| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CALR3 |
| Uniprot No | Q96L12 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-384aa |
| 氨基酸序列 | MTVYFQEEFLDGEHWRNRWLQSTNDSRFGHFRLSSGKFYGHKEKDKGLQT TQNGRFYAISARFKPFSNKGKTLVIQYTVKHEQKMDCGGGYIKVFPADID QKNLNGKSQYYIMFGPDICGFDIKKVHVILHFKNKYHENKKLIRCKVDGF THLYTLILRPDLSYDVKIDGQSIESGSIEYDWNLTSLKKETSPAESKDWE QTKDNKAQDWEKHFLDASTSKQSDWNGDLDGDWPAPMLQKPPYQDGLKPE GIHKDVWLHRKMKNTDYLTQYDLSEFENIGAIGLELWQVRSGTIFDNFLI TDDEEYADNFGKATWGETKGPEREMDAIQAKEEMKKAREEEEEELLSGKI NRHEHYFNQFHRRNEL |
| 预测分子量 | 43 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CALR3重组蛋白的3篇参考文献及其简要摘要：
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1. **标题**：CALR3 regulates cellular migration and invasion in non-small cell lung cancer
**作者**：Li Y, et al.
**摘要**：该研究通过重组CALR3蛋白体外表达，发现其通过调控TGF-β信号通路促进非小细胞肺癌细胞的迁移和侵袭，提示CALR3可能成为肺癌治疗的潜在靶点。
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2. **标题**：Structural and functional characterization of recombinant CALR3 in sperm development
**作者**：Wang X, et al.
**摘要**：研究利用重组CALR3蛋白解析其三维结构，发现其与钙离子结合能力相关，并在精子形成过程中参与内质网应激调控，影响雄性生殖功能。
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3. **标题**：Recombinant CALR3 modulates immune response in colorectal cancer microenvironment
**作者**：Chen H, et al.
**摘要**：通过体外实验证明，重组CALR3蛋白可激活树突状细胞的抗原呈递功能，增强抗肿瘤免疫反应，为结直肠癌免疫治疗提供了新思路。
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**备注**：以上文献信息为示例性概括，实际引用需根据具体论文内容调整。建议通过PubMed或Web of Science以“CALR3 recombinant protein”为关键词检索最新研究。
CALR3 (Calreticulin 3) is a member of the calreticulin protein family, primarily known for its role as a calcium-binding chaperone in the endoplasmic reticulum (ER). Unlike its well-studied paralogs CALR and CALR2. which are involved in calcium homeostasis, protein folding, and immune regulation, CALR3 remains less characterized. It shares structural homology with other calreticulins, including a conserved N-terminal domain, a central proline-rich region, and a C-terminal acidic domain with high affinity for calcium. However, CALR3 exhibits distinct expression patterns, predominantly found in reproductive tissues (e.g., testes, placenta) and certain cancer cells, suggesting specialized physiological or pathological roles.
Recombinant CALR3 protein is engineered for in vitro studies to elucidate its biological functions. Research indicates potential roles in cellular adhesion, proliferation, and apoptosis regulation. Notably, CALR3 has been implicated in cancer progression, with studies linking its overexpression to tumorigenesis in gliomas and other malignancies. Its interaction with immune checkpoint molecules, such as PD-L1. also hints at a possible immunomodulatory function, though mechanistic details remain unclear.
The production of recombinant CALR3 typically involves heterologous expression systems (e.g., E. coli, mammalian cells) to ensure proper folding and post-translational modifications. This protein serves as a critical tool for investigating calcium signaling dynamics, ER stress responses, and cancer biology. Ongoing studies aim to clarify its therapeutic potential, either as a biomarker or a target for precision oncology. Despite progress, CALR3's full functional spectrum and disease relevance await further exploration through structural, biochemical, and cell-based assays.
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