catalog number :
MBS355032
products full name :
His tag(HRP Conjugated) tag antibody
products short name :
[His Tag (HRP Conjugated)]
products name syn :
[Monoclonal Anti-His Tag (HRP Conjugated)]
specificity :
Detect over-expressed or recombinant proteins containing the 6 × His epitope tag.
storage stability :
Store at -20 degree C for 1 year. Or aliquot and store at -80 degree C for long term. Avoid repeated freeze and thaw cycles
tested application :
Western Blot (WB)
app notes :
Western Blot (1:1000-10000). Other applications have not been tested. The optimal dilutions should be determined by end user.
products categories :
Tag & Loading Control Antibodies
products description :
Background/Introduction: 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.
products references :
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.