Affinity purified mouse monoclonal anti- citrullinated collagen type II antibody clone ACC1 in PBS, sterile filtered (0.2 µm)
| 100 µg / 0.1 mL | 328 € |
| 1 mg / 1 mL | 1,548 € |
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The Anti-citrullinated COL2A1 Antibody clone ACC1 binds to the triple helical C1 epitope on collagen II when citrullinated. Binding to collagen II epitopes was determined in bead-based flow immunoassay as median fluorescence intensity (MFI).
Description
Recombinant, affinity purified, chimeric human-mouse monoclonal anti collagen II (COL2A1) antibody clone ACC1 in PBS, sterile filtered (0.2 µm). The antibody binds to the citrullinated triple helical collagen type II (CII) epitope (position 359-369; ARGLTGRPGDA)1, the C1 epitope. The ACC1 antibody recognizes the second citrulline at position 365 in mouse CII1. The antibody binds to flexible triple-helical CII determinants as well as many citrullinated CII peptides and was found to cross-react with several non-citrullinated epitopes on native CII2. The antigen or epitope-binding specificity of this antibody is identical to its mouse IgG2a variant (#10130)1,2.
Target with alternative names
COL2A1, Collagen alpha-1(II) chain, CII, Col II, citrullinated CII; citrullinated Col II; citrullinated proteins. UniProt: P28481.
Immunogen
Bovine Collagen type II 1
Species reactivity:
Mouse, human
Isotype
Human IgG1, κ
ACC1 antibody binds the citrullinated C1 epitope. The ACC1 antibody cross-reacts with triple-helical epitopes on CII, but not with other collagens or the proteins tested in Ge et al2, except for a few citrullinated peptides.2
Concentration
1 mg/ml
Supplied in
PBS
Storage
Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -‑20°C long term. Avoid repeated freeze/thaw cycles.
It is recommended the user determines the optimal dilution for their application. The typical starting working dilutions are: IHC 1:100, ELISA 1:200 - 1:500.
For Research Use Only. Not for use in diagnostic procedures.
Not for resale without express authorization.
References
https://link.springer.com/article/10.1186/s13075-022-02945-0