Mouse Anti-Human Type I Collagen

GWB-4902AE

4F6

Reacts with Human Type I Collagen. Cross reactivity with other species has not been established.

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Secreted extracellular space extracellular matrix (By similarity).

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Defects in COL1A2 are a cause of osteogenesis imperfecta type I (OI-I) [MIM:166200]. OI-I is a dominantly inherited serious newborn disease characterized by bone fragility normal stature little or no deformity blue sclerae and hearing loss in 50% of families. Dentinogenesis imperfecta is rare and may distinguish a subset of OI type I (formation of dentine).

Defects in COL1A2 are the cause of cardiac valvular form of autosomal recessive Ehlers-Danlos syndrome (cardiac valvular EDS) [MIM:225320]; also known as arthrochalasis type Ehlers-Danlos syndrome. In addition to joint laxity skin hyperextensibility and friability and abnormal scar formation individuals with this form of EDS appear to be at increased risk for cardiac valvular dysfunction.

Defects in COL1A2 are a cause of osteogenesis imperfecta type IV (OI-IV) [MIM:166220]; also known as osteogenesis imperfecta with normal sclerae. OI-IV presents with moderate to mild deformity and variable short stature. Dentinogenesis imperfecta is common and hearing loss occurs in some.

Belongs to the fibrillar collagen family. [1] Makela J. K. Vuorio T. and Vuorio E. et al. Growth-dependent modulation of type I collagen production and mRNA levels in cultured human skin fibroblasts[2] de Wet W. J. Bernard M. P. Benson-Chanda V. Chu M. -L. Dickson L. A. Weil D. Ramirez F. Organization of the human pro-alpha 2(I) collagen gene. [3] Dalgleish R. The human type I collagen mutation database. [4] Korkko J. M. Ala-Kokko L. De Paepe A. Nuytinck L. Earley J. J. Prockop D. J. Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations. [5] Kuivaniemi H. Tromp G. Chu M. -L. Prockop D. J. Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation. [6] Dickson L. A. de Wet W. Di Liberto M. Weil D. Ramirez F. Analysis of the promoter region and the N-propeptide domain of the human pro alpha 2(I) collagen gene. [7] Akai J. Kimura A. Arai K. Uehara K. Hata R. Fine structural analysis of the unique 5\' region of the human COL1A2 gene containing two regions of dinucleotide repeats adjacent to the transcriptional start site. [8] Weil D. D\' Alessio M. Ramirez F. Eyre D. R. Structural and functional characterization of a splicing mutation in the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient. [9] Watson R. B. Wallis G. A. Holmes D. F. Viljoen D. Byers P. H. Kadler K. E. Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section. [10] Click E. M. Bornstein P. Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen.