Key features and details
- Mouse monoclonal [R29.6] to Maltose Binding Protein
- Suitable for: IP, WB, ChIP, ICC/IF
- Isotype: IgG1
Product nameAnti-Maltose Binding Protein antibody [R29.6]
See all Maltose Binding Protein primary antibodies
DescriptionMouse monoclonal [R29.6] to Maltose Binding Protein
Tested applicationsSuitable for: IP, WB, ChIP, ICC/IFmore details
MOS maltose binding protein fusion protein.
General notesMBP is a bacterial protein, which is also used as a fusion protein in expression constructs.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Concentration information loading...
PurityProtein A purified
Light chain typeunknown
ChIP Related Products
Our Abpromise guarantee covers the use of ab65 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IP||Use at an assay dependent concentration.|
|WB||Use at an assay dependent concentration.|
|ChIP||Use at an assay dependent concentration.|
|ICC/IF||Use at an assay dependent concentration. PubMed: 12496278|
RelevanceEpitope tagging offers an easy and universal strategy for the identification and purification of proteins derived by recombinant DNA technology. The insertion of a Maltose Binding Protein (MBP) tag creates a stable fusion product that does not interfere with the bioactivity of the protein or with the biodistribution of the MBP tagged product. Cleavage by factor Xa separates MBP from its partner protein.
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Immunofluorescence analysis of Saos-2 cells, transfected with full-length MBP-Apoptin and MBP-Apoptin(80–121). After fixation, the cells were stained for Maltose Binding Protein using ab65. Nuclear morphology is indicated by DAPI staining.
Representative western blot detecting Maltose Binding Protein using ab65 at 1.8 µg/ml.
ab65 has been referenced in 6 publications.
- Kamennaya NA & Post AF Characterization of cyanate metabolism in marine Synechococcus and Prochlorococcus spp. Appl Environ Microbiol 77:291-301 (2011). PubMed: 21057026
- Im YJ et al. Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. Dev Cell 17:234-43 (2009). PubMed: 19686684
- Verhoeven GS et al. Differential bacterial surface display of peptides by the transmembrane domain of OmpA. PLoS One 4:e6739 (2009). WB . PubMed: 19707582
- Liu X et al. Whole-genome comparison of Leu3 binding in vitro and in vivo reveals the importance of nucleosome occupancy in target site selection. Genome Res 16:1517-28 (2006). PubMed: 17053089
- Liu X et al. DIP-chip: rapid and accurate determination of DNA-binding specificity. Genome Res 15:421-7 (2005). ChIP ; Saccharomyces cerevisiae . PubMed: 15710749
- Leliveld SR et al. Apoptin induces tumor-specific apoptosis as a globular multimer. J Biol Chem 278:9042-51 (2003). ICC/IF . PubMed: 12496278