Rat collagen solution can be used as a coating for human cells, as indicated by various publications. The following publication in PubMed suggests that rat collagen can serve as a viable alternative to human collagen for various applications in cell culture and tissue engineering. https://pubmed.ncbi.nlm.nih.gov/18203067/
C3867
Rat Collagen Type I
from rat tail, liquid, 4 mg/mL, suitable for cell culture
Collagen, Type I solution from rat tail
Synonym(s):
Collagen from rat tail, Col1a1
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Product Name
Collagen, Type I solution from rat tail, BioReagent, suitable for cell culture, sterile-filtered
biological source
rat tail
Quality Level
description
Approx. 100mg/vial ((35 - 40 ml) )
sterility
sterile-filtered
product line
BioReagent
Assay
>95% (SDS-PAGE)
form
liquid
mol wt
apparent mol wt 115-130 kDa by SDS-PAGE (doublet)
apparent mol wt 215-235 kDa by SDS-PAGE (doublet)
packaging
pkg of 1 vial
concentration
>0.5 mg/mL Biuret
technique(s)
cell culture | mammalian: suitable
surface coverage
6‑10 μg/cm2
impurities
Mycoplasma Test by Barile, none detected
solubility
soluble, clear to hazy, colorless (solubilized in 0.02M acetic acid)
NCBI accession no.
UniProt accession no.
Binding Specificity
Peptide Source: Collagen
Peptide Source: Fibronectin
shipped in
wet ice
storage temp.
2-8°C
Gene Information
rat ... Col1a1(29393)
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1 of 4
This Item | C9791 | C6745 | C8919 |
|---|---|---|---|
| technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable |
| sterility sterile-filtered | sterility - | sterility sterile-filtered | sterility aseptically processed |
| biological source rat tail | biological source bovine (calf) skin | biological source human cell culture | biological source bovine (calf) skin |
| concentration >0.5 mg/mL Biuret | concentration - | concentration 0.3 mg/mL | concentration (0.1% solution in 0.1 M acetic acid) |
| assay >95% (SDS-PAGE) | assay - | assay - | assay - |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
General description
Collagen is an extracellular matrix protein comprising triple helical structure. The structure of collagen type I, in particular, is characterized by the presence of three identical α-chains in its homotrimetric form. Among these three α-chains, one exhibits slight sequence variation.[1] Type I collagen was first isolated from rat-tail tendon, has two main α chains (α and α ) and one β chain.[2]
Application
Collagen, Type I solution from rat tail has been used for coating culture plates and dishes for human hepatocyte HepG2 cell line[3] and podocytes.[4] It has also been used as a standard for total collagen content calibration curve generation for the quantification of liver extracellular matrix pre-gel.[5]
Used as a coating material to support adherent cells growth and differentiation.
Biochem/physiol Actions
Collagen protein 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.[6] It has low antigenicity and is compatible with human gingival fibroblasts and human oral keratinocytes.[2]
Features and Benefits
- Sourced from rat tail.
- Sterile-filtered to minimize contamination risks.
- Suitable for a wide range of cell culture applications.
- Provides optimal surface coverage (6-10 μg/cm2) for promoting cell adhesion and proliferation.
Preparation Note
Recommended for use as a cell culture substratum. May not be suitable for 3-D gel formation.
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%.
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%.
Other Notes
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.
When C3867 is first removed from the cooler it will appear gelled. When it is allowed to come fully to 37°C it will appear as a liquid.
related product
Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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)
Mechanisms of angiotensin II signaling on cytoskeleton of podocytes
Hsu HH, et al.
Journal of Molecular Medicine, 86(12), 1379-1394 (2008)
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)
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)
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)
Articles
Extracelulární matrix (ECM) je vylučována buňkami a obklopuje je v tkáních.
The extracellular matrix (ECM) is secreted by cells and surrounds them in tissues.
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Can rat collagen solution be used as coating for human cells or is it better to use human collagen solutions?
1 answer-
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Should I add collagen I to acetic acid to obtain 0.1% (w/v) collagen solution, or it's already added and I should only dilute it to working concentration which is 0.01?
1 answer-
Here are our preparation instructions:
This product is prepared from rat tail tendons by modification of a published procedure.
It is supplied as an aqueous solution in 20 mM acetic acid (~100 mg of protein per vial). Protein concentration was estimated by the biuret method.
The vial contains approximately 100 mg of protein. Volume per vial: 22–25 ml. The product ships on wet ice and storage at 2–8 °C is recommended. During shipment, or if the storage temperature for this product goes slightly below the recommended range, the product may acquire a gel-like appearance. Under such circumstances, it is possible to warm the product gently, to no more than 45 °C, in order to reconstitute the product fully, before use. Aliquots that have been diluted to a working concentration may be stored at 2–8 °C for up to 2 weeks. Do not freeze. Optimal conditions for attachment must be determined for each cell line and application.1. An appropriate volume of the collagen solution should be diluted to a working concentration of 0.01% using sterile, tissue culture grade water.
2. Coat dishes with 6-10 mg/cm2. Allow the protein to bind for several hours at room temperature or 37 °C, or overnight at 2–8 °C.
3. Remove excess fluid from the coated surface and allow it to dry overnight. If sterility has been compromised, the dried, coated surface can be sterilized easily by overnight exposure to UV light in a sterile tissue culture hood.
4. Rinse with sterile tissue culture grade water or a balanced salt solution before introducing cells and medium.Helpful?
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What will be the concentration of collagen? I am trying to download the CoA, but I am unable to download it.
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This product is prepared at a concentration of approximately 4 mg/mL. A package of 1 Vial will typically have a volume of approximately 35-40 mL. The exact concentration is lot specific and reported in the product Certificate of Analysis. Please see the link below to review a sample or lot specific Certificate:
https://www.sigmaaldrich.com/product/sigma/c3867#product-documentationHelpful?
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IVD conformity: Does this product have IVDD or IVDR conformity?
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This collagen is intended for research use only, and is not approved for IVD purposes.
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In what volume should I dilute this solution in order to make collagen-coated plates for tissue culture?
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The recommended surface coverage for this product is 6?10 μg/cm2. Collagen solutions may be diluted to a working concentration of 0.01%. A general collagen coating protocol is available at https://www.sigmaaldrich.com/technical-documents/technical-article/cell-culture-and-cell-culture-analysis/mammalian-cell-culture/collagen-product-protocols
The collagen concentration of this product is reported on a lot specific basis and will be required to prepare the working solution. See the link below to review a sample Certificate of analysis:
https://www.sigmaaldrich.com/certificates/sapfs/PROD/sap/certificate_pdfs/COFA/Q14/C3867-1VL0000255665.pdfHelpful?
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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 can I make a 3-D collagen gel?
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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.
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How does the storage temperature relate to shipping conditions?
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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.
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How are collagen solutions stored?
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Collagen solutions should be stored in the refrigerator at 2-8 °C for up to 1 year, unless it becomes contaminated.
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Why am I seeing some insolubles in my collagen solution?
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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.
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