C9879

Sigma-Aldrich

Collagen from bovine achilles tendon

powder, suitable for substrate for collagenase

CAS Number:
EC Number:
MDL number:
NACRES:
NA.61

biological source

bovine Achilles tendon

Quality Level

form

powder

application(s)

ELISA: suitable
activity assay: suitable

suitability

suitable for substrate for collagenase

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... COL2A1(407142)

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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 terminology using the Bornstein and Traub designation originates from the reference; Bornstein, P. and Traub, W. The Proteins, (1979) 4, 411-605
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.

Application

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.
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.

Packaging

1, 5, 10, 25 g in poly bottle

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

  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.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  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.

  9. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

  10. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

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)
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...
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...
Extraction and partial characterization of collagen from different animal skins
Quereshi S, et al.
Recent Research in Science and Technology, 2(9) (2010)

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