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Immunology Immunoglobulins Heavy Chain IgG

Anti-IgG Affibody® Molecule (Biotin) (ab31901)

Price and availability

388 646 ₸

Availability

Order now and get it on Wednesday March 03, 2021

Anti-IgG Affibody® Molecule (Biotin) (ab31901)
  • ChIP - Anti-Histone H3 antibody - Nuclear Loading Control and ChIP Grade (ab1791)
  • ChIP - Anti-Histone H3 antibody - Nuclear Loading Control and ChIP Grade (ab1791)
  • ChIP - Anti-Histone H3 antibody - Nuclear Loading Control and ChIP Grade (ab1791)

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Overview

  • Product name

    Anti-IgG Affibody® Molecule (Biotin)
    See all IgG affibody® molecule
  • Conjugation

    Biotin
  • Species reactivity

    Reacts with: Mouse, Rabbit, Human, Rhesus monkey
  • Immunogen

    -

  • General notes

    ab31901 is a recombinant protein produced in E. coli.

    What are Affibody Molecules?
    Affibody® affinity ligands are small, simple proteins composed of a three-helix bundle based on the scaffold of one of the IgG-binding domains of Protein A. Protein A is a surface protein from the bacterium Staphylococcus aureus. This scaffold has excellent features as an affinity ligand and can be designed to bind with high affinity to any given target protein. The domain consists of 58 amino acids, 13 of which are randomized to generate Affibody® libraries with a large number of ligand variants. Thus, the libraries consist of a multitude of protein ligands with an identical backbone and variable surface- binding properties. The current Affibody® libraries contains billions of variants. In function, Affibody® molecules mimic antibodies, nature’s own binders to an infinite number of antigens. Compared to antibodies, the most striking dissimilarity of Affibody® molecules is the small size. Affibody® molecules have a molecular weight of 14 kDa, compared to the molecular weight of antibodies, which is 150 kDa. In spite of its small size, the binding site of Affibody® molecules is similar to that of an antibody. The advantages of Affibody® molecules over antibodies are · their small size · the simple structure of the molecules · its robust physical properties · its ability to fold correctly intracellularly · the fast and cost-efficient production in bacteria · the possibility to produce Affibody® molecules through chemical synthesis · the possibility to couple Affibody® molecules in multimeric constructs

Properties

  • Form

    Liquid
  • Storage instructions

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term.
  • Storage buffer

    pH: 7.20
    Preservative: 0.02% Sodium azide
    Constituents: 0.328% Sodium phosphate, 0.87% Sodium chloride
  • Concentration information loading...
  • Purification notes

    ab31901 is >98% pure, as determined by RP-HPLC analysis.
  • Affibody® molecule notes

    What are Affibody Molecules?
    Affibody® affinity ligands are small, simple proteins composed of a three-helix bundle based on the scaffold of one of the IgG-binding domains of Protein A. Protein A is a surface protein from the bacterium Staphylococcus aureus. This scaffold has excellent features as an affinity ligand and can be designed to bind with high affinity to any given target protein. The domain consists of 58 amino acids, 13 of which are randomized to generate Affibody® libraries with a large number of ligand variants. Thus, the libraries consist of a multitude of protein ligands with an identical backbone and variable surface- binding properties. The current Affibody® libraries contains billions of variants. In function, Affibody® molecules mimic antibodies, nature’s own binders to an infinite number of antigens. Compared to antibodies, the most striking dissimilarity of Affibody® molecules is the small size. Affibody® molecules have a molecular weight of 14 kDa, compared to the molecular weight of antibodies, which is 150 kDa. In spite of its small size, the binding site of Affibody® molecules is similar to that of an antibody. The advantages of Affibody® molecules over antibodies are · their small size · the simple structure of the molecules · its robust physical properties · its ability to fold correctly intracellularly · the fast and cost-efficient production in bacteria · the possibility to produce Affibody® molecules through chemical synthesis · the possibility to couple Affibody® molecules in multimeric constructs
  • Research areas

    • Immunology
    • Immunoglobulins
    • Heavy Chain
    • IgG
  • Cellular localization

