GMBS
(Synonyms: 4-马来酰亚胺基丁酸-N-羟基琥珀酰亚胺酯) 目录号 : GC38175
GMBS 是一种双功能的交联剂。
Cas No.:80307-12-6
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
GMBS is a heterobifunctional cross-linker.
[1]. Ding YH, et al. Increasing the Depth of Mass-Spectrometry-Based Structural Analysis of Protein Complexes through the Use of Multiple Cross-Linkers. Anal Chem. 2016 Apr 19;88(8):4461-9.
| Cas No. | 80307-12-6 | SDF | |
| 别名 | 4-马来酰亚胺基丁酸-N-羟基琥珀酰亚胺酯 | ||
| Canonical SMILES | O=C(ON1C(CCC1=O)=O)CCCN2C(C=CC2=O)=O | ||
| 分子式 | C12H12N2O6 | 分子量 | 280.23 |
| 溶解度 | Soluble in DMSO | 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 | 3.5685 mL | 17.8425 mL | 35.685 mL |
| 5 mM | 0.7137 mL | 3.5685 mL | 7.137 mL |
| 10 mM | 0.3568 mL | 1.7842 mL | 3.5685 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。
Preparation of monoclonal antibodies against N-(gamma-maleimidobutyryloxy)succinimide (GMBS)-conjugated acetylspermine, and development of an enzyme-linked immunosorbent assay (ELISA) for N1,N12-diacetylspermine
J Biochem 1998 Jul;124(1):244-9.PMID:9644270DOI:10.1093/oxfordjournals.jbchem.a022088.
We have developed three mouse monoclonal antibodies (mAb) of types IgG1 and IgG2b, i.e. anti-acetylspermine (Ac-Spm)-1 and 2 (ACSPM-1 and 2), and anti-acetylspermine (Ac-Spm)-3 (ACSPM-3), respectively, against Ac-Spm conjugated to bovine serum albumin via a heterobifunctional cross-linker, N-(gamma-maleimidobutyryloxy)succinimide (GMBS). Among these mAbs, ACSPM-2 was the most useful for the development of an enzyme-linked immunosorbent assay (ELISA) for acetylpolyamines (Ac-PAs) with glutaraldehyde (GA)-conjugated N1,N12-diacetylspermine (2Ac-Spm) or acetylspermine (Ac-Spm) as the solid phase antigen. However, GMBS-conjugated Ac-Spm did not behave as a solid phase antigen in the competitive ELISA. The ELISA is based on the principle of competition between an analyte and the conjugated antigen for the mAb, followed by immunoreaction with biotinylated anti-mouse immunoglobulin and horseradish peroxidase-streptavidin. The ACSPM-2 mAb reacted with 2Ac-Spm to the highest degree, followed by Ac-Spm, N1-acetylspermidine (N1-Ac-Spd), N8,N8-diacetylspermidine (2Ac-Spd), and spermine (Spm), the EC50 values being 0.06, 0.25, 7.0, 10, and 60 microM, respectively, but exhibited almost no cross-reaction with other polyamine-related compounds or amino acids. The method was used to determine the urinary Ac-PA levels in healthy subjects, the average value of 0.36 microg of 2Ac-Spm/g creatinine (n = 16) being obtained. The ACSPM-2 ELISA for 2Ac-Spm, which was the PA most relevant to the analysis of human urine among the five PA analogs mentioned above, might have potential for elucidation of the correlation of urinary 2Ac-Spm levels in cancers.
Intrinsic and extrinsic factors influence on an omnivore's gut microbiome
PLoS One 2022 Apr 8;17(4):e0266698.PMID:35395042DOI:10.1371/journal.pone.0266698.
Gut microbiomes (GMBS), complex communities of microorganisms inhabiting the gastrointestinal tracts of their hosts, perform countless micro-ecosystem services such as facilitating energy uptake and modulating immune responses. While scientists increasingly recognize the role GMBS play in host health, the role of GMBS in wildlife ecology and conservation has yet to be realized fully. Here, we use brown bears (Ursus arctos) as an ecological model to (1) characterize GMB community composition associated with location, season, and reproductive condition of a large omnivore; (2) investigate how both extrinsic and intrinsic factors influence GMB community membership and structure; and (3) quantify differences in GMB communities among different locations, seasons, sex, and reproductive conditions. To achieve these aims, we subsampled brown bear fecal samples collected during United States National Park Service research activities at three National Parks and Preserves (Katmai, Lake Clark, and Gates of the Arctic) and extracted microbial DNA for 16S rRNA amplicon sequencing and microbial taxonomic classification. We analyzed GMB communities using alpha and beta diversity indices, subsequently using linear mixed models to examine relationships between alpha diversity and extrinsic and intrinsic factors. Katmai brown bears hosted the greatest alpha diversity, whereas Gates brown bears hosted the least alpha diversity. Our results indicate that location and diet drive GMB variation, with bears hosting less phylogenetic diversity as park distance inland increases. Monitoring brown bear GMBS could enable managers to quickly detect and assess the impact of environmental perturbations on brown bear health. By integrating macro and micro-ecological perspectives we aim to inform local and landscape-level management decisions to promote long-term brown bear conservation and management.
