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Key Specifications Table
| Key Applications |
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| CULT |
| Description | |
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| Catalogue Number | CC050 |
| Brand Family | Chemicon® |
| Trade Name |
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| Description | Human Collagen Type I |
| Overview | Human type I collagen purified by serial salt precipitations, alcohol precipitation and DEAE chromatography of a pepsin extraction of human placenta. Composition: [α1(I)]2, <α2(I), native triple helix. |
| Background Information | COL1A1 is the gene responsible for the production of the alpha1(I) chain of type I collagen. Collagen, which adds structure and strength to connective tissues, is found throughout the body for example, in skin, tendon, cartilage, ligaments, bone, the part of the eyeball that is white (sclera), and the spaces between cells and tissues called the extracellular matrix. Type I collagen is initially produced as procollagen in cells. This protein consists of two pro-alpha1(I) protein strands combined with a pro-alpha2(I) procollagen strand that form a triple-stranded rope-like structure. While in the cell, enzymes modify certain amino acids in the protein (lysine and proline) by adding chemical groups that are necessary for the three strands to form stable molecules and make connections (cross-links) between chains. Other enzymes add sugars to the protein. Now complete, the triple-stranded type I procollagen molecule leaves the cell and is processed by enzymes that clip small segments off both ends. The procollagen molecules arrange themselves into long, thin fibrils outside of the cell. The fibrils come together in side-by-side groups to form collagen fibers. Cross-linking between molecules in fibrils produces a very stable protein structure, which contributes to collagens tissue strengthening function. {http://ghr.nlm.nih.gov} |
| Product Information | |
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| Presentation | Purified protein. Liquid containing 0.5 M Acetic acid, pH 2.5. Can be diluted in PBS for applications. |
| Quality Level | MQ100 |
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| Key Applications |
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| Biological Information | |
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| Concentration | 1 mg/mL |
| Purity | > 90% collagen type I. Purity was controlled by SDS-PAGE and reaction with anti-collagen type-specific antibodies. Contaminants: < 10% collagen type III, < 1% collagen type II, IV-VI and non-collagen proteins. |
| Source | Human placenta, negative for HBsAG and HIV antibodies. |
| Entrez Gene Number |
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| Entrez Gene Summary | This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish] |
| Gene Symbol |
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| UniProt Number |
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| UniProt Summary | FUNCTION: SwissProt: P02452 # Type I collagen is a member of group I collagen (fibrillar forming collagen). SIZE: 1464 amino acids; 138911 Da SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. PTM: Proline residues at the third position of the tripeptide repeating unit (g-X-Y) are hydroxylated in some or all of the chains. & O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. DISEASE: SwissProt: P02452 # Defects in COL1A1 are the cause of Caffey disease [MIM:114000]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. & Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type I (EDS-I) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis. Ehlers-Danlos syndrome is a genetically and phenotypically heterogeneous connective-tissue disorder characterized by loose- jointedness and fragile, velvety, stretchable, bruisable skin that heals with peculiar cigarette-paper scars. EDS-I is an autosomal dominant trait. & Defects in COL1A1 are a cause of autosomal dominant Ehlers-Danlos syndrome type VII (EDS-VII) [MIM:130060]; which includes also Ehlers-Danlos syndrome type VII-A1. EDS-VII is characterized by arthrochalasis multiplex congenita, skin hyperextensibility and bruisability. & Defects in COL1A1 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 COL1A1 are a cause of osteogenesis imperfecta type II (OI-II) [MIM:166210]; also known as osteogenesis imperfecta congenita. OI-II is lethal in the perinatal period and is charaterized by calvarial mineralization, beaded ribs, compressed femurs, marked long bone deformity and platyspondyly (congenital flattening of the vertebral bodies). & Defects in COL1A1 are a cause of osteogenesis imperfecta type III (OI-III) [MIM:259420]; also called progressively deforming osteogenesis imperfecta with normal sclerae. OI-III is characterized by progressively deforming bones, usually with moderate deformity at birth, sclerae is variable in color, dentinogenesis imperfecta and hearing loss are common. The stature is very short. & Defects in COL1A1 are a cause of osteogenesis imperfecta type IV (OI-IV) [MIM:166220]. OI-IV is charaterized by normal sclerae, moderate to mild deformity and variable short stature. Dentinogenesis imperfecta is common and hearing loss occurs in some patients. & Genetic variations in COL1A1 are associated with susceptibility to involutional osteoporosis [MIM:166710]; also known as senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mineral density, disrutption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture. & A chromosomal aberration involving COL1A1 is a cause of dermatofibrosarcoma protuberans (DFSP) [MIM:607907]. Translocation t(17;22)(q22;q13) with PDGF. DFSP is an uncommon, locally aggressive, but rarely metastasizing tumor of the deep dermis and subcutaneous tissue. It typically occurs during early or middle adult life and is most frequently located on the trunk and proximal extremities. SIMILARITY: SwissProt: P02452 ## Belongs to the fibrillar collagen family. & Contains 1 VWFC domain. |
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| Product Usage Statements | |
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| Usage Statement |
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| Storage and Shipping Information | |
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| Storage Conditions | Maintain at -20°C in undiluted aliquots for up to 12 months. Avoid repeated freeze/thaw cycles. |
| Packaging Information | |
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| Material Size | 100 µg |