N-Bromoacetamide
(Synonyms: N-溴代乙酰胺) 目录号 : GC65231
N-Bromoacetamide 能不可逆地去除细胞膜胞质表面的钠离子通道失活，也能降低钾离子电流的快速失活。
Cas No.:79-15-2
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
N-Bromoacetamide can irreversibly remove sodium channel inactivation in the cytoplasmic face of the membrane, also decreasing K current rapid inactivation[1][2].
[1]. Matteson DR, et al. Modification of K channel inactivation by papain and N-bromoacetamide. Biophys J. 1988;53(4):641-645.
[2]. Patlak J, et al. Effect of N-bromoacetamide on single sodium channel currents in excised membrane patches. J Gen Physiol. 1982;79(3):333-351.
| Cas No. | 79-15-2 | SDF | Download SDF |
| 别名 | N-溴代乙酰胺 | ||
| 分子式 | C2H4BrNO | 分子量 | 137.96 |
| 溶解度 | 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 | 7.2485 mL | 36.2424 mL | 72.4848 mL |
| 5 mM | 1.4497 mL | 7.2485 mL | 14.497 mL |
| 10 mM | 0.7248 mL | 3.6242 mL | 7.2485 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。
N-Bromoacetamide removes a calcium-dependent component of channel opening from calcium-activated potassium channels in rat skeletal muscle
J Gen Physiol 1985 Nov;86(5):601-11.PMID:2415669DOI:10.1085/jgp.86.5.601.
Calcium-activated potassium channels from cultured rat skeletal muscle were treated with the protein-modifying reagent N-Bromoacetamide (NBA) (0.3-1 mM) and studied in excised patches using patch-clamp techniques. After NBA treatment, channels opened only occasionally, and, in contrast to untreated channels, the open probability was no longer sensitive to intracellular surface calcium ions (1 nM to 100 microM). Channel activity did, however, exhibit a voltage dependence similar in direction and magnitude to that shown before NBA treatment (increasing e-fold with 19 mV depolarization). Distributions of open channel lifetimes revealed that NBA treatment virtually abolished openings of long duration, which suggests that this class of openings requires calcium sensitivity. These effects were not reversed by subsequent washing. Quantitatively similar open probability, voltage dependence, and open-interval distributions were observed in untreated channels in calcium-free medium. These results suggest that NBA removed a calcium-dependent component of channel opening, and that normal channels are able to open in the absence of significant intracellular calcium concentrations.
K3PO4-catalyzed regiospecific aminobromination of beta-nitrostyrene derivatives with N-Bromoacetamide as aminobrominating agent
J Org Chem 2010 Mar 19;75(6):2085-8.PMID:20170090DOI:10.1021/jo9026879.
A very simple, efficient, and regiospecific protocol for aminobromination of a wide scope of beta-nitrostyrene derivatives with N-Bromoacetamide (NBA) as nitrogen/bromine sources has been developed by using K(3)PO(4) as catalyst. The reaction proceeded smoothly and cleanly to give the bromoamines in good to excellent yields (78-99%) within 24 h in CH(2)Cl(2) at room temperature without protection of inert gases. A possible mechanism involving a nucleophilic conjugate addition was proposed.
Effect of N-Bromoacetamide on single sodium channel currents in excised membrane patches
J Gen Physiol 1982 Mar;79(3):333-51.PMID:6281357DOI:10.1085/jgp.79.3.333.
We have studied the effect of N-Bromoacetamide (NBA) on the behavior of single sodium channel currents in excised patches of rat myotube membrane at 10 degree C. Inward sodium currents were activated by voltage steps from holding potentials of about -100 mV to test potentials of -40 mV. The cytoplasmic-face solution was isotonic CsF. Application of NBA or pronase to the cytoplasmic face of the membrane irreversibly removed sodium channel inactivation, as determined by averaged single-channel records. Teh lifetime of the open channel at -40 mV was increased about 10-fold by NBA treatment without affecting the amplitude of single-channel currents. A binomial analysis was used both before and after treatment to determine the number of channels within the excised patch. NBA was shown to have little effect on activation kinetics, as determined by an examination of both the rising phase of averaged currents and measurements f the delay between the start of the pulse and the first channel opening. Our data support a kinetic model of sodium channel activation in which the rate constant leading back from the open state to the last closed state is slower than expected from a strict Hodgkin-Huxley model. The data also suggest that the normal open-channel lifetime is primarily determined by the inactivation process in the voltage range we have examined.
Voltage-dependent removal of sodium inactivation by N-Bromoacetamide and pronase
Biophys J 1985 Apr;47(4):567-71.PMID:2580570DOI:10.1016/S0006-3495(85)83952-7.
When perfused internally through crayfish giant axons, pronase removed sodium inactivation more than three times as fast at -100 mV as compared with -30 mV. N-Bromoacetamide, applied internally, removed sodium inactivation twice as fast at -100 mV as at -30 mV, and the relative rate of removal declined with membrane depolarization in proportion to steady-state sodium inactivation. We conclude that in the closed conformation the sodium inactivation gate is partially protected from destruction by N-Bromoacetamide and pronase.
N-Bromoacetamide-mediated domino cyclization and elimination of homoallylic trichloroacetimidates: a novel approach toward the synthesis of 1-bromo-2-amino-3-butene derivatives
Org Biomol Chem 2014 Sep 14;12(34):6653-60.PMID:25029658DOI:10.1039/c4ob01126k.
A practical synthesis of 1-bromo-2-amino-3-butene derivatives from homoallylic trichloroacetimidates was reported. Simply heating the mixture of substrates and N-Bromoacetamide in DMF at 90 °C would give the desired products in moderate to excellent yields. The reaction may proceed through a domino bromo-cyclization and elimination pathway. The synthesis of 4,5-dihydrooxazoles from 1-bromo-2-amino-3-butene derivatives was also investigated.