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Collagen, Type I solution from rat tail

BioReagent, suitable for cell culture, sterile-filtered

Collagen from rat tail
Número CAS:
Número EC:
Número MDL:

Nível de qualidade


fonte biológica

rat tail


Approx. 100mg/vial (Volume 22 - 25ml/vial, see label for lot-specific protein concentration)



linha de produto



>95% (SDS-PAGE)



peso molecular

apparent mol wt 115-130 kDa by SDS-PAGE (doublet)
apparent mol wt 215-235 kDa by SDS-PAGE (doublet)


pkg of 1 vial


cell culture | mammalian: suitable

cobertura de superfície

6‑10 μg/cm2

nº de adesão UniProt

enviado em

wet ice

temperatura de armazenamento


Gene Information

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Descrição geral

Collagen is an extracellular matrix protein comprising triple helical structure. Homotrimetric collagens have three identical α-chains. Type I collagen have one α-chain different in sequence among the three. Type I collagen was first isolated from rat-tail tendon, has two main α chains (α and α ) and one β chain.


Used as a coating material to support adherent cells growth and differentiation.
Collagen, Type I solution from rat tail has been used for coating culture plates and dishes for human hepatocyte HepG2 cell line and podocytes. It has also been used as a standard for total collagen content calibration curve generation for the quantification of liver extracellular matrix pre-gel.

Ações bioquímicas/fisiológicas

Collagen is essential for the mechanical integrity of tendons and bone. Rat tail tendon collagen is used in tissue engineering especially in the generation of 3-D scaffolds based gels. It has low antigenicity and is compatible with human gingival fibroblasts and human oral keratinocytes.

Nota de preparo

Sterile solution prepared from rat tail tendons by a modification of the published extraction method 1. It is supplied as an aqueous solution in 20mM acetic acid with a protein concentration as stated on the bottle. (approx.100mg protein per vial). Protein concentration was estimated by the Biuret method 2.
SDS polyacrylamide gel electrophoresis analysis shows the typical band pattern for Type I collagen, with a doublet at apparent molecular weights of 115 and 130kDa and another doublet at 215 and 235kDa. Based on this analysis, the purity of the collagen sample is >95%.
Recommended for use as a cell culture substratum. May not be suitable for 3-D gel formation.

Outras notas

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.

Código de classe de armazenamento

10 - Combustible liquids



Ponto de fulgor (ºF)

Not applicable

Ponto de fulgor (ºC)

Not applicable

Certificado de análise

Insira o número de lote para pesquisar o Certificado de análise (COA).

Certificado de origem

Insira o número de lote para pesquisar o Certificado de origem (COO).

  1. How does the storage temperature relate to shipping conditions?

    The storage conditions that a Sigma-Aldrich catalog and label recommend for products are deliberately conservative. For many products, long-term storage at low temperatures will increase the time during which they are expected to remain in specification and therefore are labeled accordingly. Where short-term storage, shipping time frame, or exposure to conditions other than those recommended for long-term storage will not affect product quality, Sigma-Aldrich will ship at ambient temperature. The products sensitive to short-term exposure to conditions other than their recommended long-term storage are shipped on wet or dry ice. Ambient temperature shipping helps to control shipping costs for our customers. At any time, our customers can request wet- or dry-ice shipment, but the special handling is at customer expense if our product history indicates that the product is stable for regular shipment. See Shipping and Storage for more information.

  2. How are collagen solutions stored?

    Collagen solutions should be stored in the refrigerator at 2-8 °C for up to 1 year, unless it becomes contaminated.

  3. Why am I seeing some insolubles in my collagen solution?

    The solubility specifications for this product is clear to hazy colorless solution with a few insolubles at 1 mg/ml in water with 2 μl acetic acid (or 0.1 N acetic acid). The insolubles can be removed by settling or centrifugation.

  4. How can I make a 3-D collagen gel?

    Not all lots of C7661 are suitable for 3D gels. Product No. C4243 has been use-tested in this application. If C4243 is not available, we recommend that customers screen lots of C7661 to try to make 3D gels. We have found that collagen that has been sterilized by gamma-irradiation or by chloroform cannot be used to make 3D collagen gels. The following protocol can be used to make collagen gels: Materials required:Collagen gel solution 1.5 - 3 mg/mL 10X tissue culture medium containing phenol red Sodium bicarbonate or HEPES buffer Procedure: 1.Measure out 800 μL of collagen solution. 2.Add 100 μL of 10X medium (buffered with 1X sodium bicarbonate or HEPES) 3.Adjust pH with 1 N sodium hydroxide, if required (100 μl or less) 4.Add 10X medium to bring volume to 1 ml 5.Mix contents well. Solution should maintain red color to indicate physiological pH6. Dispense into wells to a depth of 1-2 mm (approx. 15 μL/well) 7.Transfer to 37 °C for 20-40 minutes 8.Examine for gel formation The above volumes represent quantities for use in 24 well plates. Volumes can be adjusted to accommodate any culture vessel.

  5. 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.

  6. 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.

  7. 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.

  8. 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. 

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

    Ask a Scientist here.

Type I collagen extracted from rat-tail and bovine Achilles tendon for dental application: a comparative study
Techatanawat S, et al.
Asian Biomedicine : Research, Reviews and News, 5(6), 787-798 (2011)
Preparation of ready-to-use, storable and reconstituted type I collagen from rat tail tendon for tissue engineering applications
Rajan N, et al.
Nature Protocols, 1(6), 2753-2753 (2006)
Thermal helix-coil transition in UV irradiated collagen from rat tail tendon
Sionkowska A and Kaminska A
International Journal of Biological Macromolecules, 24(4), 337-340 (1999)
Mechanisms of angiotensin II signaling on cytoskeleton of podocytes
Hsu HH, et al.
Journal of Molecular Medicine, 86(12), 1379-1394 (2008)
Ectopic adenine nucleotide translocase activity controls extracellular ADP levels and regulates the F1-ATPase-mediated HDL endocytosis pathway on hepatocytes
Cardouat G, et al.
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1862(9), 832-841 (2017)


Attachment Factors for Three-dimensional Cell Culture

Attachment Factors for 3-Dimensional Cell Culture

What is the Extracellular Matrix?

The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues.

Extracellular Matrix Proteins and Tools for Cell Culture Optimization

Extracellular matrix proteins such as laminin, collagen, and fibronectin can be used as cell attachment substrates in cell culture.

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