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Recombinant Human IgG1 Fc Avi-tag Protein, CF

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When Biotinylated Recombinant Human IgG1 Fc Avi-tag (Catalog # AVI110) is immobilized at 2 μg/mL (100 μL/well) onto a Streptavidin coated plate (Catalog # CP004), it binds to Human C1q with an ED50 of ...read more
2 μg/lane of Recombinant Human IgG1 Fc Avi-tag (Catalog # AVI110) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 30-42 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IgG1 Fc Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA.

When Biotinylated Recombinant Human IgG1 Fc Avi-tag (Catalog # AVI110) is immobilized at 2 µg/mL (100 µL/well) onto a Streptavidin coated plate (Catalog # CP004), it binds to Human C1q with an ED50 of 0.2-2.0 μg/mL.

Source
Human embryonic kidney cell, HEK293-derived human IgG1 protein
IEGRMD Human IgG1
(Pro100-Lys330)
Avi-tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Ile
Structure / Form
Disulfide-linked homodimer, Biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
28 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
30-42 kDa

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IgG1 Fc Avi-tag Protein, CF

  • IgG1
  • Igh-4
  • RGD1359539
  • VH7183

Background

Human Fc is the crystallizable fragment in the constant region of the human immunoglobulin heavy chain. Members of the immunoglobulin superfamily (IgSF) consist of two heavy (H) and two light (L) chains, with each component containing one variable (V) and one or more constant (C) domains (1, 2). Produced by B lymphocytes, Ig gamma (IgG) is the predominant isotype found in the body and has the longest half-life of all immunoglobulin isotypes (3). Four IgG subclasses (IgG1-4) were identified based on structural, antigenic and functional differences in the constant region of the heavy chain. The constant tail of the antibody is where proteins involved in immune responses typically bind, most notably the first component of the complement pathway, C1q, and Fc receptors found on immune cells such as B lymphocytes. Affinities for C1q and Fc gamma receptor (Fc gamma R) differ among the IgG subclasses. Fc receptors mediate the recruitment of immune cells to a site of infection (4). Engineered crystallizable fragment (Fc) regions of antibody which assume a unique and unprecedented asymmetric structure within the homodimeric Fc polypeptide, enable completely selective binding to the complement component C1q and activation of complement via the classical pathway without any concomitant engagement of the Fc gamma R (5).
  1. Williams, A.F. and A.N. Barclay (1988) Annu. Rev. Immunol. 6:381.
  2. Harpaz, Y. and C. Chothia (1994) J. Mol. Biol. 238:528.
  3. Schroeder, H.W. and L. Cavacini (2010) J. Allergy Clin. Immunol. 125:S41.
  4. Duncan, A.R. and G. Winter (1998) Nature 332:738.
  5. Lee, C.H. et al. (2017) Nat. Immunol. 18:889.

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