Immunohistochemistry (IHC) : Human tonsil stained with anti-IgG4 antibody using peroxidase-conjugate and DAB chromogen. Note the cytoplasmic staining of plasma cells.

rabbit anti-IgG4 monoclonal antibody (ZR299) 6225

$160.00 – $528.00

Antibody summary

Rabbit monoclonal to IgG4
Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
Reacts with: Human
Isotype:IgG
Control: Tonsil
Visualization: Cytoplasmic
0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted

SKU: 6225parent Category: antibody Tags: anatomy, Hematopathology, IgG4

Weight	1 lbs
Dimensions	9 × 5 × 2 in
host	mouse
isotype	IgG
clonality	monoclonal
concentration	concentrate, predilute
applications	IHC
reactivity	human
available size	0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted

rabbit anti-IgG4 monoclonal antibody ZR299 6225

antibody
Database link: human P01861
Tested applications IHC
Recommended dilutions Concentrated 1:100-200
Applicaiton Notes Positive control: Tonsil
Immunogen Recombinant full-length human IGHG4 protein
Size and concentration 7 mL prediluted or 0.1, 0.5, 1.0 mL and concentrated
Form liquid
Storage Instructions 2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Purity affinity purified
Clonality monoclonal
Isotype IgG
Compatible secondaries goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863 goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371 goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715 goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control Rabbit polyclonal - Isotype Control

target relevance
Protein names Immunoglobulin heavy constant gamma 4 (Ig gamma-4 chain C region)
Gene names IGHG4,IGHG4
Mass 9606Da
Function Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
Subellular location [Isoform 1]: Secreted .; [Isoform 2]: Cell membrane ; Single-pass membrane protein .
Structure Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.
Post-translational modification Glycosylation on Asn-177 is required for interaction with Fc receptors and ability to activate the complement pathway.; (Microbial infection) Deglycosylation on Asn-177 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway.
Target Relevance information above includes information from UniProt accession: P01861
The UniProt Consortium

Data

Human tonsil stained with anti-IgG4 antibody using peroxidase-conjugate and DAB chromogen. Note the cytoplasmic staining of plasma cells.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.