United Kingdom (UK)
Recombinant monoclonal antibody to Collagen I . Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma AFA.
Alternative Name(s) of Target: CTTR1; α2Ct; α2(I)C-telopeptide; C-terminal telopeptide of the α2 chain; Procollagen I
Immunogen: The original antibody was produced by immunizing mice with a synthetic peptide (GGGYDFGYDGDFYRA) whose sequence corresponds to that of the C-terminal telopeptide of the α2 chain (α2Ct).
Specificity: This antibody is specific for human collagen I, showing high affinity to the GDF sequence (in A2_DGDFY, part of the α2(I)C-telopeptide), suggesting it is a critical epitope.
Application Notes: This antibody binds human collagen I and blocks the binding activity of its C-terminal telopeptide region (denoted as CTTR1) consisting of two α1(I)C-telopeptides (denoted as α1Ct) and one α2(I)C-telopeptide (denoted as α2Ct). The KD of this antibody and its Fab and scFv with native α2Ct present in procollagen I and with synthetic α2Ct were 663 pM, 268 nM, 21 pM, 57 nM, and 75nM for full-length AFA/procollagen I, Fab AFA antibody/procollagen I, full-length AFA antibody/synthetic α2Ct, Fab AFA antibody/synthetic α2Ct, and scFv/procollagen I, respectively (US20200048333A1). A chimeric IgG version of the original IgA version of this antibody was engineered (Fertala et al., 2013; PMID: 23586407). This antibody has been shown to be an effective therapeutic tool for blocking collagen fibril formation in various models (Fertala et al., 2017; PMID: 28972447) (Fertala et al., 2017; PMID: 23586407).
Antibody first published in:
Chung et al. Collagen fibril formation. A new target to limit fibrosis J Biol Chem. 2008 Sep 19;283(38):25879-86. doi: 10.1074/jbc.M804272200 PMID:18650436
Note on publication:
The original publication introduces a novel concept for reducing fibrotic deposits by inhibiting the self-assembly of collagen molecules into fibrils, utilizing monoclonal antibodies targeting the telopeptide region to block collagen interactions and demonstrating efficacy in reducing collagen fibrils in vitro and in organotypic constructs.