Rat IgG F(c)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Description | RAT IgG F(c) fragment |
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Conjugate | Unconjugated |
Physical State | Liquid (sterile filtered) |
Host Isotype | IgG F(c) |
Buffer | 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 |
Species of Origin | Rat |
Preservative | 0.01% (w/v) Sodium Azide |
Shipping Condition | Wet Ice |
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Purity | Rat 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. Rat IgG F(c) fragment was assayed by immunoelectrophoresis resulted in a single precipitin arc against anti-Rat Serum, anti-Rat IgG and anti-Rat IgG F(c). No reaction was observed against anti-Rat IgG F(ab’)2 or anti-Papain. |
Storage Condition | Store vial at 4° C prior to restoration. Restore with 1.0 mL of deionized water (or equivalent). For extended storage aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. Rat IgG Fc fragment is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use. |
Precautions Note | This product is for research use only and is not intended for therapeutic or diagnostic applications. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsinization for phagocytosis. The F(c) fragment binds with very high affinity to the Fc receptor proteins on phagocytic leukocytes. When digested from the whole antibody molecule, the F(c) fragment no longer posses the epitope recognition site.
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