Collagen I
Collagen I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. The COL1A2 gene (also known as OI4) encodes its pro-alpha2 chain, one of the two chain types that make up the triple helix. Browse Assay Genie's current range of Collagen I research reagents below, or read on for the biology behind the target.
Type I collagen is a member of group I collagen, the fibril-forming collagens, and belongs to the fibrillar collagen family. It is a secreted protein that is deposited in the extracellular space as part of the extracellular matrix. Its triple helix comprises two alpha1 chains and one alpha2 chain, and the alpha2 chain is the product of the COL1A2 gene. Collagen I is found in most connective tissues and is particularly abundant in bone, cornea, dermis and tendon.
The collagen type I alpha 2 chain gene encodes the pro-alpha2 chain of type I collagen. UniProt names the mature product collagen alpha-2(I) chain. HGNC places the gene in the fibrillar collagens group. Three transcripts, produced through the use of alternate polyadenylation signals, have been identified for this gene. The mouse and rat orthologs are both named Col1a2, which makes rodent models a practical route for studying the gene.
The gene's earlier names reflect its disease associations: osteogenesis imperfecta type IV, with the alias OI4, as well as collagen, type I, alpha 2. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIB, recessive Ehlers-Danlos syndrome Classical type, idiopathic osteoporosis and atypical Marfan syndrome. Symptoms tend to be less severe than those caused by mutations in COL1A1, the gene for the alpha1 chain of type I collagen. This difference is thought to reflect the different role of alpha2 chains in matrix integrity. Researchers studying the Collagen I protein or the COL1A2 gene therefore often consider it alongside COL1A1.
Collagen I is a fibril-forming collagen found in most connective tissues, making it a core component for studying matrix structure.
Type I collagen is abundant in bone, and COL1A2 mutations are associated with osteogenesis imperfecta and idiopathic osteoporosis.
Collagen I is abundant in dermis, cornea and tendon, supporting work on the matrix of these tissues.
COL1A2 variants are linked to Ehlers-Danlos syndrome types and atypical Marfan syndrome, as well as osteogenesis imperfecta.
Collagen I is a fibril-forming collagen found in most connective tissues, and is abundant in bone, cornea, dermis and tendon. Its triple helix contains two alpha1 chains and one alpha2 chain. The alpha2 chain, encoded by COL1A2, contributes to the integrity of the matrix.
COL1A2 encodes collagen type I alpha 2 chain, called collagen alpha-2(I) chain in UniProt. Its alias is OI4. Previous names include osteogenesis imperfecta type IV and collagen, type I, alpha 2. The gene produces three transcripts through alternate polyadenylation signals.
Mutations in COL1A2 are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndromes, idiopathic osteoporosis and atypical Marfan syndrome. Mouse and rat both carry a Col1a2 ortholog; check the datasheet of any product for its validated reactivity.
Other fibrillar and non-fibrillar collagens and extracellular matrix proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P08123; product specifications from Assay Genie datasheets.