Recombinant Human COL17 protein

Collagen XVIII (COL18) is a multifaceted component of the extracellular matrix, belonging to the multiplexin collagen family characterized by interrupted triple-helical domains and multiple non-collagenous regions. It exists as three major isoforms (short, medium, and long) produced by alternative splicing of the COL18A1 gene. The protein’s C-terminal end contains the endostatin domain, a bioactive fragment with anti-angiogenic properties released upon proteolytic cleavage. COL18 is widely expressed in basement membranes of tissues like the liver, kidney, and eye, where it contributes to structural stability, cell adhesion, and tissue organization.

Research on COL18 gained momentum due to its role in human diseases. Mutations in COL18A1 are linked to Knobloch syndrome, a rare disorder characterized by ocular defects and occipital encephalocele. Additionally, COL18 deficiency in mice models revealed impaired retinal angiogenesis and muscle regeneration, highlighting its importance in developmental and repair processes. The endostatin domain, in particular, has been extensively studied for its ability to inhibit endothelial cell proliferation and tumor growth, making it a candidate for anticancer therapies.

Recombinant COL18 proteins, often generated in mammalian or bacterial expression systems, enable detailed functional studies and therapeutic exploration. These proteins retain critical domains for binding heparan sulfate proteoglycans and integrins, facilitating research into their roles in vascular biology, fibrosis, and tissue remodeling. Recombinant endostatin (e.g., Endostar) has already entered clinical trials for cancers and age-related macular degeneration. Challenges remain in producing full-length COL18 with proper post-translational modifications, but advances in protein engineering continue to refine its applications in regenerative medicine and disease modeling. Overall, COL18 exemplifies the intersection of structural complexity and therapeutic potential in extracellular matrix biology. (Word count: 398)

COL17 (Type XVII collagen), also known as BP180 or BPAG2. is a transmembrane protein belonging to the collagen family. It is encoded by the COL17A1 gene in humans, located on chromosome 10. Structurally, COL17 consists of a non-collagenous intracellular N-terminal domain, a transmembrane region, and a large extracellular C-terminal domain containing multiple collagenous repeats. This unique configuration allows it to anchor epithelial cells to the basement membrane by forming hemidesmosomes, critical structures for epidermal-dermal adhesion. COL17 interacts with laminin-332 and integrin α6β4. stabilizing tissue integrity in skin and mucous membranes.

Functionally, COL17 plays a vital role in maintaining epithelial homeostasis, tissue regeneration, and wound healing. Its expression is particularly prominent in basal keratinocytes. Research has linked COL17 mutations to junctional epidermolysis bullosa (JEB), a blistering skin disorder characterized by fragile skin and mucosal tissues. Additionally, COL17 dysregulation is implicated in autoimmune blistering diseases like bullous pemphigoid, where autoantibodies target its extracellular domain, disrupting cell-matrix adhesion.

Recombinant COL17 protein, typically produced in mammalian or insect cell systems, retains key functional domains and is widely used to study molecular mechanisms of skin diseases, screen therapeutic antibodies, or model cell-matrix interactions. In cancer biology, COL17 overexpression in certain carcinomas correlates with tumor invasion and metastasis, highlighting its dual role in tissue repair and pathology. Recent studies also explore its potential in regenerative medicine, as COL17 expression declines with aging, affecting stem cell maintenance. Therapeutic strategies leveraging recombinant COL17 aim to restore hemidesmosome function or block pathogenic autoantibodies, offering promising avenues for treating genetic and acquired epithelial disorders.