Anti-MMP8 [Nb14]

Description:

Recombinant monoclonal antibody to MMP8. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the alpaca peripheral lymphocyte Nb14.

Clone Name:

Nb14

Published Application(s):

functional assays, in vivo, SPR, ELISA

Published Species Reactivity:

Human, Mouse

UniProt Accession Number of Target Protein: O70138

Alternative Name(s) of Target: MMP-8; Neutrophil collagenase; Matrix metalloproteinase-8; Matrix Metallo-Proteinase 8; Collagenase 2; PMNL-CL; PMNL collagenase; MNL-CL; CLG1; HNC; Nb 70; Nanobody 70
Immunogen: The original antibody was generated by immunizing an alpaca (Vicugna pacos) with the recombinant mouse catalytic domain of matrix metalloproteinase 8 (mMMP8_CD). A VHH library was constructed using total RNA from peripheral blood lymphocytes, and phages displaying the VHH repertoire were screened for mMMP8_CD-specific nanobodies.

Specificity: This antibody is specific for mouse MMP8. It was found to be cross-reactive with the catalytic domain of human MMP8 (hMMP8_CD). This antibody has inhibitory capacity, achieved by steric hindrance of MMP8 or induction of conformational changes in MMP8 rather than direct binding to the catalytic pocket. This antibody does not exhibit cross-reactivity with other MMPs (human) and ADAM10/ADAM17.

Application Notes: The binding affinity of this antibody's original format (VHH) to different substrates, including the catalytic domain of mouse MMP8 (mMMP8_CD), full-length mouse MMP8 (mMMP8_FL), and the catalytic domain human MMP8 (hMMP8_FL), was measured by ELISA. It had a K_D of 0.24 nM with mMMP8_CD, a K_D of 1.69 nM with mMMP8_FL, and a K_D of 158.4 nM with hMMP8_CD. SPR analysis was conducted to measure its binding kinetics to mMMP8_CD; a K_D of 1.334 ± 0.137 nM was measured. Its in vivo pharmacokinetic properties were studied by injecting a single dose intraperitoneally into mice; blood samples were collected at different time points, and the nanobody's level in the mouse serum was detected using ELISA to evaluate its persistence and clearance in the bloodstream over time. This antibody's inhibitory capacity against MMP8 was investigated; it demonstrated the strongest inhibition of mMMP8_CD with an IC₅₀ of 4.359 µM using DQ gelatin as a substrate and an IC₅₀ value of 19.5 µM using DQ collagen type I. This antibody was used to create a bivalent nanobody by linking it to itself and to clone Nb Albumin using flexible [G₄-S]₃ linkers. The resulting nanobodies (Nb 14-Alb and Nb 14-Alb-14) were used in in vivo experiments for various applications (Demeestere et al., 2016; PMID: 26775809). The original format of this antibody was used to create another trivalent nanobody by linking it to clones Nb 70 and Nb Albumin using the same linkers. The resulting nanobody (Nb 70-Alb-14) was used in vivo to study the effects of inhibiting matrix MMP8 and TNFR1 on sepsis, using endotoxemia and CLP (cecal ligation and puncture; a surgical procedure commonly used in animal models to induce polymicrobial sepsis) experimental models (Steeland et al., 2018; PMID: 29095202).

Antibody first published in: Demeestere et al. Development and Validation of a Small Single-domain Antibody That Effectively Inhibits Matrix Metalloproteinase 8 Mol Ther. 2016 May;24(5):890-902. doi: 10.1038/mt.2016.2 PMID:26775809
Note on publication: The original publication focuses on the development and validation of a small single-domain antibody (nanobody) that effectively inhibits Matrix Metalloproteinase 8 (MMP8).

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