10XHis Succinimidyl Ester
10XHis succinimidyl ester is an excellent building block to make 10XHis conjugates for developing His tag detection probes and purification tools. It readily reacts with a biomolecule that contains an amino group such as antibodies, peptides and amino-modified oligos. The 10XHis tag is one of the most common His tags and has a molecular weight of ~2kDa. 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 10X-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, 0XHis, NTA, bis-NTA, tris-NTA and IDA reagents for His Tag detections and purifications.
References
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Structural and biochemical insights into His-tag-induced higher-order oligomerization of membrane proteins by cryo-EM and size exclusion chromatography.
Authors: Ayoub, Nooraldeen and Roth, Patrick and Ucurum, Zöhre and Fotiadis, Dimitrios and Hirschi, Stephan
Journal: Journal of structural biology (2023): 107924
Authors: Ayoub, Nooraldeen and Roth, Patrick and Ucurum, Zöhre and Fotiadis, Dimitrios and Hirschi, Stephan
Journal: Journal of structural biology (2023): 107924
Ni aptamer: DNA mimic of His-tag to recognize Ni-NTA.
Authors: Jahan, Raunak and Silwal, Achut Prasad and Thennakoon, Siddhartha Kalpa Samadhi and Arya, Satya Prakash and Postema, Rick Mason and Timilsina, Hari and Reynolds, Andrew Michael and Tan, Xiaohong
Journal: Chemical communications (Cambridge, England) (2023): 12851-12854
Authors: Jahan, Raunak and Silwal, Achut Prasad and Thennakoon, Siddhartha Kalpa Samadhi and Arya, Satya Prakash and Postema, Rick Mason and Timilsina, Hari and Reynolds, Andrew Michael and Tan, Xiaohong
Journal: Chemical communications (Cambridge, England) (2023): 12851-12854
N-terminal LysSN-His-tag improves the production of intracellular recombinant protein in Bacillus subtilis.
Authors: Le, Ngan Thi Phuong and Phan, Trang Thi Phuong and Truong, Tuom Thi Tinh and Schumann, Wolfgang and Nguyen, Hoang Duc
Journal: Cell biochemistry and function (2023): 823-832
Authors: Le, Ngan Thi Phuong and Phan, Trang Thi Phuong and Truong, Tuom Thi Tinh and Schumann, Wolfgang and Nguyen, Hoang Duc
Journal: Cell biochemistry and function (2023): 823-832
Expression of a Copper Activated Xylanase in Yeast: Location of the His-Tag in the Protein Significantly Affects the Enzymatic Properties.
Authors: Elgharbi, Fatma and Ben Hlima, Hajer and Ben Mabrouk, Sameh and Hmida-Sayari, Aïda
Journal: Molecular biotechnology (2023): 1109-1118
Authors: Elgharbi, Fatma and Ben Hlima, Hajer and Ben Mabrouk, Sameh and Hmida-Sayari, Aïda
Journal: Molecular biotechnology (2023): 1109-1118
Development of a Modular NTA:His Tag Viral Vaccine for Co-delivery of Antigen and Adjuvant.
Authors: Chung, Young Hun and Volckaert, Britney A and Steinmetz, Nicole F
Journal: Bioconjugate chemistry (2023): 269-278
Authors: Chung, Young Hun and Volckaert, Britney A and Steinmetz, Nicole F
Journal: Bioconjugate chemistry (2023): 269-278
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