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Key Documents

M1321

Sigma-Aldrich

Monoclonal Anti-Maltose Binding Protein antibody produced in mouse

clone MBP-17, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Anti-MBP

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

MBP-17, monoclonal

Forme

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

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.

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
Wubei Zong et al.
The New phytologist, 229(3), 1635-1649 (2020-10-23)
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)
Ilona Turek et al.
The Journal of biological chemistry, 293(42), 16324-16336 (2018-09-07)
Ubiquitination is a prevalent post-translational modification involved in all aspects of cell physiology. It is mediated by an enzymatic cascade and the E2 ubiquitin-conjugating enzymes (UBCs) lie at its heart. Even though E3 ubiquitin ligases determine the specificity of the

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