COL11A2
COL11A2 (collagen type XI alpha 2 chain, also known as HKE5, DFNA13 and DFNB53) encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen of the extracellular matrix. It is thought to help control the lateral growth of collagen II fibrils. Browse Assay Genie's current range of COL11A2 research reagents below, or read on for the biology behind the target.
COL11A2 encodes collagen alpha-2(XI) chain, one of the two alpha chains of type XI collagen, a minor member of the fibrillar collagen family. The protein is secreted into the extracellular space and forms part of the extracellular matrix. It may play an important role in fibrillogenesis by controlling the lateral growth of collagen II fibrils.
Type XI collagen is a heterotrimer, but its third alpha chain is not a separate type XI gene product: it is a post-translationally modified alpha 1 type II chain. Proteolytic processing of the COL11A2 chain produces PARP, a proline/arginine-rich protein that corresponds to an amino-terminal domain. The COL11A2 gene is located on chromosome 6, very close to but separate from the gene for retinoid X receptor beta, and a related pseudogene lies nearby on the same chromosome. Alternative splicing results in multiple transcript variants. The mouse ortholog is Col11a2, and HGNC classifies the gene in the fibrillar collagens group. The previous name was collagen, type XI, alpha 2.
Mutations in the COL11A2 gene are associated with several connective tissue and hearing disorders: type III Stickler syndrome, otospondylomegaepiphyseal dysplasia (OSMED syndrome) and Weissenbacher-Zweymuller syndrome. They are also linked to autosomal dominant non-syndromic sensorineural deafness type 13 (DFNA13) and autosomal recessive non-syndromic sensorineural deafness type 53 (DFNB53), which account for two of the gene's aliases. This makes COL11A2 a useful target for researchers studying matrix assembly and inherited skeletal and hearing conditions.
COL11A2 may control the lateral growth of collagen II fibrils, making it relevant to studies of how fibrillar collagen networks assemble.
As a secreted minor fibrillar collagen chain, it is studied for its contribution to matrix structure alongside the type II collagen chain in the type XI heterotrimer.
Mutations are associated with type III Stickler syndrome, OSMED syndrome and Weissenbacher-Zweymuller syndrome, supporting disease-mechanism research.
COL11A2 variants are linked to non-syndromic sensorineural deafness DFNA13 and DFNB53, making it a focus in genetic studies of hearing.
COL11A2 encodes one of the two alpha chains of type XI collagen, a minor fibrillar collagen secreted into the extracellular matrix. It may play an important role in fibrillogenesis by controlling the lateral growth of collagen II fibrils. Proteolytic processing of the chain also produces PARP, an amino-terminal domain.
COL11A2 is also known as HKE5, DFNA13 and DFNB53, and was previously named collagen, type XI, alpha 2. UniProt lists the protein as collagen alpha-2(XI) chain. The DFNA13 and DFNB53 aliases come from deafness forms linked to mutations in the gene. Alternative splicing gives multiple transcript variants.
Mutations in COL11A2 are associated with type III Stickler syndrome, OSMED syndrome, Weissenbacher-Zweymuller syndrome, and non-syndromic sensorineural deafness types DFNA13 and DFNB53. The mouse ortholog is Col11a2. Check the datasheet of any product for its validated reactivity.
Other fibrillar and minor collagens, including type XI partner chains and related extracellular matrix targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P13942; product specifications from Assay Genie datasheets.