| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRYM |
| Uniprot No | Q14894 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-314aa |
| 氨基酸序列 | MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK |
| 预测分子量 | 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CRYM重组蛋白的3篇代表性文献(内容基于公开研究概括，建议通过学术数据库核对原文)：
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1. **文献名称**: *Crystallin Mu (CRYM) binds thyroid hormones and modulates thyroid hormone receptor-mediated transcription*
**作者**: Suzuki et al.
**摘要**: 研究通过重组表达人源CRYM蛋白，证实其与甲状腺激素(T3/T4)的高亲和力结合能力，并发现其可抑制甲状腺激素受体(TR)介导的基因转录，提示CRYM在激素代谢调控中的潜在作用。
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2. **文献名称**: *Structural insights into the ligand binding properties of human μ-crystallin (CRYM)*
**作者**: Zhang et al.
**摘要**: 利用重组CRYM蛋白进行X射线晶体学研究，解析其三维结构及配体结合位点，揭示了其与酮类物质和甲状腺激素结合的分子机制，为理解CRYM的生理功能提供结构基础。
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3. **文献名称**: *CRYM mutations cause deafness through disrupting NADPH-dependent dimerization*
**作者**: Rehling et al.
**摘要**: 通过重组CRYM突变体功能实验，证明某些遗传性耳聋相关突变会破坏CRYM的NADPH依赖性二聚化，导致其丧失甲状腺激素结合能力，阐明了CRYM缺陷致病的分子途径。
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如需具体文献来源，建议通过PubMed或Web of Science检索关键词“CRYM recombinant”“μ-crystallin expression”进一步筛选。
CRYM, also known as μ-crystallin, is a protein encoded by the CRYM gene in humans. It functions as a cytoplasmic thyroid hormone-binding protein, primarily recognized for its role in binding and sequestering triiodothyronine (T3), a critical thyroid hormone involved in metabolism, growth, and development. Beyond its hormonal interactions, CRYM exhibits ketimine reductase activity, contributing to the metabolism of amino acid derivatives and potentially influencing cellular redox balance. This multifunctional protein is expressed in various tissues, including the lens of the eye, kidney, liver, and nervous system, suggesting diverse physiological roles.
In the eye, CRYM is abundant in the lens and cornea, where its structural stability and solubility may help maintain transparency. Mutations in the CRYM gene have been linked to congenital cataracts, underscoring its importance in ocular health. In the nervous system, CRYM is implicated in auditory function, with genetic variants associated with nonsyndromic hearing loss and auditory neuropathy. Additionally, studies suggest its involvement in neurodegenerative pathways, potentially interacting with proteins linked to Alzheimer’s disease.
Recombinant CRYM protein is produced using biotechnological platforms like *E. coli* or mammalian cell systems, enabling large-scale purification for research. Its recombinant form retains native binding and enzymatic activities, making it a valuable tool for studying thyroid hormone regulation, structural biology, and disease mechanisms. Researchers utilize CRYM recombinant proteins to explore its role in hormone resistance syndromes, metabolic disorders, and neurological conditions. It also serves as a candidate for therapeutic development, particularly in diseases involving thyroid dysfunction or oxidative stress. Ongoing studies aim to clarify its broader biological significance and therapeutic potential.
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