Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.

P4HA1 Protein, Human, Recombinant (His) is expressed in E. coli.

P4HA3 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.

BMP-1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 102.0 kDa and the accession number is P13497.

PLOD3 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with N-10xHis tag. The predicted molecular weight is 85.9 kDa and the accession number is O60568.

Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. PLOD2 Protein, Mouse, Recombinant (His & Myc) is expressed in Baculovirus insect cells with C-6xHis-Myc tag. The predicted molecular weight is 85.2 kDa and the accession number is Q9R0B9.

Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM40) is one of the most abundant non-collagenous protein expressed in mineralized tissues.The capacity of SPARC to influence pathways involved in extracellular matrix assembly such as procollagen processing and collagen fibril formation as well as the capacity to influence osteoblast differentiation and osteoclast activity will be addressed.

Langerin (CD207) is a type II transmembrane glycoprotein which is member K of the C-type lectin domain family. Langerin is used as a marker for Langerhans cells (LCs) which represent the immature dendritic cells in the epidermis. Langerin is necessary and sufficient for Birbeck granule formation. Human langerin sequence contains a 43 aa cytoplasmic domain, a 21 aa transmembrane domain and a 264 aa extracellular domain (ECD) that contains a coiled-coil domain and a single C-type lectin domain. Human langerin shares 68%, 62%, 71% aa identity with mouse, rat and bovine langerin ECD, respectively. Trimerization greatly increases the lectin binding affinity. Langerin internalizes endogenous proteins such as type I procollagen. Internalization by LC is thought to lead to suppression of self reactions. Langerin also mediates endocytosis of non-peptide antigens containing mannose, N-acetyl glucosamine and fucose that are expressed by mycobacteria and fungae.

Collagen alpha-1(III) chain（Col3a1） is a secreted protein and belongs to the fibrillar collagen family.It contains 1 fibrillar collagen NC1 domain and 1 VWFC domain. Collagen alpha-1(III) chain is a fibrillar collagen that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. The COL3A1 gene produces the components of type III collagen, called pro-alpha1(III) chains. Three copies of this chain combine to make a molecule of type III procollagen. These triple-stranded, rope-like procollagen molecules must be processed by enzymes outside the cell to remove extra protein segments from their ends. Once these molecules are processed, the collagen molecules arrange themselves into long, thin fibrils. Within these fibrils, the individual collagen molecules are cross-linked to one another. These cross-links result in the formation of very strong mature type III collagen fibrils, which are found in the spaces around cells.

MFAP5 (Microfibril Associated Protein 5, also known as MAGP2) is a Protein Coding gene. MFAP5 is a component of the elastin-associated microfibrils. It belongs to the MFAP family. As a 25-kD microfibril-associated glycoprotein, MFAP5 is rich in serine and threonine residues. It stimulates the assembly of elastic fibers, a complex structure composed of a tropoelastin inner core and microfibril outer mantle comprising proteins such as fibrillins and microfibril-associated glycoproteins that guide tropoelastin deposition. MFAP5 also stabilizes type 1 procollagen and thus plays an important role in extracellular matrix homeostasis. It has multiple binding regions on fibrillins and has a covalent periodic association with fibrillin-containing microfibrils. Diseases associated with MFAP5 include Aortic Aneurysm, Familial Thoracic 9, and Familial Thoracic Aortic Aneurysm And Aortic Dissection.

COL5A2 is a component of type V collagen. It is known as the pro-alpha2(V) chain. COL5A2, together with two pro-alpha1(V) chains can form type V procollagen. These triple-stranded, rope-like procollagen molecules arrange themselves into long, thin fibrils that cross-link to one another in the spaces around cells. The cross-links result in the formation of very strong, mature type V collagen fibers. Type V collagen can be detected in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen.