Mouse Monoclonal Antibody
Catalog No. H99-61M
Catalog No. | Pack Size | Price (USD) | |
---|---|---|---|
H99-61M-100 | 100 ug | $248 | |
H99-61M-BULK | BULK | Contact Us |
Overview:
This polyhistidine epitope tag is generally comprised of six consecutive histidine amino acid residues located at the N-terminal, C-terminal, or internally [1]. The 6 His-Tag is widely used because of its affinity to bind nickel or cobalt metal ions attached to sepharose, which can then be used to purify the protein in a native or denatured state [2].
References:
1. Jonathan, W. et al: Epitope tagging, Annual Review of Genetics, 1998; 32, 601-618
2. Schmeisser, H, et al:, Binding Characteristics of IFN-alpha Subvariants to IFNAR2-EC and Influence of the 6-Histidine Tag. J Interferon Cytokine Res. 2006; Dec. 26(12):866-76.
Specificity:
Anti-His antibody recognizes the N-terminal, C-terminal or internal 6X His-tagged fusion protein.
Cross Reactivity:
All proteins tagged with 6X His
Host / Isotype / Clone#:
Mouse, IgG2b, EH158
Immunogen:
HHHHHH peptide conjugated to KLH
Purification:
Purified by Protein A affinity chromatography from mouse ascites fluid
Stability:
Store at 4°C (add 0.1% NaN3) for several months, and at -20°C for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For optimal performance, avoid repeated handling and multiple freeze/thaw cycles.
Sample Data:
Representative western blot (1:1000) using in a positive cell lysate that contains His tagged fusion protein.
Flora Huanga Chia-Chi et al., Intermolecular Binding between TIFA-FHA and TIFA-pT Mediates Tumor Necrosis Factor Alpha Stimulation and NF-?B Activation Molecular and Cellular Biology July 2012 10.1128/MCB.00438-12
jia Liu Zhen et al., Tyrosine sulfation in N-terminal domain of human C5a receptor is necessary for binding of chemotaxis inhibitory protein of Staphylococcus aureus Acta Pharmacologia Sinica June 2011 10.1038/aps.2011.53
et al., Linker and N-Terminal Domain Engineering of Pyrrolysyl-tRNA Synthetase for Substrate Range Shifting and Activity Enhancement Frontiers in Bioengineering and Biotechnology April 2020
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