Dihydrocytochalasin B
(Synonyms: 二氢细胞松弛素 B) 目录号 : GC43461An inhibitor of actin assembly and cytokinesis
Cas No.:39156-67-7
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Dihydrocytochalasin B (H2CB) is a Cytokinesis inhibitor and changes the morphology of the cells, similar to that of cytochalasin B; does not inhibit glucose transport[1]. Dihydrocytochalasin B (H2CB) disrupts the actin structure and inhibits the ability of growth factors to stimulate DNA synthesis, reversibly blocks initiation of DNA synthesis[2]. Dihydrocytochalasin B (H2CB) inhibits active calcium transport and causes a Ca2+increase in the mucosal scrapings[3].
References:
[1]. Atlas SJ, et al. Dihydrocytochalasin B. Biological effects and binding to 3T3 cells. J Cell Biol. 1978 Feb;76(2):360-70.
[2]. Jande SS, et al. Effects of cytochalasin B and dihydrocytochalasin B on calcium transport by intestinal absorptive cells. Calcif Tissue Int. 1981;33(2):143-51.
[3]. Maness PF, et al. Dihydrocytochalasin B disorganizes actin cytoarchitecture and inhibits initiation of DNA synthesis in 3T3 cells. Cell. 1982 Aug;30(1):253-62.
| Cas No. | 39156-67-7 | SDF | |
| 别名 | 二氢细胞松弛素 B | ||
| Canonical SMILES | O=C1CC[C@H](O)CCC[C@@H](C)C/C=C/[C@]([C@H](O)C([C@@H](C)[C@@]2([H])[C@H](CC3=CC=CC=C3)NC4=O)=C)([H])[C@@]24O1 | ||
| 分子式 | C29H39NO5 | 分子量 | 481.6 |
| 溶解度 | DMF: 30 mg/mL,DMF:PBS (pH 7.2) (1:20): 0.05 mg/mL,DMSO: 20 mg/mL,Ethanol: 20 mg/mL | 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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 2.0764 mL | 10.3821 mL | 20.7641 mL |
| 5 mM | 0.4153 mL | 2.0764 mL | 4.1528 mL |
| 10 mM | 0.2076 mL | 1.0382 mL | 2.0764 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。
Dihydrocytochalasin B disorganizes actin cytoarchitecture and inhibits initiation of DNA synthesis in 3T3 cells
Cell 1982 Aug;30(1):253-62.PMID:6215122DOI:10.1016/0092-8674(82)90031-9.
Dihydrocytochalasin B (H2CB) disrupts the actin structure of Swiss/3T3 mouse fibroblasts and inhibits the ability of serum growth factors to stimulate DNA synthesis in quiescent cultures. Low doses of H2CB (2-10 X 10(-7) M) added to serum-arrested cells reversibly block initiation of DNA synthesis by serum; by epidermal growth factor and insulin; or by epidermal growth factor, fibroblast growth factor and insulin. H2CB is effective only when added to cells within 8-10 hr after stimulation. Low doses of H2CB cause cell rounding and a loss of actin microfilament bundles, but they do not interfere with glucose or thymidine transport. These results suggest that stimulation of 3T3 cells involves at least one obligatory actin-mediated step. Transformed cells appear to obviate this step, for H2CB does not inhibit the entry into S phase of SV40-transformed or Moloney murine sarcoma virus-transformed 3T3 cells synchronized by mitotic shake-off.
Dihydrocytochalasin B. Biological effects and binding to 3T3 cells
J Cell Biol 1978 Feb;76(2):360-70.PMID:10605443DOI:10.1083/jcb.76.2.360.
Dihydrocytochalasin B (H2CB) does not inhibit sugar uptake in BALB/c 3T3 cells. Excess H2CB does not affect inhibition of sugar uptake by cytochalasin B (CB), indicating that it does not compete with CB for binding to high-affinity sites. As in the case of CB, H2CB inhibits cytokinesis and changes the morphology of the cells. These results demonstrate that the effects of CB on sugar transport and on cell motility and morphology involve separate and independent sites. Comparison of the effects of H2CB, CB, and cytochalasin D (CD) indicates that treatment of cells with any one of the compounds results in the same series of morphological changes; the cells undergo zeiosis and elongation at 2-4 microM CB and become arborized and rounded up at 10-50 microM CB. H2CB is slightly less potent than CB, whereas CD is five to eight times more potent than CB in causing a given state of morphological change. These results indicate that the cytochalasin-induced changes in cell morphology are mediated by a specific site(s) which can distinguish the subtle differences in the structures of the three compounds. Competitive binding studies indicate that excess H2CB displaces essentially all of the high-affinity bound [3H]CB, but, at less than 5 x 10(-5) M H2CB is not so efficient as unlabeled CB in the displacement reaction. In contrast, excess CD displaces up to 40% of the bound [3H]CB. These results suggest that three different classes of high-affinity CB binding sites exist in 3T3 cells: sites related to sugar transport, sites related to cell motility and morphology, and sites with undetermined function.
