Mouse Monoclonal JCHAIN Antibody

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     Black line: Control Antigen (100 ng); Purple line: Antigen(10ng); Blue line: Antigen (50 ng); Red line: Antigen (100 ng);    

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     Immunofluorescence analysis of Hela cells using PDGFRA mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor- 555 phalloidin. Secondary antibody from Fisher (Cat#: 35503)    

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     Immunofluorescence analysis of NIH/3T3 cells using PDGFRA mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor- 555 phalloidin.    

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     Immunofluorescence analysis of COS-7 cells using PDGFRA mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor- 555 phalloidin.    

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     Flow cytometric analysis of Hela cells using PDGFRA mouse mAb (green) and negative control (red).    

The J chain (joining chain) is a small polypeptide critical for the polymerization and secretion of multimeric immunoglobulins, particularly IgA and IgM. Encoded by the *JCHAIN* gene in humans, this 15 kDa protein facilitates the assembly of antibody monomers into dimers (IgA) or pentamers (IgM) by linking their Fc regions via disulfide bonds. It also mediates binding to the polymeric immunoglobulin receptor (pIgR), enabling transcytosis of these antibodies across mucosal surfaces. JCHAIN expression is primarily restricted to plasma cells and activated B lymphocytes, underscoring its role in adaptive immunity.

Antibodies targeting JCHAIN are essential tools in immunological research and diagnostics. They are widely used to study antibody polymerization, mucosal immunity, and B-cell differentiation. In clinical contexts, JCHAIN antibodies aid in identifying plasma cell disorders (e.g., multiple myeloma) or autoimmune conditions linked to IgA/IgM dysfunction, such as selective IgA deficiency or Sjögren’s syndrome. Additionally, JCHAIN detection helps characterize pathological secretions in mucosal infections or inflammation. Recent studies also explore its potential as a biomarker in certain cancers, where aberrant JCHAIN expression correlates with tumor progression. However, variability in glycosylation and structural complexity of JCHAIN-containing complexes can challenge antibody specificity, necessitating careful validation for experimental accuracy.