This product has not been tested for platelet aggregation. The end user would have to determine suitability, although Collagen Type I has been sited in the literature in platelet aggregation studies. Collagen Type III and IV are more commonly cited, however. Please see the links below to review alternative Collagen products that have been successfully used by other researchers for platelet aggregation:
Human Collagen Type IV
https://www.sigmaaldrich.com/product/sigma/c7521
https://www.sigmaaldrich.com/US/en/product/sigma/h4417
Human Collagen Type III
https://www.sigmaaldrich.com/US/en/product/sigma/c4407
C9879
Bovine Collagen Type I
from bovine achilles tendon, powder, suitable for substrate for collagenase
Synonym(s):
Collagen powder
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About This Item
Form:
powder
Biological source:
bovine Achilles tendon
Pricing and availability is not currently available.
Product Name
Collagen from bovine achilles tendon, powder, suitable for substrate for collagenase
biological source
bovine Achilles tendon
Quality Level
form
powder
technique(s)
ELISA: suitable, activity assay: suitable
suitability
suitable for substrate for collagenase
UniProt accession no.
storage temp.
2-8°C
General description
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
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.
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[1][2]
- 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[3]
- 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[4]
Biochem/physiol Actions
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.[5][6]
Preparation Note
Prepared by the method of Einbinder, J. and Schubert, M., J. Biol. Chem., 188, 335 (1951).
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.
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This Item | |||
|---|---|---|---|
| technique(s) ELISA: suitable, activity assay: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | stem cell: suitable | technique(s) - |
| biological source bovine Achilles tendon | biological source rat tail | biological source human | biological source - |
| suitability suitable for substrate for collagenase | suitability - | suitability - | suitability - |
| form powder | form powder | form powder | form liquid |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. - |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
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Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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
M L Tanzer
Science (New York, N.Y.), 180(4086), 561-566 (1973-05-11)
The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C9879-25G | 04054839595417 |
| C9879-1G | 04061833531297 |
| C9879-5G | 04061833531303 |
| C9879-10G | 04061833629451 |
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Is this collagen suitable as an agonist in platelet aggregation assays?
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Is this suitable for cell culture?
1 answer-
This product has not been tested for suitability in cell culture applications. Please see products C9791 and C8919 at the link below to review cell culture tested product options:
https://www.sigmaaldrich.com/substance/bovinecollagentypei123459007345Helpful?
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What is the most suitable solvent for this product?
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As mentioned in the 'DESCRIPTION' section under '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.
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Is it suitable to fabricate a 3D matrix with gelatin and water?
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This collagen product is not tested for 3D gel formation. Residual acids from the extraction and purification process may impact the ability of the material to form a 3D matrix. However, there are several bovine collagen products that are recommended for this application. Please see the links below to review these product options:
Bovine Collagen Type I for 3D
https://www.sigmaaldrich.com/US/en/substance/bovinecollagentypei1234598765
Bovine Collagen Solutions for 3D
https://www.sigmaaldrich.com/US/en/substance/collagensolutionfrombovineskin1234598765Helpful?
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Do you have a nominal purity on this product?
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The purity of this product is not tested. It is qualified for use as a substrate for collagenase.
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What application can Product No. C9879, Collagen from bovine, be used in?
1 answer-
This product is suitable for use as a substrate for collagenase. It is not suitable for use as an attachment factor in coating glassware.
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What is the molecular weight of product C9879, Collagen from bovine achilles tendon?
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Since product C9879 is an insoluble collagen preparation, it is difficult to make any kind of molecular weight determination. However, based on the reported structure of this collagen, the expected molecular weight would be approximately 300 kDa.
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What is the structure of the Collagen from bovine - C9879?
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The amino acid sequence of the primary structure is mainly a repeating motif with glycine in every third position, and a proline or 4-hydroxyproline frequently preceding the glycine residue.
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What is the Department of Transportation shipping information for this product?
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Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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How should Product No. C9879, Collagen from bovine, be reconstituted?
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This product is an insoluble collagen preparation. It is insoluble in water, aqueous buffers, dilute acid, and organic solvents. A suspension can be prepared in 50 mM TES buffer, pH 7.4 with 0.36 mM calcium chloride, but not a clear solution.
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