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A4213

Sigma-Aldrich

Monoclonal Anti-Maltose Binding Protein−Peroxidase antibody produced in mouse

clone MBP-17, purified immunoglobulin, lyophilized powder

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Synonym(s):
Monoclonal Anti-Maltose Binding Protein, Anti-MBP
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

conjugate

peroxidase conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MBP-17, monoclonal

form

lyophilized powder

packaging

vial of 0.5 mL

technique(s)

western blot: 1:1,000 using purified, recombinant MBP

isotype

IgG1

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

Monoclonal Anti-Maltose Binding Protein (MBP) (mouse IgG1 isotype) is derived from the MBP-17 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a BALB/c mouse immunized with purified recombinant MBP fusion protein. Maltose Binding Protein (MBP) is a periplasmic protein, which is specific to bacteria. It has maltodextrin binding site and binds to linear and cyclic maltodextrins. The mature MBP is produced from the pre-protein containing 26 amino acids, as signal peptide.
The antibody recognizes native as well as denatured-reduced forms of purified MBP and MBP fusion proteins.

Immunogen

Purified, recombinant MBP fusion protein

Application

Endogenous intracellular levels of MBP in salmonella cells were determined by western blot analysis using a monoclonal anti-MBP antibody.
Monoclonal Anti-Maltose Binding Protein Peroxidase antibody produced in mouse has been used in:
  • immunoblotting
  • dot blot
  • enzyme-linked immunosorbent assay (ELISA)

Biochem/physiol Actions

Maltose Binding Protein (MBP) is often used to tag recombinant proteins to enhance the yield and facilitate the purification of the fusion product. Additionally, MBP tags can also improve the immunogenicity of the tagged protein. Thus, MBP can also be used as a carrier protein for vaccinations.
Maltose Binding Protein (MBP) mediates uptake of maltose. MBP is a substrate for chaperone secB. It has been reported that the addition of a 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.

Physical form

Lyophilized in 0.01 M sodium phosphate buffered saline containing 1% bovine serum albumin and 0.05% MIT.

Preparation Note

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

Reconstitution

The antibody conjugate should be reconstituted with 0.5 mL deionized water.

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.

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Skin Sens. 1

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

含少量动物源组分生物产品
常规特殊物品

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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Effect of signal peptide on the stability and folding kinetics of maltose binding protein.
Beena K, et al.
Biochemistry, 43(12), 3608-3619 (2004)
P Bellot et al.
Veterinary immunology and immunopathology, 152(1-2), 101-108 (2012-10-20)
Maltose binding protein (MBP) is often fused to a relevant protein to improve its yield and facilitate its purification, but MBP can also enhance the immunogenicity of the fused proteins. Recent data suggest that MBP may potentiate antigen-presenting functions in
The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.
Spurlino JC, et al.
The Journal of Biological Chemistry, 266(8), 5202-5219 (1991)

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