Protein G Resin

Produktnummer ABIN1536254

Produktdetails

Target: Protein G

Reaktivität: Streptococcus

Applikation: Purification (Purif), Affinity Chromatography (AC)

Verwendungszweck: Protein G Resin is an affinity chromatography medium designed for easy, one-step purification of classes, subclasses and fragments of immunoglobulins from biological fluids and cell culture media. 

Produktmerkmale: The recombinant protein G ligand is coupled to 4% highly cross-linked agarose. The static binding capacity of Protein G Resin is greater than 20 mg sheep IgG/ml settled resin. The dynamic binding capacity will vary depending on several factors such as target antibody, flow rate etc.
Ligand: Recombinant Streptococcal Protein G lacking the albumin-binding produced in E. coli
- Number of IgG binding sites per ligand: 3
- MW of ligand: Approximately 22 kDa
- PI of ligand: 4.69
- Degree of substitution: Approximately 2 mg protein G/ml settled resin
- Static binding capacity: >20 mg sheep IgG/ml settled resin
- Matrix spherical: agarose, 4% cross-linked
- Average particle size: 90 μm (45-165 μm)

Bead Ligand: Protein G

Bead Matrix: Agarose beads

Bead Size: 90 µm

Anwendungsinformationen

Kommentare:

High temperature heating is not recommended. The agarose melts above 65°C.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: 1X PBS containing 20% ethanol

Handhabung: High temperature heating is not recommended. The agarose melts above 65°C.

Lagerung: 4 °C

Informationen zur Lagerung: Store regenerated Protein G Resin in Binding/Wash Buffer containing 20% ethanol at 2°C to 8°C. Do not freeze.

Haltbarkeit: 18 months

Referenzen

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Hakimi, Goto, Suganuma, Angeles, Kawai, Inoue, Kawazu: "Development of monoclonal antibodies against Plasmodium falciparum thioredoxin peroxidase 1 and its possible application for malaria diagnosis." in: Experimental parasitology, Vol. 154, pp. 62-6, (2015) (PubMed).

Ringel, Probst, Dammeyer, Buchmeier, Jänsch, Wissing, Tinnefeld, Mendel, Jockusch, Kruse: "Enzymatic characterization of recombinant nitrate reductase expressed and purified from Neurospora crassa." in: Fungal genetics and biology : FG & B, Vol. 80, pp. 10-8, (2015) (PubMed).

Tian, von Dahl, Liu, Friso, van Wijk, Klessig: "The combined use of photoaffinity labeling and surface plasmon resonance-based technology identifies multiple salicylic acid-binding proteins." in: The Plant journal : for cell and molecular biology, Vol. 72, Issue 6, pp. 1027-38, (2014) (PubMed).

Muth, Schütze, Hain, Yagita, Schild, Probst: "A CD40/CD40L feedback loop drives the breakdown of CD8(+) T-cell tolerance following depletion of suppressive CD4(+) T cells." in: European journal of immunology, Vol. 44, Issue 4, pp. 1099-107, (2014) (PubMed).

Armitage, OMeara, Harvie, Timms, Blumberg, Beagley: "Divergent outcomes following transcytosis of IgG targeting intracellular and extracellular chlamydial antigens." in: Immunology and cell biology, Vol. 92, Issue 5, pp. 417-26, (2014) (PubMed).

Kan, Adjobo-Hermans, Burroughs, Faibis, Malik, Tall, Smrcka: "M3 muscarinic receptor interaction with phospholipase C ?3 determines its signaling efficiency." in: The Journal of biological chemistry, Vol. 289, Issue 16, pp. 11206-18, (2014) (PubMed).

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Muth, Schütze, Schild, Probst: "Release of dendritic cells from cognate CD4+ T-cell recognition results in impaired peripheral tolerance and fatal cytotoxic T-cell mediated autoimmunity." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, Issue 23, pp. 9059-64, (2012) (PubMed).

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Antigendetails

Target: Protein G

Abstract: Protein G Produkte

Hintergrund: Protein G, a bacterial cell wall protein isolated from group G Streptococci, binds to mammalian IgGs mainly through Fc regions. Native protein G has 3 IgG binding domains and also sites for albumin and cell-surface binding. The latter have been eliminated from recombinant protein G to reduce nonspecific binding. Although protein G has very similar tertiary structures to protein A, their amino acid compositions differ significantly, resulting in different binding characteristics. Protein G can be used for purification of mammalian monoclonal and polyclonal IgGs that do not bind well to protein A. Protein G has greater affinity than protein A for most mammalian IgGs, especially for certain subclasses including human IgG3, mouse IgG1 and rat IgG2a. Unlike protein A, protein G does not bind to human IgM, IgD and IgA.
Broad IgG binding spectrum
Binding specificity complements of protein A
Agarose media
No specific albumin binding
Optimized homogeneous recombinant ligand
High capacity