| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | B3GAT3 |
| Uniprot No | O94766 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-335aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSQPCDCLPPLRAAAEQLRQKDLRISQLQ AELRRPPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPR LHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHP RGVEQRNKALDWLRGRGGAVGGEKDPPPPGTQGVVYFADDDNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGRVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTA PRGHLESSLLSHLVDPKDLEPRAANCTRVLVWHTRTEKPKMKQEEQLQRQ GRGSDPAIEV |
| 预测分子量 | 36 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于B3GAT3重组蛋白的3篇代表性文献的简要总结：
1. **文献名称**：*Mutations in B3GAT3 cause a skeletal disorder with joint laxity and metabolic abnormalities*
**作者**：Baasanjav S, et al.
**摘要**：该研究首次报道了B3GAT3基因突变导致人类骨骼发育异常和关节过度活动症。通过重组蛋白功能实验，证实突变会降低β3-葡糖醛酸转移酶的活性，影响糖胺聚糖(GAG)的合成，进而干扰细胞外基质功能(Nature Genetics, 2011)。
2. **文献名称**：*β3GlcAT-I (B3GAT3) synthesizes the glycosaminoglycan-protein linkage region through a novel mechanism*
**作者**：Cartee N, et al.
**摘要**：本研究利用重组B3GAT3蛋白进行体外酶活性分析，揭示了其通过独特的“两步转移”机制催化糖胺聚糖链与核心蛋白的连接反应，为蛋白聚糖生物合成机制提供了关键证据(Journal of Biological Chemistry, 2001)。
3. **文献名称**：*Functional analysis of B3GAT3 mutations associated with skeletal dysplasia*
**作者**：Mizumoto S, et al.
**摘要**：通过表达野生型和突变型B3GAT3重组蛋白，发现致病突变会导致酶活性显著下降，并影响硫酸软骨素和硫酸皮肤素的合成，阐明了B3GAT3缺陷导致骨骼异常的分子机制(Human Molecular Genetics, 2013)。
B3GAT3 (β-1.3-glucuronyltransferase 3) is a key enzyme in the biosynthesis of glycosaminoglycans (GAGs), particularly heparan sulfate and chondroitin sulfate chains. These sulfated polysaccharides are critical components of proteoglycans, which mediate cell-matrix interactions, signaling pathways, and tissue development. The B3GAT3 gene encodes a type II transmembrane protein localized to the Golgi apparatus, where it transfers glucuronic acid to the linker tetrasaccharide during GAG chain initiation—a rate-limiting step in proteoglycan assembly.
Mutations in B3GAT3 are associated with autosomal recessive disorders such as musculocontractural Ehlers-Danlos syndrome (mcEDS), characterized by connective tissue defects, craniofacial abnormalities, and developmental delays. These pathogenic variants impair enzyme activity, leading to reduced GAG sulfation and disrupted extracellular matrix integrity, underscoring B3GAT3's biological importance.
Recombinant B3GAT3 proteins are typically produced in mammalian or insect expression systems to ensure proper post-translational modifications. Purification often employs affinity tags (e.g., His-tag) followed by chromatography. The recombinant enzyme serves as a vital tool for studying GAG biosynthesis mechanisms, characterizing disease-causing mutations through in vitro activity assays, and screening potential modulators of enzymatic function. Additionally, it enables structural studies to resolve catalytic domains and substrate-binding sites, informing therapeutic strategies targeting GAG-related pathologies like osteoarthritis or genetic connective tissue disorders. Recent research also explores its role in cancer progression, as altered GAG profiles influence tumor microenvironment interactions. As a reagent, recombinant B3GAT3 facilitates the reconstruction of synthetic proteoglycans for biomaterial applications and drug delivery systems leveraging GAG-mediated cellular uptake.
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