Anti-Human IgG (H&L) (Peroxidase Conjugated) Secondary Antibody
Chicken Polyclonal, Peroxidase (Horseradish)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Description | Anti-HUMAN IgG (H&L) (CHICKEN) Antibody Peroxidase Conjugated |
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Host | Chicken |
Conjugate | Peroxidase (Horseradish) |
Target Species | Human |
Clonality | Polyclonal |
Application
| WB, E, IC |
Application Note | ELISA 1:30,000 Western Blot 1:1,000-1:5,000 Immunochemistry 1:500-1:2,500 |
Physical State | Lyophilized |
Host Isotype | IgG |
Target Isotype | IgG (H&L) |
Buffer | 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 |
Immunogen | Human IgG whole molecule |
Reconstitution Volume | 1.0 mL |
Reconstitution Buffer | Restore with deionized water (or equivalent) |
Stabilizer | 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free |
Preservative | 0.01% (w/v) Gentamicin Sulfate. Do NOT add Sodium Azide! |
Shipping Condition | Ambient |
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Purity | Human IgG (H&L) Antibody Peroxidase Conjugate was prepared from monospecific antiserum by immunoaffinity chromatography using Human IgG coupled to agarose. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Peroxidase, anti-Chicken Serum, Human IgG and Human Serum. |
Storage Condition | Store vial at 4° C prior to restoration. 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. This product 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
Anti-Human IgG (H&L) Antibody Peroxidase Conjugated antibody detects human IgG. IgG antibodies are large molecules of about 150 kDa composed of four peptide chains. Each IgG contains two identical ? heavy chains of about 51 kDa and two identical light chains of about 26 kDa, thus a tetrameric quaternary structure. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves, which together form the Y-like shape. Each end of the fork contains an identical antigen binding site. The Fc regions of IgGs bear a highly conserved N-glycosylation site.
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