Chitosan modification of adenovirus to modify transfection efficiency in bovine corneal epithelial cells
PLoS One 2010 Aug 10;5(8):e12085.PMID:20711466DOI:10.1371/journal.pone.0012085.
Background: The purpose of this study is to modulate the transfection efficiency of adenovirus (Ad) on the cornea by the covalent attachment of chitosan on adenoviral capsids via a thioether linkage between chitosan modified with 2-iminothiolane and Ad cross-linked with N-[gamma-maleimidobutyryloxy]succinimide ester (GMBS). Methodology/principal findings: Modified Ad was obtained by reaction with the heterobifunctional crosslinking reagent, GMBS, producing maleimide-modified Ad (Ad-GMBS). Then, the chitosan-SH was conjugated to Ad-GMBS via a thioether bond at different ratios of Ad to GMBS to chitosan-SH. The sizes and zeta potentials of unmodified Ad and chitosan-modified Ads were measured, and the morphologies of the virus particles were observed under transmission electron microscope. Primary cultures of bovine corneal epithelial cells were transfected with Ads and chitosan-modified Ads in the absence or presence of anti-adenovirus antibodies. Chitosan modification did not significantly change the particle size of Ad, but the surface charge of Ad increased significantly from -24.3 mV to nearly neutral. Furthermore, primary cultures of bovine corneal epithelial cells were transfected with Ad or chitosan-modified Ad in the absence or presence of anti-Ad antibodies. The transfection efficiency was attenuated gradually with increasing amounts of GMBS. However, incorporation of chitosan partly restored transfection activity and rendered the modified antibody resistant to antibody neutralization. Conclusions/significance: Chitosan can provide a platform for chemical modification of Ad, which offers potential for further in vivo applications.
Enhanced iron(III) reduction following amendment of paddy soils with biochar and glucose modified biochar
Environ Sci Pollut Res Int 2018 Jan;25(1):91-103.PMID:27858276DOI:10.1007/s11356-016-8081-3.
Although biochar application to paddy fields has been widely studied, its effects on Fe(III) reduction have not yet been investigated. Paddy soil slurry and soil microbial inoculation incubation were conducted with unmodified biochar (UMB) or glucose-modified biochar (GMB) additions at different particle sizes. The Fe(II) concentration and pH value were determined regularly, and Fe(III) reducing capacity (FeRC) was evaluated by modeling. Fe(III) reduction potential (a) was increased by 0-1.96 mg g-1 in response to UMBs addition, and a more remarkable increase in a was related to the decrease of particle size. The dissolved organic carbon of UMBs was responsible for the majority of the biochar reducing capacity. UMBs addition increased the contribution of free Fe and nitrate nitrogen to FeRC, while it decreased that of available phosphorus. Moreover, GMBS led to greater promotion of FeRC than the corresponding UMBs, with an increase in a of 2.9-16% in soil slurry and reduction rate of 13-35% in microbial inoculation incubation. The maximum Fe(III) reduction rate (V max) with GMBS addition was faster or invariable than UMBs, while the time to V max (T Vmax) was shorter or stable. The effect of GMBS on Fe(III) reduction was less sensitive as GMB particle size increased. Compared with UMBs addition, pH declined remarkably in response to GMBS. These findings suggest that GMBS can effectively stimulate Fe(III) reduction in paddy fields, while simultaneously alleviating the pH increase usually caused by pristine biochar application.
Increasing the Depth of Mass-Spectrometry-Based Structural Analysis of Protein Complexes through the Use of Multiple Cross-Linkers
Anal Chem 2016 Apr 19;88(8):4461-9.PMID:27010980DOI:10.1021/acs.analchem.6b00281.
Chemical cross-linking of proteins coupled with mass spectrometry (CXMS) is a powerful tool to study protein folding and to map the interfaces between interacting proteins. The most commonly used cross-linkers in CXMS are BS(3) and DSS, which have similar structures and generate the same linkages between pairs of lysine residues in spatial proximity. However, there are cases where no cross-linkable lysine pairs are present at certain regions of a protein or at the interface of two interacting proteins. In order to find the cross-linkers that can best complement the performance of BS(3) and DSS, we tested seven additional cross-linkers that either have different spacer arm structures or that target different amino acids (BS(2)G, EGS, AMAS, GMBS, Sulfo-GMBS, EDC, and TFCS). Using BSA, aldolase, the yeast H/ACA protein complex, and E. coli 70S ribosomes, we showed that, in terms of providing structural information not obtained through the use of BS(3) and DSS, EGS and Sulfo-GMBS worked better than the other cross-linkers that we tested. EGS generated a large number of cross-links not seen with the other amine-specific cross-linkers, possibly due to its hydrophilic spacer arm. We demonstrate that incorporating the cross-links contributed by the EGS and amine-sulfhydryl cross-linkers greatly increased the accuracy of Rosetta in docking the structure of the yeast H/ACA protein complex. Given the improved depth of useful information it can provide, we suggest that the multilinker CXMS approach should be used routinely when the amount of a sample permits.