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AB99773

Mouse monoclonal [4E3] Anti-Human IgG1 hinge heavy chain (Alkaline Phosphatase)

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(2 Publications)

Suitable for Flow Cyt, ELISA. Cited in 2 publications.

View Alternative Names

Immunoglobulin heavy constant gamma 1, Ig gamma-1 chain C region, Ig gamma-1 chain C region EU, Ig gamma-1 chain C region KOL, Ig gamma-1 chain C region NIE, IGHG1

  • Unconjugated

    Mouse monoclonal [4E3] Anti-Human IgG1 hinge heavy chain

  • 519 FITC

    Mouse monoclonal [4E3] anti- Human IgG1 - hinge heavy chain (FITC)

  • HRP

    Mouse monoclonal [4E3] Anti-Human IgG1 hinge heavy chain (HRP)

  • Biotin

    Mouse monoclonal [4E3] Anti-Human IgG1 gamma chain (Biotin)

  • 578 PE

    Mouse monoclonal [4E3] Anti-Human IgG1 hinge heavy chain (PE)

Key facts

Host species

Mouse

Target species

Human

Target isotype

IgG1

Target specificity

Heavy chain hinge

Minimal cross-reactivity
Pre-adsorbed

No

Conjugation

Alkaline Phosphatase

Excitation/Emission
Applications

Flow Cyt, ELISA

applications

Clonality

Monoclonal

Clone number

4E3

Isotype

IgG1

Specificity

ab99773 reacts with the hinge region of the heavy chain of Human IgG1 as demonstrated by ELISA. May also react with IgG from other species.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Flow Cyt": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/500 - 1/1000", "notes":"<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 8 Preservative: 0.1% Sodium azide Constituents: 50% Glycerol (glycerin, glycerine), 0.605% Tris, 0.0095% Magnesium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Product protocols

Target data

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). Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells.
See full target information IGHG1

Publications (2)

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Experimental and therapeutic medicine 21:434 PubMed33747173

2021

Effect of TNF-α on the proliferation and osteogenesis of human periodontal mesenchymal stem cells.

Applications

Unspecified application

Species

Unspecified reactive species

Yiting Cao,Yiwei Wang,Chenlin Li,Qian Jiang,Laikuan Zhu

Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology 14:1464-9 PubMed15941957

2005

Intestinal helminthiasis in Colombian children promotes a Th2 response to Helicobacter pylori: possible implications for gastric carcinogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Mark T Whary,Nataliya Sundina,Luis E Bravo,Pelayo Correa,Francisco Quinones,Fanny Caro,James G Fox
View all publications

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