纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PNLIPRP1 |
Uniprot No | P54315 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-467aa |
氨基酸序列 | MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE KIGTRFLLYT NENPNNFQI LLLSDPSTIE ASNFQMDRKT RFIIHGFIDK GDESWVTDMC KKLFEVEEVN CICVDWKKG SQATYTQAAN NVRVVGAQVA QMLDILLTEY SYPPSKVHLI GHSLGAHVAG EAGSKTPGL SRITGLDPVE ASFESTPEEV RLDPSDADFV DVIHTDAAPL IPFLGFGTNQ QMGHLDFFP NGGESMPGCK KNALSQIVDL DGIWAGTRDF VACNHLRSYK YYLESILNPD GFAAYPCTS YKSFESDKCF PCPDQGCPQM GHYADKFAGR TSEEQQKFFL NTGEASNFAR WRYGVSITL SGRTATGQIK VALFGNKGNT HQYSIFRGIL KPGSTHSYEF DAKLDVGTIE KVKFLWNNN VINPTLPKVG ATKITVQKGE EKTVYNFCSE DTVREDTLLT LTPC |
预测分子量 | 51 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. |
以下是与PNLIPRP1重组蛋白相关的3篇模拟参考文献示例:
1. **标题**:*Structural and functional characterization of recombinant PNLIPRP1 as a pancreatic lipase inhibitor*
**作者**:Zhang et al.
**摘要**:通过重组表达纯化PNLIPRP1蛋白,解析其三维结构,证明其通过竞争性结合脂肪酶底物界面抑制胰脂肪酶活性,揭示其在调节脂肪消化中的作用机制。
2. **标题**:*Role of PNLIPRP1 in modulating lipid metabolism and inflammation in acute pancreatitis*
**作者**:Smith et al.
**摘要**:利用重组PNLIPRP1蛋白研究其在急性胰腺炎模型中的作用,发现其通过抑制胰脂肪酶活性减少游离脂肪酸释放,从而缓解胰腺组织炎症损伤。
3. **标题**:*Expression and purification of bioactive recombinant PNLIPRP1 in E. coli*
**作者**:Chen et al.
**摘要**:优化大肠杆菌表达系统,成功获得高纯度重组PNLIPRP1蛋白,并验证其与胆汁盐及脂质底物的结合能力,为后续功能研究提供可靠材料。
(注:以上文献为模拟内容,实际研究需通过PubMed/Google Scholar等平台检索。)
PNLIPRP1 (pancreatic lipase-related protein 1) is a member of the pancreatic lipase gene family, primarily expressed in the pancreas. Unlike classical pancreatic lipase (PNLIP), which hydrolyzes dietary triglycerides in the small intestine, PNLIPRP1 exhibits distinct functional characteristics due to structural variations. It shares approximately 65% amino acid sequence identity with PNLIP but lacks canonical lipase activity owing to mutations in its catalytic triad. Instead, PNLIPRP1 has been implicated in lipid metabolism modulation, potentially acting as a cofactor or inhibitor for other lipases or interacting with lipid substrates non-catalytically.
Studies suggest PNLIPRP1 may play a role in regulating dietary lipid absorption and protecting against lipid overload. It demonstrates phospholipase A1 activity under specific conditions and shows affinity for lipid-water interfaces, possibly influencing emulsion stability or lipid accessibility. Additionally, PNLIPRP1 has been associated with cholesterol homeostasis through interactions with pancreatic cholesterol esterase.
Recombinant PNLIPRP1 protein is typically produced using expression systems like mammalian cells or bacteria, enabling functional studies without contamination from native pancreatic enzymes. Its recombinant form facilitates research into lipid-protein interactions, enzyme inhibition mechanisms, and potential therapeutic applications. Emerging evidence links PNLIPRP1 polymorphisms to pancreatic disorders and metabolic diseases, driving interest in its recombinant form for diagnostic and pathophysiological investigations. Current research focuses on elucidating its precise biological role, structural determinants of function, and possible clinical relevance in obesity, pancreatitis, and lipid malabsorption syndromes.
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