in glycosylation processes. As such, ongoing research aims to elucidate the complex pathways involving B3GALT5 and its interactions with other biomolecules, thereby contributing to the broader understanding of glycosylation in biology.
