纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PYCR1 |
Uniprot No | P32322 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-319aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSVGFIGAGQLAFALAKGFTAAGVLAAHKI MASSPDMDLATVSALRKMGVKLTPHNKETVQHSDVLFLAVKPHIIPFILD EIGADIEDRHIVVSCAAGVTISSIEKKLSAFRPAPRVIRCMTNTPVVVRE GATVYATGTHAQVEDGRLMEQLLSSVGFCTEVEEDLIDAVTGLSGSGPAY AFTALDALADGGVKMGLPRRLAVRLGAQALLGAAKMLLHSEQHPGQLKDN VSSPGGATIHALHVLESGGFRSLLINAVEASCIRTRELQSMADQEQVSPA AIKKTILDKVKLDSPAGTALSPSGHTKLLPRSLAPAGKD |
预测分子量 | 36 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PYCR1重组蛋白的3篇参考文献及其摘要概括:
1. **标题**:*"Structural insights into human pyrroline-5-carboxylate reductase 1 (PYCR1) and its role in cancer metabolism"*
**作者**:Smith J, et al.
**摘要**:该研究解析了重组人源PYCR1蛋白的晶体结构,揭示了其催化活性位点及与NADH结合的机制,并证明PYCR1在肿瘤细胞中通过调控脯氨酸合成促进细胞增殖。
2. **标题**:*"Recombinant PYCR1 expression and enzymatic characterization in colorectal cancer models"*
**作者**:Li X, Wang Y, Zhang H.
**摘要**:通过大肠杆菌系统表达并纯化重组PYCR1蛋白,发现其酶活性在结直肠癌细胞中显著升高,敲低PYCR1可抑制肿瘤生长,提示其作为潜在治疗靶点。
3. **标题**:*"Functional analysis of PYCR1 mutations in autosomal recessive cutis laxa using recombinant protein assays"*
**作者**:Mendoza G, et al.
**摘要**:研究利用重组PYCR1蛋白进行功能实验,发现皮肤松弛症相关突变导致酶活性和脯氨酸合成能力下降,阐明了PYCR1在细胞外基质稳态中的作用。
注:以上文献为示例,实际引用时需以真实发表的论文为准。建议通过PubMed或Web of Science以“PYCR1 recombinant protein”为关键词检索最新研究。
PYCR1 (Pyrroline-5-Carboxylate Reductase 1) is a mitochondrial enzyme critical for proline biosynthesis, catalyzing the final step in the conversion of pyrroline-5-carboxylate (P5C) to proline using NAD(P)H as a cofactor. This metabolic pathway plays a vital role in cellular homeostasis, including redox balance, collagen synthesis, and stress response. PYCR1 is highly expressed in tissues with high proline demand, such as skin, connective tissues, and rapidly proliferating cells. Its dysfunction is linked to genetic disorders like autosomal recessive cutis laxa (ARCL) and hyperprolinemia, as well as cancer, where elevated PYCR1 activity supports tumor growth by mitigating oxidative stress and promoting protein stability.
Recombinant PYCR1 protein is engineered for research and therapeutic applications. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains enzymatic activity and structural integrity, enabling studies on its kinetic properties, substrate specificity, and interactions with inhibitors. Recombinant PYCR1 is essential for structural biology (e.g., X-ray crystallography) to elucidate catalytic mechanisms and design targeted therapies. In drug discovery, it serves as a tool for screening small molecules that modulate proline metabolism, particularly in cancers reliant on PYCR1 overexpression. Additionally, it aids in diagnostic development for proline-related metabolic disorders.
Current research focuses on PYCR1's dual role in metabolism and disease, highlighting its potential as a biomarker or therapeutic target. Recombinant variants, including tagged or mutant forms, facilitate functional studies, advancing our understanding of proline metabolism's broader implications in aging, fibrosis, and neurodegeneration.
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