GRGESP
目录号 : GC68027GRGESP 是一种胶原凝胶收缩抑制剂。GRGESP 抑制人成纤维细胞在胶原凝胶内的扩散并显着降低凝胶收缩。GRGDSP 可用于结缔组织形态发生的研究。
Cas No.:99896-88-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
GRGESP is a collagen gel contraction inhibitor. GRGESP inhibits the spreading of human fibroblasts inside collagen gels and markedly decreased gel contraction. GRGDSP can be used for the research of connective tissue morphogenesis[1].
GRGESP inhibits the spreading of human fibroblasts inside collagen gels and markedly decreased gel contraction[1].
GRGDSP inhibits cell spreading on collagen-coated surfaces[1].
[1]. F Grinnell, et al. The collagen recognition sequence for fibroblasts depends on collagen topography. Exp Cell Res. 1989 Jun;182(2):668-72.
| Cas No. | 99896-88-5 | SDF | Download SDF |
| 分子式 | C23H39N9O10 | 分子量 | 601.61 |
| 溶解度 | H2O : 50 mg/mL (83.11 mM; Need ultrasonic) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.6622 mL | 8.311 mL | 16.6221 mL |
| 5 mM | 0.3324 mL | 1.6622 mL | 3.3244 mL |
| 10 mM | 0.1662 mL | 0.8311 mL | 1.6622 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Inhibition of experimental metastasis of murine fibrosarcoma cells by oligopeptide analogues to the fibronectin cell-binding site
Int J Cancer 1989 Jan 15;43(1):102-6.PMID:2521334DOI:10.1002/ijc.2910430120.
We have analyzed the effect of the synthetic oligopeptides Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP) and Gly-Arg-Gly-Glu-Ser-Pro (GRGESP), analogues to the fibronectin cell-binding sequence, on the formation of experimental lung metastasis. SR-BALB were injected alone or in conjunction with GRGDSP or GRGESP in the tail vein of BALB/c mice. Co-injection with GRGESP reduced by approximately 70% the number of metastatic colonies per mouse. However, co-injection with the closely related peptide GRGDSP, containing the conservative substitution Glu/Asp, did not affect metastatic behavior. GRGESP peptide anti-metastatic activity was not due to a toxic effect on tumor cells or on mice. In vitro adhesion assays testing for a possible effect of the peptide on cell-matrix interactions indicated that the GRGESP peptide did not affect cell adhesion to the matrix proteins tested.
A fibronectin receptor on Candida albicans mediates adherence of the fungus to extracellular matrix
J Infect Dis 1991 Mar;163(3):604-10.PMID:1825316DOI:10.1093/infdis/163.3.604.
Binding of fibronectin, an extracellular matrix (ECM) protein, to Candida albicans was measured, and adherence of the fungus to immobilized ECM proteins, fibronectin, laminin, types I and IV collagen, and subendothelial ECM was studied. 125I-labeled fibronectin was inhibited from binding to the fungus by unlabeled human plasma fibronectin and by Arg-Gly-Asp (RGD), Gly-Arg-Gly-Glu-Ser-Pro (GRGESP), and Gly-Arg-Gly-Asp-Thr-Pro (GRGDTP), but binding was not inhibited by Gly-Arg-Gly-Asp-Ser-Pro. Soluble fibronectin, RGD, GRGESP, and GRGDTP also inhibited fungal adherence to the individual immobilized ECM proteins in a complex pattern, but only soluble fibronectin (10(-7) M) inhibited fungal adherence to subendothelial ECM. Thus, C. albicans possesses at least one type of cell surface receptor for binding soluble fibronectin that can be inhibited with peptides. This receptor apparently is used to bind the fungus to immobilized ECM proteins and to subendothelial ECM and may play a role in the initiation of disseminated disease by bloodborne fungi by providing for adherence of the microorganisms to ECM proteins.
Preparation of an RGD ALB conjugate. In vitro analysis of cellular responses
ASAIO J 1992 Jul-Sep;38(3):M275-8.PMID:1457864DOI:10.1097/00002480-199207000-00036.
