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P3351

Millipore

Protein L–Agarose from Peptostreptococcus magnus

recombinant, expressed in E. coli

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About This Item

Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56

Produit recombinant

expressed in E. coli

Niveau de qualité

200

Matrice

6% beaded agarose supplied as 50% slurry

Activation de la matrice

cyanogen bromide

Fixation de matrice

amino

Capacité

3-10 mg/mL binding capacity

Température de stockage

2-8°C

Catégories apparentées

Application

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.

Notes préparatoires

Prepared with recombinant Peptostreptococcus magnus Protein L.

Code de la classe de stockage

3 - Flammable liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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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
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
Annemarie Larkin et al.
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
Roberto de Giorgio et al.
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
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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Protocoles

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

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