Monoclonal Anti-His Tag Antibody
Lot # Check on the product label
Size: 100 μg
Host: Mouse
Reactivity: All
Application: WB, ELISA, IP, IF
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Price: $150.00
Catalog# BTL1010
Lot # Check on the product label
Size 100 μg
Isotype IgG1
Host Mouse
Reactivity All
Specificity
Detect over-expressed or recombinant proteins containing the 6 × His epitope tag.
Product Form Liquid (1mg/ml)
Immunogen
A synthetic peptide 6 × His conjugated to KLH.
Recommend Application
Western Blot (1:5000)
Immunoprecipitation, IP (1:100)
Immunofluorescence, IF (1:2000)
ELISA (1:2000)
Other applications have not been tested.
The optimal dilutions should be determined by end user.
Storage Instruction
Store at -20°C for 1 year. Or aliquot and store at -80°C for long term.
Avoid repeated freeze and thaw cycles.
Background
A polyhistidine-tag is an amino acid motif in proteins that consists of at least five histidine (His) residues, often at the N- or C-terminus of the protein. It is also known as hexa histidine-tag, 6xHis-tag. Polyhistidine-tags are often used for affinity purification of polyhistidine-tagged recombinant proteins expressed in Escherichia coli and other prokaryotic expression systems. Affinity purification using a polyhistidine-tag usually results in relatively pure protein when the recombinant protein is expressed in prokaryotic organisms. Depending on downstream applications including the purification of protein complexes to study protein interactions, purification from higher organisms such as yeasts or other eukaryotes may require a tandem affinity purification using two tags to yield higher purity. The most common polyhistidine tags are formed of six histidine (6xHis tag) residues - preceded by Methionine - which are added at the C-terminal or N-terminal of the protein of interest.
Reference
1. Hengen, P (1995). "Purification of His-Tag fusion proteins from Escherichia coli". Trends in Biochemical Sciences 20 (7): 285–6.
2. Gavin, AC; Bösche, M; Krause, R; Grandi, P; Marzioch, M; Bauer, A; Schultz, J; Rick, JM et al. (2002). "Functional organization of the yeast proteome by systematic analysis of protein complexes". Nature 415 (6868): 141–7.
