Rat IgG

SKU: orb2652744

Description

Rat IgG

Research Area

Protein Biochemistry

Images & Validation

• Tested Applications: SDS-PAGE, WB
• Application Notes:
  Rat IgG whole molecule has been tested by SDS-Page and western blot and is suitable for use as antigen or ligand in immunochemical reactions, as a control or standard in assays, for conjugation and most other immunological methods requiring highly purified immunoglobulins. Reconstitution Buffer: Restore with deionized water (or equivalent). Reconstitution Volume: 1.0 mL

Key Properties

• Source: Rat
• Biological Origin: Rat
• Isotype: IgG
• Purity: Rat IgG was prepared from normal serum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer stated above. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rat IgG and anti-Rat Serum.
• Conjugation: Unconjugated

Storage & Handling

• Storage: 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.
• Form/Appearance: Lyophilized
• Buffer/Preservatives: Preservative: 0.01% (w/v) Sodium Azide. Stabilizer: None; Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
• Concentration: 10.0 mg/mL
• Expiration Date: 6 months from date of receipt.
• Disclaimer: For research use only

Alternative Names

Rat Immunoglobulin G, Rat IgG whole molecule, Rat IgG purified protein

Elav Regulates Dscam1 Long 3' UTR Biogenesis. (E) RIP-qRT-PCR experiments demonstrate binding of Elav downstream of the Dscam1 proximal polyA site (left), and as a positive control, binding of Elav downstream of the Elav proximal polyA site (right). RIP was performed using rat and mouse anti-Elav antibodies from 12–16 h embryos. Primers were designed to detect a region in the CDS or a region immediately downstream of the proximal polyA site (EBS). Error bars represent SEM of four separate immunoprecipitation reactions on independently prepared nuclei. n = 4. p value reflects two-tailed paired Student's t test. Samples were incubated with a mixture of 1 µg rat and 1 µg mouse anti-Elav antibodies or a mixture of 1 µg rat and 1 µg mouse IgG.

SDS PAGE of Rat IgG Whole Molecule. Lane 1: Non-Reduced Rat IgG Whole Molecule. Lane 2: 5 µl Opal Prestained Marker. Lane 3: Reduced Rat IgG Whole Molecule. Load: 1 µg per lane. Predicted/Observed size: Non-Reduced at 160 kDa/Observed at 245 kDa; Reduced at 55, 25 kDa. Non-reduced IgG migrates slightly higher.

SDS-PAGE of Rat IgG F(c) Fragment Rhodamine Conjugated. Lane M: 3 µl Opal Prestained Marker. Lane 1: Reduced Rat IgG Whole Molecule (p/n orb2652744). Lane 2: Reduced Rat IgG F(c) Fragment Rhodamine Conjugated. Lane 3: Reduced Rat IgG Fab Fragment (p/n orb346340). Lane 4: Reduced Rat IgM Whole Molecule (p/n orb346341). Load: 1 µg of IgG, F(c), Fab; 1.5 µg of IgM. Predicted/Observed size: IgG at 55 and 25 kDa; F(c) at 25 kDa; Fab at 25 kDa; IgM at 78 and 25 kDa. Observed F(c) Fragment migrates slightly higher.

γIMC-Derived IL-6 Upregulates Mincle Expression. (A–G) C57BL/6 mice, Il6−/− mice, and Mincle−/− mice intraperitoneally infected for 48 h with NIH34 (1.0 × 107 colony-forming units/mouse) were sacrificed. Splenocytes were immediately negatively selected by magnetic separation, and CD11b+ CD11c− CD38+ IL-5Rα (T21)+ γIMC subsets were isolated by fluorescence-activated cell sorting. (A and C) Il6−/− γIMCs were treated for 12 h with or without 100 ng/mL IL-6 (A) or with 1 µg/ml IL-6 neutralizing mAb (clone MP5-20F3) or control rat IgG in combination with 90% culture supernatant from wild type γIMCs stimulated with NIH34 for 24 h at a multiplicity of infection of 30 (C). Cells were analyzed for Mincle expression by flow cytometry using anti-Mincle mAb and an isotype control, represented by the solid and dashed lines, respectively. (B and D) Data are mean ± SD (B, n = 5 mice for each experimental cell group; D, n = 4 mice for each experimental cell group) of the geometric mean fluorescent intensity due to surface expression of Mincle. ∗∗p < 0.01 by Student's t test. Data are representative of two independent experiments. (E) The numbers (%) in the plots represent the population of CD38+ IL-5Rα (T21)+ γIMC subsets. Cytospin preparations of each sorted cell subset were visualized with May-Grünwald-Giemsa staining. Scale bars, 20 µm. (F) Data are expressed as mean ± SD (n = 5 independent experiments) of CD38+ IL-5Rα (T21)+ γIMC subsets as% of total splenocytes. (G) RNA sequencing of wild type, Il6−/−, and Mincle−/− γIMCs (n = 3 independent experiments). Visualization of 18 cell types in two dimensions by principal component analysis of 20596 protein-coding genes expressed in at least one sample. Left: first versus second principal component (PC1 versus PC2). Right: second versus third principal component (PC2 versus PC3). Control rat IgG (p/n orb2652744).