| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL11a2 |
| Uniprot No | P13942 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1736aa |
| 氨基酸序列 | MERCSRCHRLLLLLPLVLGLSAAPGWAGAPPVDVLRALRFPSLPDGVRRAKGICPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPSQPVFRGLSLADGKWHRVAVAVKGQSVTLIVDCKKRVTRPLPRSARPVLDTHGVIIFGARILDEEVFEGDVQELAIVPGVQAAYESCEQKELECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEILESSLLPPLEEEQTDLQVPPTADRFQAEEYGEGGTDPPEGPYDYTYGYGDDYREETELGPALSAETAHSGAAAHGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGDPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPQGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPQGKPGLPGMPGSDGPPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPPGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPLGPPGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGETGPMGERGHPGPPGPPGEQGLPGTAGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPSGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGIQGEPGVKGPRGERGEKGESGQPGEPGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEGGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGSPGSEGRQGGKGAKGDPGAIGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSPGQKGEMGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPGGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSRLMQEDEAIPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVCFMG |
| 预测分子量 | 171 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3篇与COL11A2重组蛋白相关的参考文献示例(注：部分文献为模拟示例，实际引用时请核实)：
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1. **文献名称**: *Expression and purification of recombinant human COL11A2 for structural studies*
**作者**: Smith J, et al.
**摘要**: 本研究描述了在大肠杆菌系统中高效表达人源COL11A2重组蛋白的方法，并通过亲和层析和离子交换层析纯化获得高纯度蛋白。通过圆二色谱和X射线晶体学分析，揭示了COL11A2的三股螺旋结构特征，为研究其与胶原XI复合物的相互作用提供了基础。
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2. **文献名称**: *COL11A2 mutations alter collagen fibril assembly in vitro: Functional analysis using recombinant protein models*
**作者**: Tanaka K, et al.
**摘要**: 作者在HEK293细胞中表达了携带耳聋相关突变的COL11A2重组蛋白，发现特定突变(如p.Gly955Glu)导致蛋白错误折叠，破坏胶原XI/II复合物的形成，并影响体外胶原纤维的组装。该研究为遗传性耳聋的分子机制提供了实验依据。
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3. **文献名称**: *Role of recombinant COL11A2 in chondrocyte differentiation and osteoarthritis*
**作者**: Lee S, et al.
**摘要**: 通过在小鼠软骨细胞中过表达重组COL11A2蛋白，研究发现其通过调控TGF-β信号通路促进软骨细胞分化，并抑制炎症因子(如IL-1β)诱导的细胞外基质降解，提示COL11A2可能成为骨关节炎治疗的潜在靶点。
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4. **文献名称**: *Development of a COL11A2 ELISA kit using recombinant protein for clinical diagnostics*
**作者**: Müller R, et al.
**摘要**: 利用昆虫细胞表达系统制备重组COL11A2蛋白，开发出高灵敏度的ELISA检测方法，成功用于检测Stickler综合征患者血清中的COL11A2抗体水平，为疾病的无创诊断提供了新工具。
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**注**：以上文献为示例性内容，实际研究中请通过PubMed(https://pubmed.ncbi.nlm.nih.gov)或Google Scholar检索具体文献。
The COL11A2 gene encodes the alpha-2 chain of type XI collagen, a fibrillar collagen critical for extracellular matrix (ECM) organization. Type XI collagen is a heterotrimer composed of α1. α2. and α3 chains (encoded by COL11A1. COL11A2. and COL2A1. respectively), which co-assembles with type II collagen to regulate fibril diameter and matrix stability in cartilage, vitreous humor, and the inner ear. COL11A2 is essential for skeletal development, auditory function, and connective tissue integrity. Mutations in COL11A2 are linked to autosomal dominant disorders such as Stickler syndrome, Marshall syndrome, and non-syndromic hearing loss (DFNA53), often caused by dominant-negative effects disrupting collagen networks.
Recombinant COL11A2 protein is produced using expression systems (e.g., mammalian cells) to ensure proper post-translational modifications, such as hydroxylation and triple-helix formation. This engineered protein enables functional studies of collagen assembly, cell-ECM interactions, and disease mechanisms. Researchers utilize it to investigate pathogenic variants, screen therapeutic agents, and model tissue-specific defects in vitro. In regenerative medicine, recombinant COL11A2 may support cartilage repair strategies or serve as a biomarker for connective tissue disorders. Challenges include maintaining structural fidelity during production and addressing its complex interactions with other collagens. Current research also explores its role in tumor progression, as aberrant COL11A2 expression is observed in certain cancers. Overall, recombinant COL11A2 is a vital tool for unraveling collagen biology and developing targeted therapies. (Word count: 245)
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