Anti-MBP [R29.6]

Cat. #151017

Anti-MBP [R29.6]

Cat. #: 151017

Sub-type: Primary antibody

Unit size: 100 ug

Availability: 3-5 days

Target: Maltose binding protein (MBP)

Class: Monoclonal

Application: ChIP ; IHC ; IF ; IP ; WB

Reactivity: Bovine

Host: Mouse


This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.


Inventor: Julian Gannon

Institute: Cancer Research UK, London Research Institute: Clare Hall Laboratories

Tool Details
Target Details

Tool Details

*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)

  • Name: Anti-MBP [R29.6]
  • Alternate name: CCNA1; Cyclin A1; Testicular Tissue Protein Li 34; CT146
  • Research fields: Cell biology;Neurobiology
  • Clone: R29.6
  • Tool sub type: Primary antibody
  • Class: Monoclonal
  • Conjugation: Unconjugated
  • Molecular weight: 53 kDa
  • Reactivity: Bovine
  • Host: Mouse
  • Application: ChIP ; IHC ; IF ; IP ; WB
  • Description: R29.6 is useful for detection and isolation of recombinant MBP fusion proteins.
  • Immunogen: MOS maltose binding protein fusion protein
  • Isotype: IgG1
  • Myeloma used: Sp2/0-Ag14
  • Recommended controls: MBP fusion protein generated with the pmal plasmid (New England Biolabs) in bacterial lysate.

Target Details

  • Target: Maltose binding protein (MBP)
  • Molecular weight: 53 kDa
  • Tissue cell line specificity: MBP fusion protein generated with the pmal plasmid (New England Biolabs) in bacterial lysate.
  • Target background: MBP is a bacterial protein commonly used as a fusion protein.


  • Application: ChIP ; IHC ; IF ; IP ; WB


  • Format: Liquid
  • Concentration: 1 mg/ml
  • Unit size: 100 ug
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: -15° C to -25° C
  • Shipping conditions: Shipping at 4° C


  • Verhoeven et al. 2009. PLoS One. 4(8):e6739. PMID: 19707582.
  • Differential bacterial surface display of peptides by the transmembrane domain of OmpA.
  • Im et al. 2009. Dev Cell. 17(2):234-43. PMID: 19686684.
  • Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis.
  • Liu et al. 2006. Genome Res. 16(12):1517-28. PMID: 17053089.
  • Whole-genome comparison of Leu3 binding in vitro and in vivo reveals the importance of nucleosome occupancy in target site selection.
  • Liu et al. 2005. Genome Res. 15(3):421-7. PMID: 15710749.
  • DIP-chip: rapid and accurate determination of DNA-binding specificity.