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GenScript
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Reconstitute the lyophilized antibody with deionized water (or equivalent) to a final concentration of 0.5 mg/ml.
Monoclonal antibodies specific to six histidine tags can greatly improve the effectiveness of several different kinds of immunoassays, helping researchers identify, detect, and purify polyhistidine fusion proteins in bacteria, insect cells, and mammalian cells. However, since 6XHis-tag is poorly immunogenic, it needs to be conjugated to KLH or some other carrier as an immunogen. After hundreds of selection cycles, researchers at GenScript successfully isolated an antibody against His-tag. THE™ His Tag Antibody, mAb, Mouse (subtype IgG1) has very high affinity. Tests performed at GenScript show that the antibody can also recognize 4xHis- and 5xHis-tags. This means that even if the 6xHis-tag is only partially exposed, it will still be recognized and bound by this antibody. THE™ His Tag mAb is produced from mice ascites and purified by protein A affinity column. This antibody recognizes native as well as denatured forms of synthetic polyhistidine and polyhistidine-tagged fusion proteins. The product reacts with fusion proteins expressed in bacteria, insect cells, and mammalian cells. THE™ His Tag mAb recognizes His tags placed at N-terminal, C-terminal, and internal regions of fusion proteins. THE™ His Tag mAb can be used in Western blot analyses, Dot blot analyses, ELISA, immunofluorescent staining, and flow cytometry of cultured cells.
The 6x His tag is a synthetic oligo peptide consisting of 6 consecutive histidine residues (HHHHHH). The His tag is commonly expressed as a tag at either N-or C-terminal regions of recombinant proteins to allow isolation or purification by immobilized metal affinity chromatography. Epitope tagging is a technique in which a known epitope is fused to a recombinant protein using genetic engineering. By choosing a particular epitope and recombinant protein combination, epitope tagging makes it possible to detect proteins for which no antibody is available. His epitope tagged proteins that contain a stretch of histidine residues at the carboxyl or amino terminus are used for purification of recombinant proteins by means of metal chelate chromatography due to metal binding properties of histidine clusters on His tagged proteins. For example, the affinity of the histidine-tag motif to Ni2+ by chelation is strong and selective enough to enable purification of the protein to homogeneity by affinity chromatography on a Ni2+-NTA adsorbent. His tag-specific antibodies are used to facilitate detection or coimmunopreciptation of tagged proteins.
仅用于科研。不用于诊断过程。未经明确授权不得转售。