Hexa-His
目录号 : GC36221
Hexa-His 是由 6 个组氨酸构成的六肽，常作为融合蛋白的金属结合位点。
Cas No.:64134-30-1
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.50%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Hexa-His is a peptide consisting of 6 His residues, used as a metal binding site for the recombinant protein.
[1]. Watly J, et al. Insight into the coordination and the binding sites of Cu(2+) by the histidyl-6-tag using experimental and computational tools. Inorg Chem. 2014 Jul 7;53(13):6675-83.
| Cas No. | 64134-30-1 | SDF | |
| 分子式 | C36H44N18O7 | 分子量 | 840.85 |
| 溶解度 | Water: 50 mg/mL (59.46 mM) | 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 | 1.1893 mL | 5.9464 mL | 11.8927 mL |
| 5 mM | 0.2379 mL | 1.1893 mL | 2.3785 mL |
| 10 mM | 0.1189 mL | 0.5946 mL | 1.1893 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。
Interaction of Hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase
Int J Biol Macromol 2011 Nov 1;49(4):778-83.PMID:21839770DOI:10.1016/j.ijbiomac.2011.07.014.
We have previously reported that amino-terminal extension sequence containing Hexa-His facilitated refolding and assembly of hexameric nucleoside diphosphate kinase from extremely halophilic archaeon Halobacterium salinarum (NDK). In this study, we made various mutations in both the tag sequence and within NDK molecule. SerNDK, in which Hexa-His was replaced with hexa-Ser, showed no facilitated folding. In addition, HisD58GD63G, in which both Asp58 and Asp63 in NDK were replaced with Gly, also showed no refolding enhancement. These results suggest that Hexa-His in His-tag interact cooperatively with either Asp58 or Asp63 or both. Furthermore, G114D mutant, which formed a dimer in low salt solution, was strongly stabilized by His-tag to form a stable hexamer.
Bioadsorption of cadmium ion by cell surface-engineered yeasts displaying metallothionein and Hexa-His
Appl Microbiol Biotechnol 2003 Dec;63(2):182-6.PMID:12898063DOI:10.1007/s00253-003-1399-z.
The Cd(2+)-chelating abilities of yeast metallothionein (YMT) and Hexa-His displayed on the yeast-cell surface were compared. Display of YMT and Hexa-His by alpha-agglutinin-based cell-surface engineering was confirmed by immunofluorescent labeling. Surface-engineered yeast cells with YMT and Hexa-His fused in tandem showed superior cell-surface adsorption and recovery of Cd2+ under EDTA treatment on the cell surface than hexa-His-displaying cells. YMT was demonstrated to be more effective than Hexa-His for the adsorption of Cd2+. Yeast cells displaying YMT and/or Hexa-His exhibited a higher potential for the adsorption of Cd2+ than Escherichia coli cells displaying these molecules. In order to investigate the effect of the displayed YMT and Hexa-His on sensitivity to toxic Cd2+, growth in Cd(2+)-containing liquid medium was monitored. Unlike hexa-His-displaying cells, cells displaying YMT and Hexa-His fused in tandem induced resistance to Cd2+ through active and enhanced adsorption of toxic Cd2+. These results indicate that YMT-displaying yeast cells are a unique bioadsorbent with a functional chelating ability superior to that of E. coli.
Recombinant production and affinity purification of the FraC pore forming toxin using Hexa-His tag and pET expression cassette
Iran J Basic Med Sci 2017 Apr;20(4):380-385.PMID:29026495DOI:10.22038/IJBMS.2017.8577.
Objectives: A newly-introduced protein toxin from a sea anemone, namely fragaceatoxin C is a protein with molecular weight of 20 kDa and pore-forming capability against cell membranes has recently grasped great attentions for its function. In this study, its coding sequence cloned as a fusion protein with His-tag for simple production and rapid purification. Materials and methods: After PCR amplification using NcoI and HindIII-harboring primers, the gene fragment was cloned into pET-28a(+). Escherichia coli BL21 was used for expression of constructed vector and toxin expression was verified by SDS-PAGE. For one-step purification Ni-NTA sepharose affinity chromatography was employed. For examination of purified toxin function, RBC hemolytic test was conducted. Results: The results showed that the FraC-coding gene was successfully cloned between NcoI and HindIII restriction sites and purified with affinity chromatography. Densitometric analysis represented the purity of approximately 97%. Hemolytic test indicated the purified FraC had remarkable lytic activity on RBC and almost lysed 50% of cells at the concentration value of 6.25 nM. Conclusion: The results indicated that not only purified toxin preserved its activity during expression and purification processes but also exerted its function at lower concentrations so that even the 0.09 nM displayed hemolytic effect.
Cell surface-engineered yeast displaying a histidine oligopeptide (Hexa-His) has enhanced adsorption of and tolerance to heavy metal ions
Appl Microbiol Biotechnol 2001 Dec;57(5-6):697-701.PMID:11778880DOI:10.1007/s002530100813.
A histidine oligopeptide (Hexa-His) with the ability to chelate divalent heavy metal ions was displayed on the yeast cell surface for the purpose of enhanced adsorption of heavy metal ions. We genetically fused a hexa-His-encoding gene with the gene encoding the C-terminal half of alpha-agglutinin that includes a glycosylphosphatidylinositol anchor attachment signal sequence and attached the Hexa-His peptide on the cell wall of Saccharomyces cerevisiae. This surface-engineered yeast adsorbed three to eight times more copper ions than the parent strain and was more resistant to copper (4 mM) than the parent (below 1 mM at pH 7.8). It was possible to recover about a half of the copper ions adsorbed by whole cells with EDTA treatment without disintegrating the cells. Thus, we succeeded in constructing a novel yeast cell with both tolerance to toxic contaminants and enhanced adsorption of metal ions onto the cell surface.
Enhanced metalloadsorption of bacterial cells displaying poly-His peptides
Nat Biotechnol 1996 Aug;14(8):1017-20.PMID:9631043DOI:10.1038/nbt0896-1017.
The properties of Escherichia coli cells, acquired by cell surface presentation of one or two hexahistidine (His) clusters carried by the outer membrane LamB protein, have been examined. Strains producing LamB hybrids with the His chains accumulated greater than 11-fold more Cd2+ than E. coli cells expressing the protein without the His insert. Furthermore, the Hexa-His chains on the cell surface caused cells to adhere reversibly to a Ni(2+)-containing solid matrix in a metal-dependent fashion. Thus, expression of poly-His peptides enables bacteria to act as a metalloaffinity adsorbent. These results open up the possibility for biosorption of heavy ions using engineered microorganisms.