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C7661

Sigma-Aldrich

Collagen from rat tail

Bornstein and Traub Type I, powder, BioReagent, suitable for cell culture

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CAS Number:
9007-34-5
EC Number:
232-697-4
MDL number:
MFCD00130825
NACRES:
NA.75

biological source

rat tail

product line

BioReagent

form

powder

mol wt

120—160 kDa

packaging

glass bottle of 5 mg

technique(s)

cell culture | mammalian: suitable

surface coverage

6‑10 μg/cm2

solubility

soluble (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.)

NCBI accession no.

NM_053304.1

UniProt accession no.

P02454

Binding Specificity

Peptide Source: Fibrinogen

Peptide Source: Laminin

storage temp.

2-8°C

Gene Information

rat ... Col1a1(29393)

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General description

All collagen molecules are composed of three polypeptide chains arranged in a triple helical conformation, with a primary structure that is mostly a repeating motif with glycine in every third position and proline or 4-hydroxyproline frequently preceding the glycine residue. Type I collagen differs from other collagens by its low lysine hydroxylation and low carbohydrate composition. Col1a1 (collagen, type I, α1) or collagen is a major structural human protein, which assembles in the form of fibrils. It is a very long, thin and the most abundant protein found in the human body. It is a supercoiled right-helix of three left-handed polypeptide chains. These chains are composed of ~1040 amino acids, which are essentially repeats of three amino acids -(Gly-X-Y)n. Gly is glycine and X and Y can be any amino acids, but in humans are usually proline and hydroxyproline, respectively.

Application

Collagen from rat tail is used for the following applications:

  • Immunohistochemistry
  • Cellular activity assays
  • Used in generation of dorsal root ganglion (DRG) explant cultures
  • Used as one of the components during the preparation of the functionalized surface (in NMR setup)
  • Used in cell culture (the glass coverslips were coated with nanowires at high concentrations mixed with collagen)
  • Used for biofunctionalization of the microchannels

Biochem/physiol Actions

Collagen is an essential ingredient of connective tissue. Studies in a Chinese family show that mutation in COL1A1 (collagenase type I) is linked with type I osteogenesis imperfecta. Collagen is linked with subchondral turnover of bone, and might have potential as marker to determine the state of joint space narrowing and osteophytes in osteoarthritis.Collagen from rat tail is intended to produce thin layer coatings on tissue culture plates to facilitate attachment of anchorage-dependent cells, recommended for use at 6-10 μg/cm2. It is NOT intended for production of 3-D gels. Type I collagen is often used in cell culture as an attachment substratum with myoblasts, spinal ganglia, hepatocytes, embryonic lung, heart explants, fibroblasts, endothelial cells, and islet cells have all been cultured successfully on films or gels of type I collagen. Collagen type I may also be used in research of Idiopathic pulmonary fibrosis (IPF), studies on the effect of ER stress IPF on lung fibroblasts. Collagen in acidic solution can produce three dimensional scaffolding with use in bioengineering and cell culture applications.

Preparation Note

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.

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.

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

Certificates of Analysis (COA)

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  1. How can I sterilize collagen solutions?

    We recommend transferring the collagen solution to a glass bottle with a screw cap and carefully layering chloroform at the bottom. The amount of chloroform to use should be ~10% of the volume of collagen solution. DO NOT SHAKE OR STIR. Allow to stand overnight at 2-8 °C. Aseptically remove the top layer containing the collagen solution to a new bottle. We do not recommend sterilizing the collagen solution by membrane filtration. We have found substantial protein loss by this method.

  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. How long can collagen coated plates be stored?

    We make no recommendations about storage of plates after coating.  Since several factors such as humidity may impact longevity of coated plates, customers should make their own determination as to whether plates can be stored and under which conditions.  We offer Sigma Screen collagen coated plates (Product No. S3315) that indicates the following: For optimal performance, the unopened product should be stored in a dry place at 2-8 °C. The product may be stored at room temperature for up to three months. The product should not be exposed to temperatures above 50 °C.

  6. 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.

  7. 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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    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.

  9. 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. 

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    Ask a Scientist here.

M A Fallah et al.
Biomicrofluidics, 7(4), 44124-44124 (2014-01-10)
The role of von Willebrand factor (VWF) as a shear stress activated platelet adhesive has been related to a coiled-elongated shape conformation. The forces dominating this transition have been suggested to be controlled by the proteins polymeric architecture. However, the
Shali Chen et al.
Investigative ophthalmology & visual science, 53(13), 8333-8343 (2012-11-15)
Diabetic retinopathy entails proliferation of vascular endothelial cells (ECs) and unregulated angiogenesis. We have previously shown that ECs increase the expression of an embryonic variant of fibronectin (FN), called extra domain-B FN (ED-B FN) in response to high glucose. We
H P Huinink et al.
Magnetic resonance in medicine, 59(6), 1282-1286 (2008-04-19)
A major application of molecular MR imaging is receptor mapping of cells lining blood vessels with targeted contrast agents. Since these agents accumulate at interfaces, knowledge of their influence on the relaxation process in this specific configuration is a prerequisite
K Makibayashi et al.
The American journal of pathology, 158(5), 1733-1741 (2001-05-05)
OCT (22-oxa-calcitriol), a vitamin D analog, has been reported to show strong inhibitory effects on mesangial cell proliferation in vitro. In the present study, we report a study of the effect of OCT on anti-thy-1 glomerulonephritis. Both OCT and 1,25(OH)(2)D(3)
Peggy Romero et al.
BioTechniques, 47(6 Suppl), iii-viii (2010-01-01)
Current methods to assess neurodegradation in dorsal root ganglion cultures as a model for neurodegenerative diseases are imprecise and time-consuming. Here we describe two new methods to quantify neuroprotection in these cultures. The neurite quality index (NQI) builds upon earlier
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