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Fibronectin CS1 Peptide Sale

目录号 : GC36042

连接片段 1 (CS-1) 是位于纤维连接蛋白的 III 型同源连接段 (IIIC) 中的细胞连接域。Fibronectin CS1 Peptide 缺乏 Arg-Gly-Asp 结构域,在自发和实验性转移模型中能有效抑制肿瘤转移。

Fibronectin CS1 Peptide Chemical Structure

Cas No.:136466-51-8

规格 价格 库存 购买数量
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5mg 待询 待询

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Sample solution is provided at 25 µL, 10mM.

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产品描述

The connecting segment 1 (CS-1) is a cell attachment domain located in the type III homology connecting segment (IIICS) of fibronectin. Fibronectin CS1 Peptide lacks the Arg-Gly-Asp-containing domain, actively inhibits tumor metastases in spontaneous and experimental metastasis models[1].

[1]. Saiki I, et al. Inhibition of lung metastasis by synthetic and recombinant fragments of human fibronectin with functional domains. Jpn J Cancer Res. 1990 Oct;81(10):1003-11.

Chemical Properties

Cas No. 136466-51-8 SDF
分子式 C38H64N8O15 分子量 872.96
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.1455 mL 5.7276 mL 11.4553 mL
5 mM 0.2291 mL 1.1455 mL 2.2911 mL
10 mM 0.1146 mL 0.5728 mL 1.1455 mL
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Research Update

Exosomes released during reticulocyte maturation bind to fibronectin via integrin alpha4beta1

Eur J Biochem 2000 Jan;267(2):583-90.PMID:10632729DOI:10.1046/j.1432-1327.2000.01036.x.

Exosomes are vesicles formed in the endosomal compartment and released in the extracellular medium during reticulocyte maturation into erythrocytes. They have a clearing function because of their enrichment with some proteins known to decrease or disappear from the cell surface during maturation, e.g. acetylcholinesterase and transferrin receptor. We show here that integrin alpha4beta1, present on the surface of erythroid precursors but absent from the mature red cell membrane, is at least partly cleared from the reticulocyte plasma membrane by the exosomal pathway. Using flow cytometry, we found that the alpha4 subunit disappears from the reticulocyte surface during in vitro maturation. Two different monoclonal antibodies (B-5G10 and HP 2/1) were used to demonstrate the presence of the alpha4 chain on the exosome surface. Moreover, membrane acetylcholinesterase and lumenal peroxidase-like (i.e. hemoglobin) enzymatic activities were assayed to demonstrate exosome binding to plates coated with increasing fibronectin (FN) concentrations. This interaction was dependent on divalent cations (MnCl2 > MgCl2 > CaCl2). Similarly, vesicles bound to plates coated with the chymotryptic 40 K fragment (FN-40) containing the heparin-binding region of FN. This binding was inhibited by exosome preincubation with Fibronectin CS1 Peptide and with a monoclonal antibody (HP 2/1) against the integrin alpha4-chain, confirming an alpha4beta1-induced interaction. The importance of the exosome clearance function is highlighted here, since the presence of VLA-4 on reticulocytes often leads to blood circulation complications in some diseases. Moreover, the presence of alpha4beta1 on the exosome surface, by allowing binding to endothelial cells through vascular cell adhesion molecule 1 (VCAM-1), might confer another physiological function to the secreted vesicles.