ITM3764
ITM3764
- Catalog: ITM3764
- Gene/Protein: COL1A1
- Product Description: Immunotag™ Collagen I mouse Monoclonal Antibody(4H10)
405.0000
Price in reward points: 405
| Antibody Specification | |
| Datasheet | 
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| Target Protein | Collagen I (4H10) |
| Clonality | Monoclonal |
| Storage/Stability | -20°C/1 year |
| Application | IF,IHC-p |
| Recommended Dilution | IF: 1:50-200 IHC-p 1:50-300 |
| Concentration | 1 mg/ml |
| Reactive Species | Human,Mouse,Rat |
| Host Species | Mouse |
| Immunogen | Synthetic Peptide of Collagen I |
| Specificity | The antibody detects endogenous Collagen I protein |
| Purification | The antibody was affinity-purified from mouse antiserum by affinity-chromatography using epitope-specific immunogen |
| Form | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. |
| Gene Name | COL1A1 |
| Accession No. | P02452 P11087 P02454 |
| Alternate Names | Collagen alpha-1(I) chain (Alpha-1 type I collagen) |
| Description | collagen type I alpha 1 chain(COL1A1) Homo sapiens 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, Feb 2008], |
| Cell Pathway/ Category | Focal adhesion,ECM-receptor interaction, |
| Protein Expression | Bone,Brain,Fetal brain cortex,Skin,Spleen, |
| Subcellular Localization | extracellular region,collagen trimer,collagen type I trimer,extracellular space,endoplasmic reticulum lumen,Golgi apparatus,integral component of membrane,secretory granule,extracellular matrix, |
| Protein Function | disease: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.,disease:Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.,disease: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).,disease: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).,disease: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.,disease: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.,disease: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.,disease:Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:130060]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.,disease: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.,function:Type I collagen is a member of group I collagen (fibrillar forming collagen).,online information:Collagen type I alpha-1 chain mutations,online information:Type-I collagen entry,PTM:O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.,PTM:Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.,similarity:Belongs to the fibrillar collagen family.,similarity:Contains 1 VWFC domain.,subunit:Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2.,tissue specificity:Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite., |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |
| Material Safety Data Sheet | |
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