Skip to Content
Merck
All Photos(1)

Key Documents

More Documents

A3963

Sigma-Aldrich

Monoclonal Anti-Maltose Binding Protein−Alkaline Phosphatase antibody produced in mouse

clone MBP-17, purified immunoglobulin, buffered aqueous glycerol solution

Synonym(s):

Monoclonal Anti-Maltose Binding Protein, Anti-MBP

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

conjugate

alkaline phosphatase conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MBP-17, monoclonal

form

buffered aqueous glycerol solution

technique(s)

western blot: 1:400 using using purified, recombinant MBP

isotype

IgG1

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

General description

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.
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-Alkaline Phosphatase antibody is suitable for use in ELISA.

Physical form

Solution in 0.05 M Tris buffer, containing 1 mM MgCl2, 1% bovine serum albumin, 50% glycerol and 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.

Not finding the right product?  

Try our Product Selector Tool.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H319 - H334

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

R R Beerli et al.
The Journal of biological chemistry, 275(42), 32617-32627 (2000-08-05)
Ligand-dependent transcriptional regulators were generated by fusion of designed Cys(2)-His(2) zinc finger proteins and steroid hormone receptor ligand binding domains. To produce novel DNA binding domains, three-finger proteins binding specific 9-base pair sequences were constructed from modular building blocks. Fusion
Jingtong Hou et al.
Toxins, 11(3) (2019-03-17)
A novel Bacillus thuringiensis Cry protein, Cry8Hb, active against Diabrotica virgifera virgifera (Western corn rootworm, WCRW) was discovered. Unexpectedly, the anti-rootworm activity of the Cry8Hb toxin was enhanced significantly by fusing Escherichia coli maltose binding protein (MBP) to this Cry
D J Segal et al.
Proceedings of the National Academy of Sciences of the United States of America, 96(6), 2758-2763 (1999-03-17)
We have taken a comprehensive approach to the generation of novel DNA binding zinc finger domains of defined specificity. Herein we describe the generation and characterization of a family of zinc finger domains developed for the recognition of each of
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service