C9879
Bovine Collagen Type I
from bovine achilles tendon, powder, suitable for substrate for collagenase
Synonyme(s) :
Collagen powder
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About This Item
Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61
Produits recommandés
product name
Collagen from bovine achilles tendon, powder, suitable for substrate for collagenase
Source biologique
bovine Achilles tendon
Niveau de qualité
Forme
powder
Technique(s)
ELISA: suitable
activity assay: suitable
Adéquation
suitable for substrate for collagenase
Numéro d'accès UniProt
Température de stockage
2-8°C
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Description générale
Collagen is a widely expressed protein in the body. There are 20 different types of collagen in human tissue. Type I collagen is the abundant bone protein. It constitutes ~90% of bone organic matter.
Collagen is classified into a number of structurally and genetically distinct types. We use the nomenclature proposed by Bornstein and Traub. Do not confuse Sigma type designations with recognized collagen classification types.
Collagen terminology using the Bornstein and Traub designation originates from the reference; Bornstein, P. and Traub, W. The Proteins, (1979) 4, 411-605
Application
Bovine achilles tendon collagen was used in a study of plant extracts as inhibitors of MMP-collagenases, the putative active agents in the breakdown of cartilage in osteoarthritis and rheumatoid arthritis.
Collagen from bovine achilles tendon is suitable for use in:
- the detection of collagenase activity
- as a reference sample in the thermal analysis study of human bone using differential scanning calorimetry, thermogravimetry, gas chromatography and Fourier transform infrared spectroscopy
- as a substrate for developing a simple assay for determining collagen degradation in vitro
- a study to examine the binding activity of the integral glycoprotein dipeptidyl peptidase IV to insoluble type I collagen by solid-phase enzyme-linked immunosorbent assay
Actions biochimiques/physiologiques
Collagen from bovine Achilles tendon is a naturally occurring protein in the form of elongated fibrils. It may be used in studies of the fibrocartilaginous zone, which the collagen must first pass through before inserting into the calcaneus. It may also be used in studies of growth factor effects on collagen content and cross-linking during Achilles tendon healing.
Collagen is an insoluble fibrous protein that is part of the extracellular matrix and the connective tissue. It is responsible for the ability of the tissues to withstand stretching. The long precursors called procollagens are synthesized and assembled in the ER, secreted into the extracellular space and processed to form collagen fibres. The different types of collagen are composed of molecules containing three polypeptide chains arranged in a triple helical conformation varying slightly in the amino acid sequence. The primary structure is a repeating motif with glycine in every third position preceded frequently with a proline or 4-hydroxyproline residue.
Notes préparatoires
Prepared by the method of Einbinder, J. and Schubert, M., J. Biol. Chem., 188, 335 (1951).
Reconstitution
This product is an insoluble collagen preparation. It is insoluble in water, aqueous buffers, dilute acid, and organic solvents. For use as a substrate in collagenase assays, this collagen can be prepared as a suspension in 50 mM TES buffer, pH 7.4 with 0.36 mM calcium chloride.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
E K Steffen et al.
Journal of clinical microbiology, 14(2), 153-156 (1981-08-01)
Thirty-three strains of anaerobic bacteria isolated from human clinical specimens were examined for the presence of heparinase, hyaluronidase, chondroitin sulfatase, gelatinase, collagenase, fibrinolysin, lecithinase, and lipase activities. Pronounced heparinase activity was limited to species of the genus Bacteroides. A number
Thermal analysis study of human bone
Lozano L F, et al.
J. Mater. Sci., 38, 4777-4782 (2003)
Structurally distinct collagen types.
P Bornstein et al.
Annual review of biochemistry, 49, 957-1003 (1980-01-01)
Bradley E Layton et al.
Journal of molecular evolution, 66(6), 539-554 (2008-06-04)
Two competing effects at two vastly different scales may explain collagen's current translation length. The necessity to have long molecules for maintaining mechanical integrity at the organism and supraorganism scales may be limited by the need to have small molecules
S Bjelland et al.
Archives of dermatological research, 280(1), 50-53 (1988-01-01)
A simple assay measuring degradation of human epidermal keratin and bovine tendon collagen is presented. Insoluble protein substrate (30 mg) was incubated with 1 ml buffer and enzyme sample for 1 h at 37 degrees C, following addition of 1
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