08-115 | Collagen Type I, rat tail

08-115
100  mg
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      Overview

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      Key Spec Table

      Qty/PckKey Applications
      100 mgCULT
      Description
      Catalogue Number 08-115
      Brand Family Upstate
      Trade Name
      • Upstate
      Description Collagen Type I, rat tail
      Overview Liquid Rat tendon Collagen Type I excised from tail.
      References
      Product Information
      Presentation 0.02N acetic acid, pH 3.67
      Applications
      Key Applications
      • Cell Culture
      Application Notes Cell culture attachment factor
      Biological Information
      Species Rat
      Entrez Gene Number
      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
      • OI4
      • COL1A1
      UniProt Number
      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.
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality Assurance Routinely evaluated by testing for uniform gelation and for attachment of and spreading of PC-12 rat cells
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage Conditions 1 year at 4°C
      Packaging Information
      Qty/Pck 100 mg
      Material Size 100
      Material Package mg
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Certificates of Analysis

      TitleLot Number
      Collagen, Type I, Rat Tail (Extracted from rat tail tendons) - 2299578 2299578
      Collagen, Type I, Rat Tail (Extracted from rat tail tendons) - 2373345 2373345
      Collagen, Type I, Rat Tail (Extracted from rat tail tendons) -2425204 2425204
      Millipore - COA - Collagen, Type I, Rat Tail (Extracted from rat tail tendons) - 1957269 1957269
      Millipore - COA - Collagen, Type I, Rat Tail (Extracted from rat tail tendons) - 2197514 2197514
      Millipore - COA - Collagen, Type I, Rat Tail - DAM1571714 DAM1571714
      Millipore - COA - Collagen, Type I, Rat Tail - DAM1606689 DAM1606689
      Millipore - COA - Collagen, Type I, Rat Tail - DAM1713141 DAM1713141
      Millipore - COA - Collagen, Type I, rat tail - 0703054075B1 0703054075B1
      Millipore - COA - Collagen, Type I, rat tail - 0703054075B2 0703054075B2
      Millipore - COA - Collagen, Type I, rat tail - DAM1419397 DAM1419397
      Millipore - COA - Collagen, Type I, rat tail - DAM1471400 DAM1471400
      Millipore - COAs - Collagen Type I, rat tail - 16754 16754
      Millipore - COAs - Collagen Type I, rat tail - 16913 16913
      Millipore - COAs - Collagen Type I, rat tail - 17571 17571
      Millipore - COAs - Collagen Type I, rat tail - 18063 18063
      Millipore - COAs - Collagen Type I, rat tail - 18237 18237
      Millipore - COAs - Collagen Type I, rat tail - 18267 18267
      Millipore - COAs - Collagen Type I, rat tail - 19410 19410
      Millipore - COAs - Collagen Type I, rat tail - 19859 19859
      Millipore - COAs - Collagen Type I, rat tail - 20541 20541
      Millipore - COAs - Collagen Type I, rat tail - 20812 20812
      Millipore - COAs - Collagen Type I, rat tail - 21118 21118
      Millipore - COAs - Collagen Type I, rat tail - 21690 21690
      Millipore - COAs - Collagen Type I, rat tail - 21942 21942
      Millipore - COAs - Collagen Type I, rat tail - 23233 23233
      Millipore - COAs - Collagen Type I, rat tail - 23791 23791
      Millipore - COAs - Collagen Type I, rat tail - 24053 24053
      Millipore - COAs - Collagen Type I, rat tail - 25308 25308
      Millipore - COAs - Collagen Type I, rat tail - 26559 26559
      Millipore - COAs - Collagen Type I, rat tail - 28746 28746
      Millipore - COAs - Collagen Type I, rat tail - 31750 31750
      Millipore - COAs - Collagen Type I, rat tail - 32587 32587

      References

      Reference overviewApplicationPub Med ID
      Chronic stretch of engineered heart tissue induces hypertrophy and functional improvement
      Fink, C., et al
      Faseb J, 14:669-79 (2000) 2000

      Cell Culture10744624
      Leptin promotes invasiveness of kidney and colonic epithelial cells via phosphoinositide 3-kinase-, rho-, and rac-dependent signaling pathways.
      Attoub, S, et al.
      FASEB J., 14: 2329-38 (2000) 2000

      Show Abstract
      Cell Culture11053255
      Notch4 and Wnt-1 proteins function to regulate branching morphogenesis of mammary epithelial cells in an opposing fashion
      Uyttendaele, H., et al
      Dev Biol, 196:204-17 (1998) 1998

      Cell Culture9576833
      Gelatinase A activation is regulated by the organization of the polymerized actin cytoskeleton.
      Tomasek, J J, et al.
      J. Biol. Chem., 272: 7482-7 (1997) 1997

      Show Abstract
      Cell Stimulation9054450
      Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
      Brooks, P. C., et al
      Cell, 85:683-93 (1996) 1996

      Cell Attachment8646777
      Requirement of receptor-bound urokinase-type plasminogen activator for integrin alphavbeta5-directed cell migration
      Yebra, M., et al
      J Biol Chem, 271:29393-9 (1996) 1996

      Cell Attachment8910604