Analytical Data
-
Gene name
b3GAT1
- Application
-
Alternative Names
b3GAT1；GLCATP；GalactosylgalactosylxylosylProtein 3-beta-glucuronosyltransferase 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9P2W7
-
Expression Region
28-334aa
-
AA Sequence
TLAPLLAVHK DEGSDPRRET PPGADPREYC TSDRDIVEVV RTEYVYTRPP PWSDTLPTIH VVTPTYSRPV QKAELTRMAN TLLHVPNLHW LVVEDAPRRT PLTARLLRDT GLNYTHLHVE TPRNYKLRGD ARDPRIPRGT MQRNLALRWL RETFPRNSSQ PGVVYFADDD NTYSLELFEE MRSTRRVSVW PVAFVGGLRY EAPRVNGAGK VVGWKTVFDP HRPFAIDMAG FAVNLRLILQ RSQAYFKLRG VKGGYQESSL LRELVTLNDL EPKAANCTKI LVWHTRTEKP VLVNEGKKGF TDPSVEI
-
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
B3GAT1, also known as Beta-1,3-glucuronyltransferase 1, is an important enzyme involved in glycosaminoglycan biosynthesis, particularly in the formation of specific glycan structures that are crucial for cellular functions and signaling. Mutations in the B3GAT1 gene have been linked to various developmental disorders, including skeletal dysplasias and neurological impairments, making it a significant target for biomedical research. Understanding the structure and function of B3GAT1, especially through the study of its recombinant protein, can provide insights into its enzymatic mechanism and substrate specificity. The generation of B3GAT1 recombinant proteins enables researchers to elucidate the enzyme's role in glycosylation processes, investigate its functional consequences in disease models, and explore potential therapeutic interventions. Additionally, the study of B3GAT1 may contribute to the broader understanding of glycosylation in human health and disease, highlighting its relevance in developing novel diagnostic and therapeutic strategies for conditions associated with glycan deficiencies. Overall, the research into B3GAT1 and its recombinant protein forms opens exciting avenues for advancing our knowledge of glycosylation biology and its implications for human diseases.
