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A3963

Sigma-Aldrich

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

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

Synonyme(s) :

Monoclonal Anti-Maltose Binding Protein, Anti-MBP

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Conjugué

alkaline phosphatase conjugate

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

MBP-17, monoclonal

Forme

buffered aqueous glycerol solution

Technique(s)

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

Isotype

IgG1

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

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.

Immunogène

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.

Forme physique

Solution in 0.05 M Tris buffer, containing 1 mM MgCl2, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide

Clause de non-responsabilité

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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Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H319,H334

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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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
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
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

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