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AAT Bioquest

6XHis maleimide

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Physical properties
Molecular weight1161.22
SolventDMSO
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure

OverviewpdfSDSpdfProtocol


Molecular weight
1161.22
6XHis maleimide is an excellent building block to make 6XHis conjugates for developing His tag detection probes and purification tools. It readily reacts with a biomolecule that contains a thiol group such as antibodies. The 6xHis tag is the most common his-tag and has a molecular weight of ~0.8kDa. His-tags (i.e., polyhistidine tags) comprise a consecutive series of six to ten histidine residues. His tags are used for many recombinant proteins to facilitate purification, allowing researchers to extract a protein of interest from thousands of other proteins found in a cell or cell lysate. The small size of the 6x-His tag has a lower possibility for the tag to affect the functionality of the fusion protein. Histidine forms coordination bonds with immobilized transition metal ions, and this property can be utilized for protein purification. His-tag protein purification is by a specialized form of affinity chromatography, called immobilized metal affinity chromatography (IMAC), where proteins or peptides are separated according to their affinity for metal ions immobilized to a solid chelating resin. During this process, a small His-tag is fused to either the N or C terminus of the target protein, enabling capture by nickel or cobalt ions coordinated on a variety of resins. The small size, low cost, and ease of use have made the His-tag the most popular affinity-tag available. AAT Bioquest offers the largest collection of 6XHis, NTA, bis-NTA, tris-NTA and IDA reagents for His Tag detections and purifications.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of 6XHis maleimide to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM86.116 µL430.582 µL861.163 µL4.306 mL8.612 mL
5 mM17.223 µL86.116 µL172.233 µL861.163 µL1.722 mL
10 mM8.612 µL43.058 µL86.116 µL430.582 µL861.163 µL

Molarity calculator

Enter any two values (mass, volume, concentration) to calculate the third.

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References


View all 6 references: Citation Explorer
Heterologous overexpression of active hexokinases from microsporidia Nosema bombycis and Nosema ceranae confirms their ability to phosphorylate host glucose.
Authors: Dolgikh, Viacheslav V and Tsarev, Alexander A and Timofeev, Sergey A and Zhuravlyov, Vladimir S
Journal: Parasitology research (2019): 1511-1518
Systematic analysis of the expression, solubility and purification of a passenger protein in fusion with different tags.
Authors: Bernier, Sarah C and Cantin, Line and Salesse, Christian
Journal: Protein expression and purification (2018): 92-106
Expression, purification, and functional characterisation of flagellin, a TLR5-ligand.
Authors: Hajam, Irshad Ahmed and Dar, Pervaiz Ahmed and Sekar, Shanmugam Chandra and Nanda, Rajakishore and Kishore, Subodh and Bhanuprakash, Veerakyathappa and Ganesh, Kondabattula
Journal: Veterinaria italiana (2013): 181-6
Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase.
Authors: Maliekal, Pushpa and Vertommen, Didier and Delpierre, Ghislain and Van Schaftingen, Emile
Journal: Glycobiology (2006): 165-72
Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii.
Authors: Grassick, Alice and Murray, Patrick G and Thompson, Roisin and Collins, Catherine M and Byrnes, Lucy and Birrane, Gabriel and Higgins, Timothy M and Tuohy, Maria G
Journal: European journal of biochemistry (2004): 4495-506
Expression of functional melanocortin 1 receptors in insect cells.
Authors: Schiöth, H B and Kuusinen, A and Muceniece, R and Szardenings, M and Keinänen, K and Wikberg, J E
Journal: Biochemical and biophysical research communications (1996): 807-14