A3963
Monoclonal Anti-Maltose Binding Protein−Alkaline Phosphatase antibody produced in mouse
clone MBP-17, purified immunoglobulin, buffered aqueous glycerol solution
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Monoclonal Anti-Maltose Binding Protein, Anti-MBP
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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.
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Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
含少量动物源组分生物产品
常规特殊物品
Certificates of Analysis (COA)
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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
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
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
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
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