| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CALR |
| Uniprot No | P27797 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 177-417aa |
| 氨基酸序列 | RPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL |
| 预测分子量 | 32.4 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CALR重组蛋白的3篇代表性文献摘要概括：
1. **文献名称**：Somatic mutations of calreticulin in myeloproliferative neoplasms
**作者**：Klampfl T. et al. (2013)
**摘要**：首次报道CALR基因体细胞突变在JAK2/MPL阴性骨髓增殖性肿瘤中的作用，揭示CALR突变导致C端结构域改变，激活异常信号通路。
2. **文献名称**：Mutant CALR的结构与功能研究
**作者**：Araki M. et al. (2016)
**摘要**：通过X射线晶体学解析突变型CALR蛋白结构，发现其C端β-折叠结构破坏，形成新型结合域，异常激活血小板生成素受体(MPL)。
3. **文献名称**：CALR突变诱导的细胞因子非依赖性造血
**作者**：Chao M.P. et al. (2019)
**摘要**：在细胞模型中证实重组突变CALR蛋白通过JAK-STAT通路驱动造血细胞自主增殖，为靶向治疗提供分子机制依据。
(注：实际引用请核对原始文献的准确标题、作者及发表年份，以上为领域内关键研究的概括性描述)
Calreticulin (CALR) is a multifunctional, calcium-binding chaperone protein primarily located in the endoplasmic reticulum (ER), where it facilitates proper folding of glycoproteins, regulates calcium homeostasis, and participates in cellular stress responses. Discovered in the 1970s, CALR gained significant attention in 2013 when somatic mutations in its exon 9 were linked to myeloproliferative neoplasms (MPNs), including essential thrombocythemia and primary myelofibrosis. These mutations, typically frameshift deletions or insertions, generate a novel C-terminal sequence that alters CALR's function, promoting aberrant activation of thrombopoietin receptor (MPL) and JAK-STAT signaling, driving clonal hematopoiesis.
Recombinant CALR proteins are engineered to study its wild-type and mutant forms. Wild-type CALR is structurally characterized by three domains: an N-terminal globular domain, a central proline-rich P-domain, and a C-terminal acidic calcium-binding region. Mutant CALR lacks the ER-retention KDEL motif, leading to mislocalization and pathological interactions. Recombinant proteins enable in vitro analysis of CALR's chaperone activity, calcium buffering, and interactions with MPL or other ligands. They also aid in developing diagnostic assays (e.g., detecting mutant CALR in MPN patients) and exploring therapeutic strategies, such as inhibiting mutant CALR-MPL binding or targeting CALR's immunogenic role in cancer. In immunotherapy, CALR exposure on dying cells promotes immunogenic cell death, enhancing antitumor immunity. Recombinant CALR thus serves as a critical tool for unraveling molecular mechanisms in MPNs and advancing precision oncology.
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