| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XYLT2 |
| Uniprot No | Q9H1B5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-865aa |
| 氨基酸序列 | GLEEDEAGEKGRQRKPRPLDPGEGSKDTDSSAGRRGSTGRRHGRWRGRAESPGVPVAKVVRAVTSRQRASRRVPPAPPPEAPGRQNLSGAAAGEALVGAAGFPPHGDTGSVEGAPQPTDNGFTPKCEIVGKDALSALARASTKQCQQEIANVVCLHQAGSLMPKAVPRHCQLTGKMSPGIQWDESQAQQPMDGPPVRIAYMLVVHGRAIRQLKRLLKAVYHEQHFFYIHVDKRSDYLHREVVELAQGYDNVRVTPWRMVTIWGGASLLRMYLRSMRDLLEVPGWAWDFFINLSATDYPTRTNEELVAFLSKNRDKNFLKSHGRDNSRFIKKQGLDRLFHECDSHMWRLGERQIPAGIVVDGGSDWFVLTRSFVEYVVYTDDPLVAQLRQFYTYTLLPAESFFHTVLENSLACETLVDNNLRVTNWNRKLGCKCQYKHIVDWCGCSPNDFKPQDFLRLQQVSRPTFFARKFESTVNQEVLEILDFHLYGSYPPGTPALKAYWENTYDAADGPSGLSDVMLTAYTAFARLSLHHAATAAPPMGTPLCRFEPRGLPSSVHLYFYDDHFQGYLVTQAVQPSAQGPAETLEMWLMPQGSLKLLGRSDQASRLQSLEVGTDWDPKERLFRNFGGLLGPLDEPVAVQRWARGPNLTATVVWIDPTYVVATSYDITVDTETEVTQYKPPLSRPLRPGPWTVRLLQFWEPLGETRFLVLPLTFNRKLPLRKDDASWLHAGPPHNEYMEQSFQGLSSILNLPQPELAEEAAQRHTQLTGPALEAWTDRELSSFWSVAGLCAIGPSPCPSLEPCRLTSWSSLSPDPKSELGPVKADGRLR |
| 预测分子量 | 93.9 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XYLT2重组蛋白的虚构参考文献示例(仅供格式参考，非真实文献)：
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1. **文献名称**：Recombinant XYLT2 expression in mammalian cells and its role in proteoglycan biosynthesis
**作者**：Chen L, et al.
**摘要**：本研究利用HEK293细胞成功表达并纯化XYLT2重组蛋白，证实其催化木糖转移至核心蛋白的活性，并发现其过表达可增强细胞外基质中硫酸乙酰肝素的合成。
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2. **文献名称**：Structural characterization of human XYLT2 using recombinant protein crystallography
**作者**：Martinez R, et al.
**摘要**：通过大肠杆菌表达系统获得高纯度XYLT2重组蛋白，首次解析其晶体结构，揭示其底物结合位点及突变导致的酶活性丧失机制。
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3. **文献名称**：XYLT2 mutations impair recombinant protein function in congenital heart disease
**作者**：Wang Y, et al.
**摘要**：在先天性心脏病患者中发现XYLT2错义突变，体外实验表明突变型重组蛋白木糖转移活性显著降低，提示其与疾病发生相关。
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4. **文献名称**：High-throughput screening of XYLT2 inhibitors using recombinant enzyme activity assays
**作者**：Kumar S, et al.
**摘要**：建立基于XYLT2重组蛋白的酶活检测体系，筛选小分子抑制剂，发现候选化合物可抑制肿瘤细胞迁移，为靶向治疗提供依据。
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**注意**：以上文献为模拟示例，建议通过PubMed、Google Scholar等平台检索真实研究(关键词：XYLT2 recombinant protein/xylosyltransferase II)。
XYLT2 (xylosyltransferase 2) is a key enzyme involved in the biosynthesis of proteoglycans, which are essential components of the extracellular matrix and cell membranes. It catalyzes the initial step in glycosaminoglycan (GAG) chain formation by transferring xylose from UDP-xylose to specific serine residues in core proteins. This modification serves as a primer for subsequent GAG chain elongation, critical for structural integrity and signaling functions in tissues. The XYLT2 gene is located on chromosome 17q21.33 and encodes a type II transmembrane protein predominantly expressed in the Golgi apparatus. It shares homology with XYLT1 but exhibits distinct tissue-specific expression patterns, with higher activity in the liver, kidneys, and certain cancer cells.
Recombinant XYLT2 protein is produced using expression systems like mammalian or insect cells to ensure proper post-translational modifications. Its production enables functional studies on GAG biosynthesis regulation and disease mechanisms. Dysregulation of XYLT2 has been linked to pathological conditions, including fibrosis, cancer metastasis, and rare connective tissue disorders. For instance, elevated XYLT2 levels correlate with increased tumor invasiveness in breast and prostate cancers, likely due to enhanced proteoglycan-mediated cell adhesion and growth factor signaling. Conversely, mutations affecting XYLT2 activity are implicated in Desbuquois syndrome, a skeletal dysplasia disorder.
Research applications of recombinant XYLT2 include screening modulators for therapeutic development, structural analysis of substrate binding domains, and engineering cell lines with optimized GAG synthesis for biopharmaceutical production. Its role in disease pathways also positions it as a potential biomarker or target for precision therapies targeting extracellular matrix remodeling.
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