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C9879

Sigma-Aldrich

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

CAS Number:
9007-34-5
EC Number:
232-697-4
MDL number:
MFCD00130825
UNSPSC Code:
12352202
NACRES:
NA.61

Product Name

Collagen from bovine achilles tendon, powder, suitable for substrate for collagenase

biological source

bovine Achilles tendon

Quality Level

200

form

powder

technique(s)

ELISA: suitable
activity assay: suitable

suitability

suitable for substrate for collagenase

UniProt accession no.

P02459

storage temp.

2-8°C

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General description

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
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.

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.

Preparation Note

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
0000360894
0000350126
0000334798
0000325265
0000324146

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

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  4. What is the Department of Transportation shipping information for this product?

    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. 

  5. How should Product No. C9879, Collagen from bovine, be reconstituted?

    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.

  6. What application can Product No. C9879, Collagen from bovine, be used in?

    This product is suitable for use as a substrate for collagenase. It is not suitable for use as an attachment factor in coating glassware.

  7. What is the structure of the Collagen from bovine - C9879?

    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.

  8. What is the molecular weight of product C9879, Collagen from bovine achilles tendon?

    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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    Ask a Scientist here.

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
J M Nagmoti et al.
Indian journal of medical microbiology, 26(1), 65-67 (2008-01-30)
Anaerobic gram-negative bacteria (AGNB) produce enzymes that play a significant role in the development of disease. We tested 50 AGNB isolates, 25 each from clinically diseased and healthy human sites for in vitro production of caseinase, collagenase, etc. Majority of
Yumi Kumagai et al.
Infection and immunity, 73(5), 2655-2664 (2005-04-23)
Porphyromonas gingivalis is a pathogen associated with adult periodontitis. It produces dipeptidyl aminopeptidase IV (DPPIV), which may act as a virulence factor by contributing to the degradation of connective tissue. We investigated the molecular mechanism by which DPPIV contributes to
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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