Recombinant Human IgG1 Fc Avi-tag Protein, CF Summary
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.
|IEGRMD||Human IgG1 |
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
2 μg/lane of Recombinant Human IgG1Fc 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 kDa and 60-80 kDa, respectively.
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).
- Williams, A.F. and A.N. Barclay (1988) Annu. Rev. Immunol. 6:381.
- Harpaz, Y. and C. Chothia (1994) J. Mol. Biol. 238:528.
- Schroeder, H.W. and L. Cavacini (2010) J. Allergy Clin. Immunol. 125:S41.
- Duncan, A.R. and G. Winter (1998) Nature 332:738.
- Lee, C.H. et al. (2017) Nat. Immunol. 18:889.
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