Analytical Data
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Gene name
B3GNT6
- Application
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Alternative Names
B3GNT6Acetylgalactosaminyl-O-glycosyl-glycoProtein beta-1.3-N-acetylglucosaminyltransferase
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6ZMB0
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Expression Region
1-384aa
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AA Sequence
MAFPCRRSLTAKTLACLLVGVSFLALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEPPSELVPGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLLLAVKSAPEHYERRELIRRTWGQERSYGGRPVRRLFLLGTPGPEDEARAERLAELVALEAREHGDVLQWAFADTFLNLTLKHLHLLDWLAARCPHARFLLSGDDDVFVHTANVVRFLQAQPPGRHLFSGQLMEGSVPIRDSWSKYFVPPQLFPGSAYPVYCSGGGFLLSGPTARALRAAARHTPLFPIDDAYMGMCLERAGLAPSGHEGIRPFGVQLPGAQQSSFDPCMYRELLLVHRFAPYEMLLMWKALHSPALSCDRGHRVS
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Molecular Weight
69.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
B3GNT6, or beta-1,3-N-acetylglucosaminyltransferase 6, is an enzyme implicated in the synthesis of carbohydrate structures known as glycosaminoglycans, which play a crucial role in numerous biological processes, including cell signaling, adhesion, and the maintenance of extracellular matrix integrity. Recent studies have highlighted the significance of B3GNT6 in various physiological and pathological contexts, such as cancer progression and metastasis, due to its involvement in altering glycan structures on cell surfaces. Understanding the enzymatic activity of B3GNT6 and the resulting glycosylation patterns is essential for elucidating its functional roles in health and disease. Additionally, given the potential of glycan modifications in influencing therapeutic responses, B3GNT6 presents a promising target for drug development and biomarker discovery. Researchers are now focused on the recombinant expression of B3GNT6 to facilitate in-depth studies of its biochemical properties, substrate specificity, and interactions with other molecules, paving the way for novel therapeutic approaches that leverage the modulation of glycosylation pathways.
