His-Tag (27E8) Mouse mAb

• 产品编号：CST-2366P      品牌：Cell Signaling Technology       原厂货号：2366P
• 产品分类：抗体 > 一抗 > 表位标签和报告基因特异性抗体
• 应用分类：

描述：

His-Tag (27E8) Mouse mAb仅识别6xHis标签，此抗体可以识别转染细胞靶蛋白在氨基或羧基末端融合的6xHis-tag 。单克隆抗体是用含有流感血凝素表位(YPYDVPDYA的合成肽段肽段免疫动物生产的。在免疫印迹、免疫沉淀和免疫染色等技术中，表位标签用于标记和检测蛋白。由于它们的体积很小，它们一般不会影响标记蛋白的生化特性。很多质粒包含一种DNA，可以编码氨基末端带有6个组氨酸（ 6xHis) ）残基，其后为延伸的多克隆结合位点（1）， 于其它蛋白标签系统一样（2），这种多组氨酸标签常在剪切位点被蛋白酶剪切，如凝血酵素和肠激酶，用于分离所需要的蛋白（1）。

样（2），这种多组氨酸标签常在剪切位点被蛋白酶剪切，如凝血酵素和肠激酶，用于分离所需要的蛋白（1）。

1. Kroll, D.J. et al. (1993) DNA Cell Biol. 12, 441-453.
2. di Guan, C. et al. (1988) Gene 67, 21-30.

原厂资料：

Specificity / Sensitivity

His-Tag (27E8) Mouse mAb detects recombinant proteins containing the 6xHis epitope tag. The antibody recognizes the 6xHis-tag fused to either the amino or carboxy terminus of targeted proteins in transfected cells.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a 6xHis synthetic peptide.

Background

Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation and immunostaining techniques. Due to their small size, they are unlikely to affect the tagged protein's biochemical properties.A variety of plasmids contain DNA that encodes an amino-terminal tag cosisting of six histidine (6xHis) residues followed by an extended multiple cloning site. The 6xHis tag on the expressed recombinant proteins allows for efficient coupling to Ni2+ affinity resins and purification by single step chromatography (1).As is the case with other protein tag systems (2), this polyhistidine tag can often be cleaved at sites recognized by proteases such as thrombin and enterokinases to isolate the protein of interest (1).

样（2），这种多组氨酸标签常在剪切位点被蛋白酶剪切，如凝血酵素和肠激酶，用于分离所需要的蛋白（1）。

1. Kroll, D.J. et al. (1993) DNA Cell Biol. 12, 441-453.
2. di Guan, C. et al. (1988) Gene 67, 21-30.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150
mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02%
sodium azide. Store at –20°C. Do not aliquot the antibody.