ACPA, Monoclonal Antibody (Clone E4NG), 100ug

This antibody recognizes multiple citrullinated proteins/peptides, including CCP2, citrullinated collagen type 2 (COL2) peptides, citrullinated human/mouse alpha-enolase (citENO1), etc., and potentially other citrullinated proteins/peptides typically manifested in rheumatoid arthritis, as a...

Antibodies

1061006

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For research use only. Not for use in diagnostic procedures.

This antibody recognizes multiple citrullinated proteins/peptides, including CCP2, citrullinated collagen type 2 (COL2) peptides, citrullinated human/mouse alpha-enolase (citENO1), etc., and potentially other citrullinated proteins/peptides typically manifested in rheumatoid arthritis, as a citrulline-specific antibody. E4NG has a mutation on glycosylation sites in the variable domain, prohibiting the expression of the Fab-glycan (no N-glycosylation on the variable domain). It cross-reacts with mouse and human.

Note: For negative control antibody use Catalogue number 1061006-NC

Anti-citrullinated protein antibodies (ACPA) are autoantibodies linked to rheumatoid arthritis (RA). In RA research, collagen-induced arthritis (CIA) or CAIA mouse models are used to study ACPA's role in disease mechanisms like inflammation and joint damage.

Synonyms:
Citrullinated epitopes of COL2, Collagen alpha-1(II) chain, COL2A1, type II collagen, CII1; Citrullinated epitopes of ENO1, MPB

 

Monoclonal Antibody to ACPA Anti–Citrullinated Protein Antibody, Affinity Purified

The antibody clone E4NG (Catalogue number 1061006) binds to citrullinated collagen type II (COL2) epitopes. E4NG-mutant (Catalogue number 1061006-NC) is the control antibody that does not bind to citrulline. Binding to unmodified COL2 peptides is low by both E4NG and E4NG-mutant antibodies. A multiplex flow immunoassay determined binding. (Results published in He et al Nat Comm 2023)

 

References:

1. He, Y., Ge, C., Moreno-Giró, À. et al. A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. Nat Commun 14, 691 (2023).

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