| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HCAP-G |
| Uniprot No | Q9BPX3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1015aa |
| 氨基酸序列 | MGAERRLLSIKEAFRLAQQPHQNQAKLVVALSRTYRTMDDKTVFHEEFIHYLKYVMVVYKREPAVERVIEFAAKFVTSFHQSDMEDDEEEEDGGLLNYLFTFLLKSHEANSNAVRFRVCLLINKLLGSMPENAQIDDDVFDKINKAMLIRLKDKIPNVRIQAVLALSRLQDPKDDECPVVNAYATLIENDSNPEVRRAVLSCIAPSAKTLPKIVGRTKDVKEAVRKLAYQVLAEKVHMRAMSIAQRVMLLQQGLNDRSDAVKQAMQKHLLQGWLRFSEGNILELLHRLDVENSSEVAVSVLNALFSITPLSELVGLCKNNDGRKLIPVETLTPEIALYWCALCEYLKSKGDEGEEFLEQILPEPVVYADYLLSYIQSIPVVNEEHRGDFSYIGNLMTKEFIGQQLILIIKSLDTSEEGGRKKLLAVLQEILILPTIPISLVSFLVERLLHIIIDDNKRTQIVTEIISEIRAPIVTVGVNNDPADVRKKELKMAEIKVKLIEAKEALENCITLQDFNRASELKEEIKALEDARINLLKETEQLEIKEVHIEKNDAETLQKCLILCYELLKQMSISTGLSATMNGIIESLILPGIISIHPVVRNLAVLCLGCCGLQNQDFARKHFVLLLQVLQIDDVTIKISALKAIFDQLMTFGIEPFKTKKIKTLHCEGTEINSDDEQESKEVEETATAKNVLKLLSDFLDSEVSELRTGAAEGLAKLMFSGLLVSSRILSRLILLWYNPVTEEDVQLRHCLGVFFPVFAYASRTNQECFEEAFLPTLQTLANAPASSPLAEIDITNVAELLVDLTRPSGLNPQAKTSQDYQALTVHDNLAMKICNEILTSPCSPEIRVYTKALSSLELSSHLAKDLLVLLNEILEQVKDRTCLRALEKIKIQLEKGNKEFGDQAEAAQDATLTTTTFQNEDEKNKEVYMTPLRGVKATQASKSTQLKTNRGQRKVTVSARTNRRCQTAEADSESDHEVPEPESEMKMRLPRRAKTAALEKSKLNLAQFLNEDLS |
| 分子量 | 114.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人HCAP-G蛋白的参考文献示例(基于假设性文献)：
1. **文献名称**：*Expression and Functional Analysis of Recombinant Human HCAP-G in Mitotic Regulation*
**作者**：Liu Y. et al.
**摘要**：研究报道了通过大肠杆菌系统成功表达重组人HCAP-G蛋白，并证明其通过结合染色体着丝粒区域参与有丝分裂调控的分子机制。
2. **文献名称**：*Structural Insights into Human HCAP-G Protein and Its Role in Kinetochore Assembly*
**作者**：Wang H., Smith G.P.
**摘要**：利用X射线晶体学解析了重组HCAP-G蛋白的C端结构域，揭示了其通过与CENP-T等蛋白相互作用促进动粒组装的分子基础。
3. **文献名称**：*HCAP-G Knockdown and Overexpression Studies Reveal Its Essential Function in Chromosome Segregation*
**作者**：Tanaka K. et al.
**摘要**：通过重组HCAP-G蛋白的体外功能实验，结合细胞实验，证明其在染色体分离过程中维持基因组稳定的关键作用。
4. **文献名称**：*Development of a Novel HCAP-G-Specific Antibody Using Recombinant Protein Immunization*
**作者**：Zhang R. et al.
**摘要**：利用重组HCAP-G蛋白制备高特异性抗体，并验证其在人细胞裂解液和活细胞成像中的检测应用。
**注**：以上文献为示例性内容，实际文献需通过数据库(如PubMed、Web of Science)搜索关键词“recombinant human HCAP-G”或“CENP-G recombinant”获取。若需具体文献，建议补充蛋白的别名或研究背景以便精准检索。
Human HCAP-G protein, also known as condensin subunit CAP-G, is a critical component of the condensin I complex, essential for chromosome organization and segregation during mitosis and meiosis. Structurally, it belongs to the SMC (structural maintenance of chromosomes) protein family and functions in chromatin compaction, ensuring proper sister chromatid resolution and genomic stability. HCAP-G partners with HCAP-H, SMC2. and SMC4 to form the condensin I complex, which introduces positive supercoils into DNA, facilitating chromatin condensation and mitotic progression.
Recombinant human HCAP-G is produced via heterologous expression systems, such as *E. coli* or mammalian cells, enabling high-purity protein for functional studies. Its recombinant form is widely used to investigate molecular mechanisms of chromosome dynamics, DNA repair, and cell cycle regulation. Dysregulation of HCAP-G is linked to chromosomal instability disorders, including cancers and developmental defects, making it a target for studying tumorigenesis and potential therapeutic strategies.
Research applications include *in vitro* chromatin reconstitution assays, biochemical analyses of DNA-protein interactions, and drug screening platforms targeting mitotic errors. The availability of recombinant HCAP-G accelerates structural studies (e.g., crystallography, cryo-EM) and functional dissections of condensin roles in epigenetic regulation and genome integrity. Its study contributes to understanding pathologies linked to chromosome missegregation and innovative approaches in precision oncology.
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