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CD36片段能够阻断胶原诱导的血小板聚集,并部分抑制CD36与固定化凝血酶敏感蛋白的相互作用。
编号:180384
CAS号:143257-74-3
单字母:H2N-CNLAVAAASHIYQNQFVQ-OH
| 参考文献(References): | L. Leung et al., JBC, 267, 18244 (1992) |
CD36糖蛋白IV或IIIb序列CNLAVAAASHIYQNQFVQ是结合单克隆抗CD36抗体OKM5的表位的一部分。它增强了CD36与血小板反应素的结合,并增强了富血小板血浆中ADP诱导和胶原诱导的聚集。
The CD36 glycoprotein IV or IIIb sequence CNLAVAAASHIYQNQFVQ represents part of the epitope that binds the monoclonal anti-CD36 anti-body OKM5. It enhanced binding of CD36 to thrombospondin and augmented ADP-induced and collagen-induced aggregation in platelet-rich plasma.
CD36片段能够阻断胶原诱导的血小板聚集,并部分抑制CD36与固定化凝血酶敏感蛋白的相互作用。
CD36 fragment that blocked collagen-induced platelet aggregation and partially inhibited the interaction of CD36 to immobilized thrombospondin.
CD36 肽 P (139-155) 是一段受体片段,用于研究细胞外脂质识别的结构决定因素。其序列有助于结合位点组织表征。研究人员评估其构象稳定性以理解配体偏好。该肽促进 CD36 介导分子相互作用研究。
CD36 Peptide P (139-155) is a receptor fragment used to explore structural determinants of extracellular lipid recognition. Its sequence aids characterization of binding-site organization. Researchers assess its conformational stability to understand ligand preferences. The peptide enhances studies of CD36-mediated molecular interactions.
Cys-CD36(139‑155)三氟乙酸盐含有巯基残基,便于对 CD36 相关区域进行氧化还原敏感结构研究。其序列支持配体相互作用基序与折叠转变定位。该肽有助于探索膜相关蛋白结构域。应用包括结构生物学、生物化学与肽建模。
Cys-CD36 (139-155) trifluoroacetate salt contains a thiol-bearing residue enabling redox-sensitive structural studies of CD36-related regions. Its sequence supports mapping of ligand interaction motifs and folding transitions. The peptide aids in exploring membrane-associated protein domains. Applications include structural biology, biochemistry, and peptide modeling.
Cys-CD36(139-155)是一种经半胱氨酸修饰的配体结合受体片段,用于硫醇基偶联。其序列支持细胞外相互作用基序的定位。研究人员通过评估其结构特征来表征脂质识别决定簇。该肽段有助于构建CD36相关信号界面的模型。
Cys-CD36 (139-155) is a ligand-binding receptor fragment modified with cysteine for thiol-based conjugation. Its sequence supports mapping of extracellular interaction motifs. Researchers evaluate its structural features to characterize lipid-recognition determinants. The peptide contributes to modeling CD36-associated signaling interfaces.
ReversalL.L.K.Leung et al., J. Biol. Chem., 267, 18244(1992) : http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1381367




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