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Antibodies

Human IgG whole molecule

Product Sizes
1 g
£ POA
009-0102-1000-1G
About this Product
SKU:
009-0102-1000
Additional Names:
Human IgG whole molecule, Human Immunoglobulin G
Application:
Bioactivity, ELISA, SDS-PAGE, Western Blot
Buffer:
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride
CE/IVD:
RUO
Concentration:
20 mg/ml
Extra Details:
Human IgG purified protein (Immunoglobulin G) are antibody molecules. Human IgG is composed of four peptide chains - two heavy chains gamma and two light chains. Human IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. Human IgG typically constitutes 75% of serum immunoglobulins. Human IgG molecules are synthesized and secreted by plasma B cells.
Formulation:
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Isotype:
IgG
Physical State:
Liquid
Shipping Conditions:
Dry Ice
Specificity:
This product 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-Human IgG and anti-Human Serum.
Storage Conditions:
Please refer to datasheet
Supplier:
Rockland Inc
Type:
Antibody: Isotype Controls
Sensor response to biomolecule functionalization and biomolecule-mediated particle detection. Resonance wavelength shifts were determined for PhC geometries in which the large-defect structure was centered 4 or 5 rows from the W1 waveguide after sequentially exposing the sensors to silane+GA, IgG molecules, and anti-IgG-coupled latex microspheres. The cover medium was either PBS, or PBS with 0.1% Tween-20 (PBS-T), as indicated in the legend. Error bars were calculated as the root-sum-of-squares of the standard deviations of the mean for baseline and experimental measurements. Mean resonance wavelengths and standard deviations were calculated from 5 replicate spectrum scans for all steps except for the particle/PBS-T step, in which only 3 scans each were collected for each PhC to minimize the opportunity for analyte dissociation. Fig 4. PMID: 28357424.
Alanine scanning mutagenesis identifies a single highly conserved juxtamembrane motif, MKKK, in the syndecan-1 cytoplasmic tail as essential for efficient endocytosis after clustering. B and C, raft localization and internalization triggered by clustering. The ligand for FcR-Synd1, 125I-labeled nonimmune human IgG, was bound at 4 °C to the surface of the McArdle cell lines described in A. Unbound material was washed away, and then the cells were incubated for 1 h at 37 °C in the absence or presence of our clustering agent (goat F(ab')2 against human IgG Fab). Raft localization was assessed by cold Triton insolubility and internalization by resistance to an acid wash that releases surface-bound IgG. Displayed are clustering-dependent raft localization (B) and internalization of ligand (C), normalized to control values from cells expressing the unmutated chimera (mean +/- S.E., n = 3). Non-normalized control values were 433.91 +/- 26.24 ng/mg that moved into rafts and 416.38 +/- 14.15 ng/mg that became internalized (total cell-associated ligand was 850.29 +/- 18.2 ng/mg). The horizontal dotted lines represent the mean values from UM FcR-Synd1-expressing cells. B, p > 0.5 by ANOVA. C, *, p < 0.01 by ANOVA; **, p < 0.01 compared with the UM value by the Dunnett test. The data are representative of a total of three independent catabolism experiments. Fig 1. PMID: 23525115.
Antibody distribution analysis on BXPC3 tumor sections 48 h after injection of hIgG or MAb159. Scale bar = 100 um. DAPI 5 4'-6-diamidino-2-phenylindole. Figure 6. PMID: 25908833.
Representative optical microscopy images of the Si/SiO2 chip incubated with 1:100 dilution of human IgG-modified fluorescent latex particle solution along the different steps of surface functionalization. (a) Piranha cleaned chip surface, (b) silane (APDMES) and glutaraldehyde modified surface, (c) silane and glutaralehyde modified chip subsequently blocked with BSA, and (d) silane/GA modified chip functionalized with goat anti-human IgG. All images are at the same exposure. Figure S3. PMID: 28357424.
Dose dependent inhibition curves generated with six different FcG GammaR assays. Four different set of samples were tested to show the specificity and subclass specific binding. Analytes tested are (1) human IgG subclasses IgG1, IgG2, IgG3, IgG4; (2) human IgG; (3) Fc, Fab, and F(ab)2 domains; and (4) human serum albumin (HSA). Data represent the mean +/- standard error of triplicate experiments. IC50 (nM) values calculated from the inhibition curves are shown in the Table. IC50 values are in nM. *For FcG GammaRIIb IC50 values are intended only for qualitative purposes as mentioned in the text. n.d. not determined. Figure 3. PMID: 35842448.
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