7-Fluoro-2,1,3-benzoxadiazole-4-sulfonate (ammonium salt)
(Synonyms: 7-苯并呋咱-4-磺酸铵) 目录号 : GC49312
A thiol-reactive fluorogenic probe
Cas No.:84806-27-9
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
7-Fluoro-2,1,3-benzoxadiazole-4-sulfonate (SBD-F) is a thiol-reactive fluorogenic probe.1 It has been used to quantify the levels of homocysteine, cysteine, and cysteamine in human plasma.2 SBD-F displays excitation/emission maxima of 380/515 nm, respectively.1
1.Imai, K., Toyo’oka, T., and Watanabe, Y.A novel fluorogenic reagent for thiols: Ammonium 7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonateAnal. Biochem.128(2)471-473(1983) 2.Ichinose, S., Nakamura, M., Maeda, M., et al.A validated HPLC-fluorescence method with a semi-micro column for routine determination of homocysteine, cysteine and cysteamine, and the relation between the thiol derivatives in normal human plasmaBiomed. Chromatogr.23(9)935-939(2009)
| Cas No. | 84806-27-9 | SDF | |
| 别名 | 7-苯并呋咱-4-磺酸铵 | ||
| Canonical SMILES | O=S([O-])(C1=CC=C(C2=NON=C21)F)=O.[NH4+] | ||
| 分子式 | C6H2FN2O4S·NH4 | 分子量 | 235.2 |
| 溶解度 | DMF: 30 mg/ml,DMSO: 30 mg/ml,PBS (pH 7.2): 10 mg/ml | 储存条件 | -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 | 4.2517 mL | 21.2585 mL | 42.517 mL |
| 5 mM | 0.8503 mL | 4.2517 mL | 8.5034 mL |
| 10 mM | 0.4252 mL | 2.1259 mL | 4.2517 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。
The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure
Biochim Biophys Acta 1989 Feb 23;994(3):195-9.PMID:2645941DOI:10.1016/0167-4838(89)90293-8.
The positions of the inter- and intra-chain disulfide bonds of human plasma alpha 2 HS-glycoprotein were determined. alpha 2 HS-glycoprotein was digested with acid proteinase and then with thermolysin. The disulfide bonds containing peptides were separated by reversed-phase HPLC and detected by SBD-F (7-fluorobenzo-2-oxa-1,3-diasole-4-sulfonic acid ammonium salt) method. One inter-disulfide bond containing peptide and five intra-disulfide bond containing peptides (A-chain) were purified and identified as Cys-18 (B-chain)--Cys-14 (A-chain), Cys-71--Cys-82, Cys-96--Cys-114, Cys-128--Cys-131, Cys-190--Cys-201 and Cys-212--Cys-229, respectively. The location of the intra-disulfide bonds revealed that the A-chain of alpha 2 HS-glycoprotein is composed of three domains. Two domains were shown to possess intramolecular homology judging from the total chain length of the domains, size of the loops formed by the S--S bonds, the location of two disulfide loops near the C-terminal end of domains A and B, the distance between two S--S bonds of each domain, the amino acid sequence homology between these two domains (22.6%), number of amino acid residues between the second S--S loops and the end of domains A and B, and the positions of the ordered structures.
Positions of disulfide bonds in yam (Dioscorea japonica) acidic class IL (class IV) chitinase
Arch Biochem Biophys 1996 Nov 1;335(1):118-22.PMID:8914841DOI:10.1006/abbi.1996.0488.
Yam acidic class I chitinase belongs to a low molecular weight subclass of class I (class IL; corresponds to class IV) chitinase. The positions of disulfide bonds in this chitinase were examined. Chitinase protein was digested with acid protease and thermolysin, and the resulting disulfide bond containing peptides were separated by reversed-phase HPLC and detected using the SBD-F (7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonic acid ammonium salt) method. Four intradisulfide bonds containing peptides were purified and three disulfide bonds in the catalytic domain were identified as Cys-66 and Cys-115, Cys-128 and Cys-136, and Cys-218 and Cys-250. Location of disulfide bonds in the catalytic domain was identical to that of barley class II chitinase but different from rye class II chitinase at the C-terminal. Conservation of S-S bonds at the N-terminal half of the catalytic domain between class I and class II chitinases strongly suggests that this region is important for formation of the active site.