HEK-293 Cells Immunoglobulin G4 (IgG4) Isotype Control

Details for Product No. ABIN2181283, Supplier: Log in to see
  • immunoglobulin heavy constant gamma 4 (G4m marker)
  • IGHG4
HEK-293 Cells
Biological Activity
Isotype Control (IsoC)
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Supplier Product No.
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Isotype IgG4
Characteristics This protein carries no "tag". The protein has a calculated MW of 25.8 kDa. As a result of glycosylation, the protein migrates as 33-35 kDa under reducing (R) condition, and 50-55 kDa under non-reducing (NR) condition (SDS-PAGE).
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Alternative Name IgG4
Background Immunoglobulin G4 (IgG4) is a member of many immunoglobulin G developed and secreted by effective B cells. In wake of cutting by pepsin, IgG is divided into two F(ab)s with one antigen binding site and a high conserved Fc segment. The Fc segment bears a highly conserved N-glycosylation site. Ig gamma-4 chain Fc region contains two constant regions of IgG4 H chain (CH2, CH3).
Molecular Weight 25.8 kDa
UniProt P01861
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 100 mM Glycine, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for HEK-293 Cells Immunoglobulin G4 (IgG4) isotype control (ABIN2181283) Human IgG4 Fc, Tag Free on SDS-PAGE under reducing (R) and no-reducing (NR) condition...
Background publications Chen, Jiang, Sun, Han, Wang, Ye, Wang, Zou: "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." in: Journal of proteome research, Vol. 8, Issue 2, pp. 651-61, 2009 (PubMed).

Kristiansen, Bunkenborg, Gronborg, Molina, Thuluvath, Argani, Goggins, Maitra, Pandey: "A proteomic analysis of human bile." in: Molecular & cellular proteomics : MCP, Vol. 3, Issue 7, pp. 715-28, 2004 (PubMed).

Frangione, Milstein, Pink: "Structural studies of immunoglobulin G." in: Nature, Vol. 221, Issue 5176, pp. 145-8, 1970 (PubMed).

ODonnell, Frangione, Porter: "The disulphide bonds of the heavy chain of rabbit immunoglobulin G." in: The Biochemical journal, Vol. 116, Issue 2, pp. 261-8, 1970 (PubMed).