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M1321

Sigma-Aldrich

Monoclonal Anti-Maltose Binding Protein antibody produced in mouse

clone MBP-17, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-MBP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MBP-17, monoclonal

form

buffered aqueous solution

concentration

~2 mg/mL

technique(s)

dot blot: suitable
indirect ELISA: suitable
western blot: 0.05-0.1 μg/mL using purified recombinant MBP.

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

Monoclonal Anti-Maltose Binding Protein (MBP) (mouse IgG1 isotype) is derived from the hybridoma MBP-17 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a purified recombinant MBP fusion protein.
The antibody recognizes native as well as denatured-reduced forms of purified MBP and MBP fusion proteins.

Immunogen

Purified, recombinant MBP fusion protein.

Application

Monoclonal Anti-Maltose Binding Protein antibody produced in mouse has been used in:
  • immunoblotting
  • dot blot
  • luminometric immunoassay
  • enzyme linked immuno sorbent assay (ELISA)

Monoclonal Anti-Maltose Binding Protein antibody produced in mouse was used in agarose binding assay for the detection of activation-induced cytidine deaminase-MBP complex.

Biochem/physiol Actions

Maltose binding protein (MBP) is a periplasmic binding protein that is important for nutrient uptake and chemotaxis of Escherichia coli.
Maltose binding protein (MBP) tag creates a stable fusion product, that does not appear to interfere with the bioactivity of the protein or with the biodistribution of the MBP tagged product. It facilitates the detection, isolation and purification of the proteins.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Andrew C Miklos et al.
PloS one, 8(10), e74969-e74969 (2013-10-15)
Cellular signaling involves a cascade of recognition events occurring in a complex environment with high concentrations of proteins, polysaccharides, and other macromolecules. The influence of macromolecular crowders on protein binding affinity through hard-core repulsion is well studied, and possible contributions
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Rice (Oryza sativa) is a short-day (SD) plant originally having strong photoperiod sensitivity (PS), with SDs promoting and long days (LDs) suppressing flowering. Although the evolution of PS in rice has been extensively studied, there are few studies that combine
Steffen Frey et al.
PloS one, 10(4), e0125099-e0125099 (2015-04-30)
During autophagy, members of the ubiquitin-like Atg8 protein family get conjugated to phosphatidylethanolamine and act as protein-recruiting scaffolds on the autophagosomal membrane. The Atg4 protease produces mature Atg8 from C-terminally extended precursors and deconjugates lipid-bound Atg8. We now found that
A rapid solubility-optimized screening procedure for recombinant subtilisins in E. coli
Bjerga GEK, et al.
Journal of Biotechnology, 222, 38-46 (2016)
Arturo Vera Rodriguez et al.
The Journal of cell biology, 218(6), 2006-2020 (2019-04-27)
Cleavage of affinity tags by specific proteases can be exploited for highly selective affinity chromatography. The SUMO/SENP1 system is the most efficient for such application but fails in eukaryotic expression because it cross-reacts with endogenous proteases. Using a novel selection

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