| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | B4GALT7 |
| Uniprot No | Q9UBV7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-327aa |
| 氨基酸序列 | MFPSRRKAAQLPWEDGRSGLLSGGLPRKCSVFHLFVACLSLGFFSLLWLQLSCSGDVARAVRGQGQETSGPPRACPPEPPPEHWEEDASWGPHRLAVLVPFRERFEELLVFVPHMRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSNSTDYIAMHDVDLLPLNEELDYGFPEAGPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPAWRKRDQKRIAAQKQEQFKVDREGGLNTVKYHVASRTALSVGGAPCTVLNIMLDCDKTATPWCTFS |
| 分子量 | 37.4 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 冻干粉 |
| 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. |
1. **"Molecular cloning and characterization of human β-1.4-galactosyltransferase VII (B4GALT7)"**
- *Okajima T, et al. (1999).*
- 该研究首次克隆了人源B4GATL7基因，证实其编码的酶催化糖胺聚糖(如硫酸软骨素/皮肤素)连接区半乳糖基化，并发现其广泛表达于成纤维细胞和软骨细胞。
2. **"Mutations in B4GALT7 cause a progeroid form of Ehlers-Danlos syndrome"**
- *Nakajima M, et al. (2013).*
- 研究发现B4GALT7基因突变导致EDS伴早衰样表型，患者表现为皮肤脆弱、关节松弛及胶原糖基化缺陷，阐明了该酶在结缔组织稳态中的关键作用。
3. **"B4GALT7 deficiency disrupts collagen synthesis and causes severe skeletal dysplasia"**
- *Vennekamp R, et al. (2019).*
- 通过小鼠模型发现，B4GALT7缺失导致胶原蛋白糖基化异常，引发骨骼发育畸形和生长迟缓，强调了其在胚胎发育和骨骼形成中的必要性。
4. **"Structural insights into the catalytic mechanism of B4GALT7 in glycosaminoglycan biosynthesis"**
- *Chen Y, et al. (2021).*
- 利用X射线晶体学解析B4GALT7的三维结构，揭示其底物结合与催化机制，为靶向该酶的药物设计(如粘多糖贮积症治疗)提供结构基础。
(注：以上文献信息为模拟参考示例，实际引用需以真实发表文献为准。)
B4GALT7 (β-1.4-galactosyltransferase 7) is a key enzyme in the biosynthesis of glycosaminoglycans (GAGs), particularly involved in proteoglycan modification. It catalyzes the transfer of galactose from UDP-galactose to xylose residues in the tetrasaccharide linker region of proteoglycans, a critical step for subsequent GAG chain elongation. This enzyme is localized in the Golgi apparatus and plays essential roles in extracellular matrix (ECM) organization, cell adhesion, and signaling pathways.
Mutations in the *B4GALT7* gene are linked to rare connective tissue disorders, such as Ehlers-Danlos syndrome (progeroid type) and Larsen syndrome, characterized by skin hyperelasticity, joint hypermobility, and skeletal abnormalities. These clinical manifestations underscore its importance in collagen and proteoglycan homeostasis.
Recombinant human B4GALT7 is produced using biotechnological platforms (e.g., mammalian or insect cell systems) for functional studies, drug screening, and therapeutic development. Its recombinant form enables research into enzymatic mechanisms, substrate specificity, and interactions with other biosynthetic enzymes. Recent studies also explore its potential as a biomarker or therapeutic target for ECM-related pathologies, including fibrosis and cancer metastasis. Ongoing research aims to elucidate its regulatory networks and develop enzyme replacement strategies for congenital disorders caused by B4GALT7 deficiency.
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