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P3351

Millipore

Protein L–Agarose from Peptostreptococcus magnus

recombinant, expressed in E. coli

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About This Item

Codice UNSPSC:
41106500
NACRES:
NA.56

Ricombinante

expressed in E. coli

Livello qualitativo

200

Matrice

6% beaded agarose supplied as 50% slurry

Attivazione matrice

cyanogen bromide

Gruppi immobilizzati alla matrice

amino

Capacità

3-10 mg/mL binding capacity

Temperatura di conservazione

2-8°C

Categorie correlate

Applicazioni

Protein L-agarose is used in affinity chromatography, protein chromatography, antibody purification and characterization, immunoaffinity matrices, phosphorylation analysis, and protein A, G and L resins. Protein L-agarose has been used to provide evidence that antineuronal antibodies may contribute to neuronal dysfunction observed in a subset of patients with neurogenic chronic intestinal pseudoobstruction. Protein L agarose has also been used to evaluate a diabody to improve protection againse a potent scorpion neurotoxin.
Protein L from Peptostreptococcus magnus binds immunoglobulins (Ig) primarily through kappa light chain interactions without interfering with the antigen binding site. Recombinant Protein L contains four Ig-binding domains.

Nota sulla preparazione

Prepared with recombinant Peptostreptococcus magnus Protein L.

Codice della classe di stoccaggio

3 - Flammable liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

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Marion Avril et al.
Microbes and infection, 8(14-15), 2863-2871 (2006-11-11)
Pregnancy-associated malaria (PAM) is associated with the massive sequestration of erythrocytes infected with CSA-binding parasites in the placenta. Natural protective immunity against PAM is acquired during the course of pregnancies, with the development of anti-PfEMP1 antibodies recognizing placental infected erythrocytes
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Journal of immunological methods, 303(1-2), 53-65 (2005-07-26)
Monoclonal antibodies (MAbs) provide a powerful tool for the identification of novel tumour associated antigens. In an attempt to identify such an antigen, MAbs were generated by immunization with paraffin wax-embedded formalin-fixed invasive ductal breast tumour tissue from a patient
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Gastroenterology, 135(2), 601-609 (2008-06-28)
Activation of autoimmune pathways has been implicated as a contributing mechanism to the pathophysiology in some patients with chronic intestinal pseudoobstruction (CIP). In this study we tested the hypothesis that sera from a subpopulation of patients with CIP contain autoantibodies
Isa Santos Duarte et al.
Artificial organs, 29(4), 313-323 (2005-03-25)
This work investigated the adsorption of autoantibodies such as anti-SS-A/Ro, anti-SS-B/La, anti-Sm, and anti-dsDNA on protein L-agarose gel. In order to determine better conditions for IgG adsorption on this matrix, some buffer systems were tested. Adsorption data were analyzed using
N Aubrey et al.
Cellular and molecular life sciences : CMLS, 60(3), 617-628 (2003-05-10)
Diabodies are recombinant, dimeric, antibody-based molecules composed of two non-covalently associated single-chain antibody fragments that bind to an antigen in a divalent manner. In an attempt to develop more effective therapeutic molecules against scorpion venoms, we designed a diabody derived
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Protocolli

Immunoprecipitation Procedure

To determine the molecular weights of protein antigens, to study protein/protein interactions, to determine specific enzymatic activity, to monitor protein post-translational modifications and to determine the presence and quantity of proteins.

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