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P3351
Protein-L-Agarose aus Peptostreptococcus magnus
recombinant, expressed in E. coli
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5 ML
1.120,00 €
1.120,00 €
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5 ML
1.120,00 €
About This Item
UNSPSC-Code:
41106500
NACRES:
NA.56
1.120,00 €
Auf LagerDetails
Empfohlene Produkte
Rekombinant
expressed in E. coli
Qualitätsniveau
Matrix
6% beaded agarose supplied as 50% slurry
Matrixaktivierung
cyanogen bromide
Matrixanbindung
amino
Kapazität
3-10 mg/mL binding capacity
Lagertemp.
2-8°C
Anwendung
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.
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.
Angaben zur Herstellung
Hergestellt aus rekombinantem Peptostreptococcus magnus Protein L.
Lagerklassenschlüssel
3 - Flammable liquids
WGK
WGK 2
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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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
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
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
Protokolle
Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.
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