RGD (Arg-Gly-Asp) tripeptide was identified as the minimal active core peptide sequence common to adhesive proteins. In this paper, the authors report preparation of RGD containing peptide albumin conjugate (RGD ALB), and its effects on cellular adhesive function in vitro. RGD ALB was prepared via a coupling reaction of albumin with pentapeptide (GRGDS; Gly-RGD-Ser) by water soluble carbodiimide. Bovine endothelial cells (ECs) adhered to and spread well on a surface coated with RGD ALB, whereas few ECs adhered on surfaces coated with GRGESP-albumin conjugate (GRGESP peptide with little cell attachment activity; false control) and albumin. Cellular behavior, such as adhesion, spreading, growth, and migration, on surfaces coated with GRD-ALB, fibronectin (FN), and vitronectin (VN) were quantitatively examined. Adherent cell number on RGD ALB coated surfaces was larger than on those coated with FN and VN. Cell morphology on RGD ALB coated surfaces was similar to that on FN coated surfaces. The cell growth and migration activities on RGD ALB coated surfaces were almost equal to those coated with FN and VN. Thus, RGD ALB was found to promote cell adhesion, migration, and growth as effectively as fibronectin. This indicates that an artificial adhesive protein, simply derived with bioactive peptidyl ligand, can find versatile applications in fields in which cellular events play a critical role--for example, extracellular matrices and wound healing promotion aids.
Cilengitide, a small molecule antagonist, targeted to integrin αν inhibits proliferation and induces apoptosis of laryngeal cancer cells in vitro
Eur Arch Otorhinolaryngol 2014 Aug;271(8):2233-40.PMID:24515920DOI:10.1007/s00405-014-2918-5.
Cilengitide is a chemical synthesis cyclopeptide containing RGD sequence, which can be used as a small molecule antagonist targeted to integrin αν (ITGAV). The aim of present study was to investigate the effect on proliferation and cell apoptosis of the cilengitide in laryngeal cancer cells. In the study, we have treatmented the cultured cells of laryngeal cancer (Hep-2) with cilengitide. After the medication, the proliferation of the Hep-2 cells was detected by MTT assay, the expression of ITGAV was detected by RT-PCR and the activity of caspase-3 protein was detected by a specialized kit. RGD linear peptides (GRGDSP), non-RGD linear peptide (GRGESP), and 5-fluorouracil (5-Fu) were used as controls. Results showed that the proliferation of Hep-2 cells was signally inhibited by the cilengitide with a time and dose compliance. Its inhibition effect was significantly higher than that of 5-Fu and GRGDSP, but the GRGESP showed no obvious inhibitory effect. After intervene of cilengitide, the activity of caspase-3 protein of Hep-2 cells was significantly increased, and the expression of ITGAV was significantly decreased. 5-Fu significantly inhibited the proliferation of Hep-2 cells, but no significant changes of ITGAV expression were observed. In conclusion, cilengitide can significantly down-regulate ITGAV expression and inhibit cell proliferation in laryngeal cancer cells, it will also to induce cell apoptosis through caspase-3 pathway. Therefore, it could be as a kind of effective chemotherapy drugs that will be used in clinical treatment of the laryngeal cancer.
Integrin and cytoskeletal involvement in signalling cell volume changes to glutamine transport in rat skeletal muscle
J Physiol 1998 Oct 15;512 ( Pt 2)(Pt 2):481-5.PMID:9763637DOI:10.1111/j.1469-7793.1998.481be.x.
1. Muscle glutamine transport is modulated in response to changes in cell volume by a mechanism dependent on active phosphatidylinositol 3-kinase. We investigated the possibility that this mechanism requires interactions between the extracellular matrix (ECM), integrins and the cytoskeleton as components of a mechanochemical transduction system. 2. Using skeletal muscle cells, we studied effects of (a) inactivating integrin-substratum interactions by using integrin-binding peptide GRGDTP with inactive peptide GRGESP as control, and (b) disrupting the cytoskeleton using colchicine or cytochalasin D, on glutamine transport after brief exposure to hypo-osmotic, isosmotic or hyperosmotic medium (170, 300 and 430 mosmol kg-1, respectively). 3. Neither GRGDTP nor GRGESP significantly affected basal glutamine uptake (0.05 mM; 338 +/- 58 pmol min-1 (mg protein)-1) but GRGDTP specifically prevented the increase (71%) and decrease (39%) in glutamine uptake in response to hypo- and hyperosmotic exposure, respectively. 4. Colchicine and cytochalasin D prevented the increase and decrease in glutamine uptake in response to changes in external osmolality. They also increased basal glutamine uptake by 59 +/- 19 and 85 +/- 16%, respectively, in a wortmannin-sensitive manner. 5. These results indicate involvement of ECM-integrin-mediated cell adhesion and the cytoskeleton in mechanochemical transduction of cell volume changes to chemical signals modulating glutamine transport in skeletal muscle. Phosphatidylinositol 3-kinase may function to maintain the mechanotransducer in an active state.