    Secreted
  • Alternative names

    • Ig gamma 1 chain C region
    • Ig gamma 2 chain C region
    • Ig gamma 3 chain C region
    • Ig gamma 4 chain C region
    • IgG
    • IGHG1
    • IGHG2
    • IGHG3
    • IGHG4
    • Immunoglobin heavy constant gamma 1
    • Immunoglobulin G
    see all
  • Database links

    • Entrez Gene: 3500 Human
    • Entrez Gene: 3501 Human
    • Entrez Gene: 3502 Human
    • Entrez Gene: 3503 Human
    • SwissProt: P01857 Human
    • SwissProt: P01859 Human
    • SwissProt: P01860 Human
    • SwissProt: P01861 Human
    • Unigene: 510635 Human
    see all

Images

  • Anti-IgG Affibody® Molecule (Biotin) (ab31901)
    Anti-IgG Affibody® Molecule (Biotin) (ab31901)
    Overlay chromatograms of repeated affinity removal of IgG from serum are shown. The chromatograms represent run number 1, 50 and 300 after consecutive injections of 700 ul of five times diluted human serum on 0.37 ml SulfoLink® Coupling Gel with immobilized Anti-IgG Affibody® molecule. The peak area of eluted fraction after each run is plotted in the image below. The identical chromatograms and consistent peak areas of eluted fractions prove that the depletion procedure can be reproducibly repeated at least 300 times without loss of binding capacity. SDS-PAGE analysis of flow-through fractions and eluted fractions shown in the third image demonstrate that the high specificity of the Anti-IgG Affibody® molecule is maintained through all the 300 consecutive injections. The capacity of this coupling gel allows for depletion of IgG from 1900 ul of five times diluted human serum per ml gel, corresponding to 380 ul of undiluted human serum per ml gel.

    Overlay chromatograms of repeated affinity removal of IgG from serum are shown. The chromatograms represent run number 1, 50 and 300 after consecutive injections of 700 ul of five times diluted human serum on 0.37 ml SulfoLink® Coupling Gel with immobilized Anti-IgG Affibody® molecule. The peak area of eluted fraction after each run is plotted in the image below. The identical chromatograms and consistent peak areas of eluted fractions prove that the depletion procedure can be reproducibly repeated at least 300 times without loss of binding capacity. SDS-PAGE analysis of flow-through fractions and eluted fractions shown in the third image demonstrate that the high specificity of the Anti-IgG Affibody® molecule is maintained through all the 300 consecutive injections. The capacity of this coupling gel allows for depletion of IgG from 1900 ul of five times diluted human serum per ml gel, corresponding to 380 ul of undiluted human serum per ml gel.
  • Anti-IgG Affibody® Molecule (Biotin) (ab31901)
    Anti-IgG Affibody® Molecule (Biotin) (ab31901)
    Peak area of the eluted fraction after each run of affinity removal. The consistent peak area prove that the depletion procedure can be reproducibly repeated at least 300 times without loss of binding capacity.

    Peak area of the eluted fraction after each run of affinity removal. The consistent peak area prove that the depletion procedure can be reproducibly repeated at least 300 times without loss of binding capacity.
  • Anti-IgG Affibody® Molecule (Biotin) (ab31901)
    Anti-IgG Affibody® Molecule (Biotin) (ab31901)

    SDS-PAGE analysis of flow-through fractions (FT) and eluted fractions after repeated affinity removal of IgG from human serum.

    Lane 1: Untreated 5x diluted serum sample;

    Lane 2: FT run 1;

    Lane 3: FT run 75;

    Lane 4: FT run 150;

    Lane 5: FT run 225;

    Lane 6: FT run 300;

    Lane 7: eluate run 1;

    Lane 8: eluate run 300;

    Lane 9: IgG standard.



    SDS-PAGE analysis of flow-through fractions (FT) and eluted fractions after repeated affinity removal of IgG from human serum.

    Lane 1: Untreated 5x diluted serum sample;

    Lane 2: FT run 1;

    Lane 3: FT run 75;

    Lane 4: FT run 150;

    Lane 5: FT run 225;

    Lane 6: FT run 300;

    Lane 7: eluate run 1;

    Lane 8: eluate run 300;

    Lane 9: IgG standard.

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

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