This product is an unconjugated, non-therapeutic research-grade biosimilar of andecaliximab (originally GS-5745), an investigational humanized monoclonal antibody built around the extracellular enzyme MMP9. It is supplied as a research analog for laboratory use only and is not a clinical drug. Andecaliximab was developed as a highly selective inhibitor of matrix metalloproteinase 9, and has been evaluated clinically in indications such as gastric and gastroesophageal junction adenocarcinoma, ulcerative colitis, and rheumatoid arthritis. The molecule is a human IgG4-kappa antibody, an isotype chosen in the originator to limit effector function so that activity derives from target engagement and enzymatic inhibition rather than antibody-dependent cell killing. This research-grade material is intended to reproduce the binding characteristics of the originator so that investigators can study MMP9 engagement, enzyme inhibition, and pathway biology in controlled settings. It is offered at low endotoxin levels and in bulk quantities suitable for repeated in-vitro and functional assays, and as a reference or benchmarking standard. It carries no therapeutic claims and should be handled strictly as a research reagent.
MMP9 (matrix metalloproteinase 9, gelatinase B, 92 kDa type IV collagenase; UniProt P14780) is a secreted, zinc-dependent endopeptidase of the matrixin family. It is produced as a latent zymogen (pro-MMP9) and activated extracellularly, whereupon it degrades components of the extracellular matrix, including denatured collagens and type IV collagen of basement membranes. Through this remodeling activity MMP9 contributes to tissue turnover, angiogenesis, leukocyte trafficking, and inflammation, and its dysregulation is implicated in tumor invasion and metastasis, inflammatory bowel disease, and joint pathology. Structurally it comprises a propeptide, a catalytic domain bearing the canonical zinc-binding motif, fibronectin type-II repeats, and hemopexin-like domains. Andecaliximab binds MMP9 at a site distal to the catalytic pocket, near the prodomain-catalytic junction, blocking activation of the zymogen and allosterically inhibiting the active enzyme.