MOUSE IgG F(c) fragment, Mouse Fc, Immunoglobulin Fc
Mouse IgG F(c) Antibody
Concentration:
1.1 mg/mL
Buffer:
Preservative: 0.01% (w/v) Sodium Azide, Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Source:
Mouse
Purity:
MOUSE IgG F(c) fragment was prepared from normal serum by a multi-step process which includes delipidation, salt fractionation, ion exchange chromatography and papain digestion followed by chromatographic separation and extensive dialysis against the buffer stated above. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Mouse Serum, anti-Mouse IgG and anti-Mouse IgG F(c). No reaction was observed against anti-Mouse IgG F(ab)2 or anti-Papain.
Form:
Liquid (sterile filtered)
Application Dilute:
ELISA: User Optimized, IHC: User Optimized, WB: User Optimized
Application Notes:
Biological Origin: Mouse. Application Notes: Mouse IgG F(c) Fragment has been tested by SDS-Page and can be utilized as a control or standard reagent in Western Blotting and ELISA experiments
Ability of ProteoChip to bind the antibody F(c) region. (b) Scanning images of protein microarray: competition between FITC-labeled F(c) [p/n orb346285] and unlabeled Fab fragments [p/n orb346282] (upper picture), and FITC-labeled F(c) [p/n orb346285] and unlabeled F(c) fragments [orb346280] (lower picture). (c) Scanning images were analyzed using QuantumArray software, and fluorescence intensities of each spot were plotted versus competitor concentration. Competition between FITC-labeled F(c) and unlabeled Fab fragment, and FITC-labeled F(c) and unlabeled F(c) fragments, are shown by the solid line and broken line, respectively.
SDS-PAGE of Mouse IgG Whole Molecule Rhodamine Conjugated (p/n orb346272). MW: 5 µl Opal Prestained Marker. Lane 1: Reduced Mouse IgG Whole Molecule Rhodamine Conjugated (p/n orb346272). Lane 2: Reduced Mouse F(c) Fragment (p/n orb346280). Lane 3: Reduced Mouse F(ab) Fragment (p/n orb346282). Lane 4: Mouse IgM Kappa Myeloma Protein. Load: 1 µg per lane. Predicted/Observed size: IgG at 50 and 25 kDa, F(c) at 25 kDa, F(ab) at 25 kDa, IgM K at 70 and 23 kDa. Observed F(c) Fragment migrates slightly higher.
Strong responses to polyclonal anti-HA antiserum are readily observable on an AIR hemagglutinin microarray. (a) 1% BSA control. (b) Anti-H7 polyclonal antiserum (A/Netherlands/219/2003, H7N7), 1:80 dilution (1.3%) in 1% BSA. Spots showing substantially increased brightness indicate binding to immobilized H7. In both cases, antigens were arrayed in square patterns as indicated by the yellow boxes in (a), a mouse IgG Fc domain (p/n orb346280) was included as negative control (red boxes). Slight differences in spot intensity in the control (a) are due to differences in deposition efficiency for different antigens or controls. Specific antigens used in these experiments are indicated in Table 2. Goat anti-fluorescein, (p/n orb345272) used as an internal negative control.
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