Dihydrocytochalasin B enhances transforming growth factor-beta-induced reexpression of the differentiated chondrocyte phenotype without stimulation of collagen synthesis
Exp Cell Res 1993 Feb;204(2):268-77.PMID:8440324DOI:10.1006/excr.1993.1033.
Rabbit articular chondrocytes were treated with retinoic acid (RA) to eliminate the differentiated phenotype marked by the synthesis of type II collagen and high levels of proteoglycan. Exposure of such cells to transforming growth factor-beta 1 (TGF-beta 1) in secondary culture under serum-free and RA-free, defined conditions led to reexpression of the differentiated phenotype. The microfilament modifying drug, Dihydrocytochalasin B (DHCB), enhanced the effectiveness of TGF-beta 1 and produced a threefold stimulation of type II collagen reexpression (measured by 2-D CNBr peptide mapping) at 0.3 ng/ml TGF-beta 1 without altering total collagen synthesis. Type II collagen reexpression was maximal from 1 to 5 ng/ml TGF-beta 1, with or without DHCB. The effect of DHCB on proteoglycan synthesis was maximal at 1 ng/ml TGF-beta 1. At this dose TGF-beta alone produced no increase in 35SO4 incorporation, while simultaneous treatment with DHCB caused a sevenfold stimulation of proteoglycan synthesis. DHCB-independent stimulation proteoglycan reexpression occurred between 5 and 15 ng/ml TGF-beta 1. In contrast, TGF-beta 1-dependent stimulation of proteoglycan synthesis in differentiated chondrocytes in primary monolayer culture was not substantially affected by DHCB. The collagen data suggest that TGF-beta 1 utilizes separate pathways to control phenotypic change and collagen (matrix) synthesis. Microfilament modification by DHCB selectively enhances the effectiveness of the TGF-beta 1-dependent signaling pathway that controls reexpression of the differentiated phenotype.
Modulation of the junctional integrity by low or high concentrations of cytochalasin B and Dihydrocytochalasin B is associated with distinct changes in F-actin and ZO-1
Biosci Rep 1996 Aug;16(4):313-26.PMID:8896790DOI:10.1007/BF01855015.
In a study of Necturus gallbladder epithelium Benzel et al. (Benzel et al., 1980) found that low (0.2-1.2 microM) and higher concentrations (1.5 microM and more) of cytochalasin B (CB) caused an increase and decrease in the transepithelial electrical resistance (TER), respectively. Moreover, there were slight changes in the height and complexicity of tight junction (TJ) strands, as visualized by freeze-fracture and freeze-etching. To elucidate the mechanisms of these findings, we first demonstrated that the effect is also present in monolayers of Madin-Darby Canine Kidney strain 1 (MDCK-1) cells. Thus, a low concentration (0.1 ng/ml) cytochalasin B (CB) strengthened the permeability barrier, as evidenced quantitatively by increases in TER on transepithelial electrical measurements. Furthermore, indirect immunofluorescence and confocal microscopy demonstrated that this effect was paralleled with an accumulation of F-actin and the tight junction marker protein, ZO-1, at the level of TJ. Equimolar concentrations of Dihydrocytochalasin B (dhCB), on the other hand, did not lead to a tightening of the epithelium. Confirming previous studies, there was a general decrease in epithelial resistance after treatment with high concentrations (1 microgram/ml) of CB and dhCB, which was accompanied by distinct changes in the F-actin network and distribution of ZO-1. We speculate that the divergent effects of CB and dhCB on the F-actin and ZO-1 organization might be due to specific effects on the transport of monosaccharides across the plasma membrane, or that CB and dhCB in distinct ways involve the turnover of phosphatidylinositols in the membrane, thereby modulating junctional permeability and F-actin structure.
Fast cell membrane displacements in B lymphocytes. Modulation by Dihydrocytochalasin B and colchicine
FEBS Lett 1991 Nov 18;293(1-2):207-10.PMID:1959663DOI:10.1016/0014-5793(91)81188-e.
A novel type of cell membrane movement was characterized in B lymphocytes. Local submicron cell membrane displacements, within the frequency range 0.3-15 Hz, were registered in a murine lymphoma B cell line by a novel optical method based on point dark field microscopy. The cell membrane displacements were measured by monitoring changes in light scattering from very small illuminated areas (0.25 microns2) at the edge of the cell surface. B lymphocytes manifest a relative change in light scattering of 7.7 +/- 1.3% (mean +/- SD) which corresponds to cell membrane transverse displacement of 131 +/- 22 nm. The confinement of cell membrane displacements to microdomains (less than or equal to 0.2 microns2) emerged from the observed dependence of the displacement amplitude on the area size from which it is monitored. Colchicine (1 microM) decreased membrane fluctuations down to a value of 88 +/- 14 nm, whereas Dihydrocytochalasin B (2 microM) increased the amplitude of membrane displacements up to 184 +/- 31 nm. These findings demonstrate the existence of a dynamic mechanical interaction between the cytoskeleton and the cell membrane in the frequency range of 0.3-15 Hz. The modulation of these interactions by the disruption of microfilaments or or microtubules is explained in terms of the induced strain changes imposed on the cell membrane.