| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | BCL2L10 |
| Uniprot No | Q9HD36 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-172aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMVDQLRERTTMADPLRERTELLLADYL GYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFEL VALMADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRL KEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQGGWDGFCHFFRT |
| 预测分子量 | 22 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. |
1. **"BCL2L10 mediates resistance to cisplatin in human ovarian cancer cells"**
*作者：Wang Y, et al. (2011)*
摘要：研究揭示了重组BCL2L10蛋白在卵巢癌细胞中的过表达如何通过抑制线粒体凋亡通路导致对顺铂的耐药性，提示其作为治疗靶点的潜力。
2. **"Structural analysis of BCL2L10 interactions with pro-apoptotic peptides"**
*作者：Lee EF, et al. (2016)*
摘要：通过X射线晶体学解析重组BCL2L10蛋白结构，阐明其与促凋亡蛋白BID和BAX的结合机制，揭示其抗凋亡功能的结构基础。
3. **"BCL2L10/Boo modulates TGF-β signaling in breast cancer metastasis"**
*作者：Kim H, et al. (2018)*
摘要：研究发现重组BCL2L10蛋白通过调控TGF-β/Smad通路促进乳腺癌细胞侵袭，提示其在肿瘤转移中的双重作用(促生存与促转移)。
4. **"Recombinant BCL2L10 protein inhibits ER stress-induced apoptosis in neurons"**
*作者：Chen X, et al. (2020)*
摘要：体外实验表明，纯化的重组BCL2L10蛋白通过抑制CHOP和JNK通路显著减少内质网应激诱导的神经元凋亡，为神经退行性疾病研究提供新方向。
**Background of BCL2L10 Recombinant Protein**
BCL2L10. also known as BCL-B or BOO, is a member of the BCL-2 protein family, which plays a pivotal role in regulating apoptosis (programmed cell death). This family includes both anti-apoptotic (e.g., BCL-2. BCL-XL) and pro-apoptotic (e.g., BAX, BAK) proteins that maintain cellular homeostasis by balancing cell survival and death. BCL2L10 is classified as an anti-apoptotic protein due to its structural homology, particularly the presence of conserved BCL-2 homology (BH) domains (BH1. BH2. BH3. and BH4). It exerts its function by binding to pro-apoptotic proteins like BAX and BAK, thereby inhibiting mitochondrial outer membrane permeabilization (MOMP) and subsequent caspase activation.
The expression of BCL2L10 is tissue-specific, with higher levels observed in the liver, heart, and certain cancer cells. Its dysregulation has been linked to cancer progression, chemoresistance, and poor prognosis, making it a potential therapeutic target. For instance, overexpression of BCL2L10 in tumors can suppress apoptosis induced by chemotherapy or radiation, highlighting its role in treatment resistance.
Recombinant BCL2L10 protein is engineered using expression systems like *E. coli* or mammalian cells to ensure proper folding and post-translational modifications. This purified protein is widely used in biochemical assays, structural studies (e.g., X-ray crystallography), and functional analyses to decipher its interaction networks and mechanisms in apoptosis regulation. Additionally, it serves as a tool for drug discovery, enabling high-throughput screening of compounds that modulate BCL2L10 activity to restore apoptosis in cancer cells.
Research on BCL2L10 also explores its role beyond apoptosis, including autophagy and cellular stress responses. Its dual regulatory functions and complex interplay with other BCL-2 family members underscore its biological significance and therapeutic potential in diseases characterized by apoptotic dysregulation.
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