Analytical Data
-
Gene name
B3GNT5
- Application
-
Alternative Names
5;BGnT-5;Beta-1.3-Gn-T5;Beta-1.3-N-acetylglucosaminyltransferase 5;Beta3Gn-T5
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BYG0
-
Expression Region
1-378aa
-
AA Sequence
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVNDTLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQLNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWANTYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVSYEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDHVFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKIILLCKISYVDTYPCRAAFI
-
Molecular Weight
67.32 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
B3GNT5, or Beta-1,3-N-acetylglucosaminyltransferase 5, is an essential enzyme involved in glycosylation processes, particularly in synthesizing biologically significant glycoconjugates. Glycosylation is crucial for various cellular functions, including cell signaling, immune response, and protein stability. Dysregulation of glycosylation pathways has been linked to several diseases, including cancer, where altered glycan structures can influence tumor progression and metastasis. The study of B3GNT5 is particularly relevant in this context, as it plays a key role in the formation of specific glycan structures that may impact cellular behavior. Recent research has focused on the recombinant production of B3GNT5 to better understand its enzymatic functions, substrate specificity, and regulation. By generating this recombinant protein, researchers aim to elucidate the biochemical mechanisms underlying glycosylation and its implications in health and disease. Additionally, the availability of recombinant B3GNT5 paves the way for potential therapeutic applications, including targeted drug delivery systems and the development of glyco-engineered biomolecules. Overall, the investigation into B3GNT5 and its functional properties contributes significantly to the broader field of glycoscience and its potential applications in biotechnology and medicine.
