Anti-Human IgG2 [Clone HP6014] – Purified No Carrier Protein

Anti-Human IgG2 [Clone HP6014] – Purified No Carrier Protein

Product No.: I-1224

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Clone
HP6014
Target
Human Immunoglobulin
IgG2
Formats AvailableView All
Product Type
Hybridoma Monoclonal Antibody
Alternate Names
Immunoglobulin heavy constant gamma 2
Isotype
Mouse IgG1 κ
Applications
ELISA
,
FA
,
ICC
,
IF

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Select Product Size
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Antibody Details

Product Details

Reactive Species
Human
Host Species
Mouse
Immunogen
Purified human immunoglobulin
Product Concentration
≥1.0 mg/ml
Purity
≥90% monomer by analytical SEC
Formulation
This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added.
State of Matter
Liquid
Product Preparation
Purified antibodies are manufactured in an animal free facility using only in vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
Storage and Handling
This antibody may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at ≤ -70°C. Avoid Repeated Freeze Thaw Cycles.
Regulatory Status
Research Use Only
Country of Origin
USA
Shipping
2 – 8° C Wet Ice
Additional Applications Reported In Literature ?
ELISA,
FA,
ICC,
IF
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.

Description

Description

Specificity
Clone HP6014 activity is directed against the Fd portion of human IgG2, in the Fab region.
Background
Humans produce five classes of immunoglobulins, IgM, IgD, IgA, IgE, and IgG1. IgG is the most abundant class1 and functions in the humoral immune response2. There are four subclasses of IgG, and they are numbered according to decreasing abundance as IgG1 through IgG4. The four subclasses are highly conserved and consist of four polypeptide chains: two identical heavy chains and two identical light chains1. While the general structure is very similar between IgG subclasses, differences in their constant regions in the hinge and upper CH2 domain as well as in glycosylation affect their binding to antigens (e.g. pathogenic proteins, polysaccharides, allergens), C1q and Fc receptors, leading to differences in functionality. As a result, each IgG subclass has a unique response skewed to specific antigens.

IgG2 responds to bacterial capsular polysaccharide antigens1. Relative to the other IgG subclasses, IgG2 has a short, rigid hinge. Several structural hinge isomers exist, differing in the hinge region’s inter-chain disulfide bonds. IgG2 is less efficient at triggering C1q complement activation than IgG1 and IgG3 due to a leucine-to-alanine substitution at residue 235. Additionally, the short hinge may shield the C1q binding site. However, IgG2 can efficiently activate the complement cascade in the presence of high densities of polysaccharides. IgG2 also has a relatively reduced affinity for a number of FcγR.

HP6014 was generated by immunizing a BALB/c mouse with purified human immunoglobulin3. Spleen cells were fused with Sp2/0-Ag14 myeloma cells.

Antigen Distribution
IgG2 is produced by B cells and is present in serum.
Ligand/Receptor
IgG-Fc receptors, C1q
NCBI Gene Bank ID
UniProt.org
Research Area
Adaptive Immunity
.
Infectious Disease
.
Immunoglobulins

References & Citations

1 Vidarsson G, Dekkers G, Rispens T. Front Immunol. 5:520. 2014.
2 Rispens T, Huijbers MG. Nat Rev Immunol. 23(11):763-778. 2023.
3 Reimer CB, Phillips DJ, Aloisio CH, et al. Hybridoma. 3(3):263-275. 1984.
4 Jefferis R, Reimer CB, Skvaril F, et al. Immunol Lett. 10(3-4):223-252. 1985.
Indirect Elisa Protocol
FA
ICC
IF

Certificate of Analysis

Formats Available

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Disclaimer AlertProducts are for research use only. Not for use in diagnostic or therapeutic procedures.