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Collagen I, rat tail

Main structural protein in the extracellular matrix
 
ALX-522-435-0020 20 mg 88.00 USD
 
ALX-522-435-0100 100 mg 206.00 USD
Do you need bulk/larger quantities?
 
  • New formulation enhances gelling over a larger concentration range.

Product Details

Alternative Name:COL1
 
MW:235kDa, 215kDa, 130kDa, 115kDa
 
Source:Isolated from rat tail tendons.
 
Concentration:5mg/ml
 
Formulation:Sterile liquid. In 0.02N acetic acid.
 
Purity:≥90% (SDS-PAGE)
 
Endotoxin Content:<100 EU/mg purified protein (LAL test)
 
Appearance:Hazy viscous liquid.
 
Activity: Tested in cell proliferation assay – Increased attachment of cells on collagen coated coverslips.
 
Application Notes:Can be used for preparation of collagen gels, thin layer coating of surfaces (culture plates, slides, coverslips).
 
Shipping:Blue Ice Not Frozen
 
Short Term Storage:+4°C
 
Long Term Storage:+4°C
 
Handling:Keep sterile. Do not freeze.
 
Scientific Background:Collagen is the main component in connective tissue and helps to provide support for tissues. It is made up of several classes, with Type 1 collagen being the most common. Type 1 collagen has a herterotrimeric triple helical structure made up of two alpha-1(I) and one alpha-2(I) chains that form into elongated fibrils which are extremely strong. These fibrils can be found in skin, tendons, ligaments, and other connective tissues. Type 1 collagen has been shown to be useful as a substrate that promotes cell growth and proliferation. Under acidic conditions the protein is soluble, however by raising the temperature and pH the solution forms into a solid gel that can be useful for cellular studies. It can also be dried to form a thin layer on solid surfaces such as plates, slides, or coverslips to aid in cell attachment.
 
Protocol:Firm Gelling Procedure
(Note: The ideal concentration for gelling is 1 - 5mg/ml. The end user will need to determine the appropriate concentration for their specific purpose).


Ammonium Hydroxide Gas Method
  1. Dilute 5mg/ml collagen to the desired concentration using sterile conditions. (Note: Lower concentrations will have reduced rigidity).
  2. Add enough collagen to cover the surface.
  3. Saturate a cotton ball or piece of filter paper with concentrated ammonium hydroxide and make a closed vapor chamber.
  4. Heat to 37°C until gel forms.
  5. Remove the ammonium hydroxide.
  6. Soak the gel surface in PBS for 1 hour.
  7. Wash several times PBS.
  8. Store the gel in PBS at +4°C until use.
  9. Equilibrate the gel in the desired media for 30 minutes prior to use.

NaOH Method (For 10ml)
  1. Sterilely add 1- 7ml of 5mg/ml collagen to a tube depending on desired final concentration. (Note: Lower concentrations will have reduced rigidity).
  2. Add 1ml of sterile 10X PBS.
  3. Add 1 ml of sterile 1N NaOH.
  4. Bring final volume to 10ml with sterile dH2O
  5. Cover the desired surface with a layer of the collagen and place at 37°C until the gel has solidified. Gel will only form if the pH is ≥7.0.
  6. Store in PBS at +4°C until use.
  7. Equilibrate the gel in the desired media for 30 minutes prior to use.
 
Regulatory Status:RUO - Research Use Only
 
Collagen I, rat tail CHO
Glass coverslips were coated with or without collagen in 60% ethanol and allowed to dry overnight. CHO cells were plated at onto the coverslips and grown for two days at 37oC with 5% CO2. Cells were fixed in 10% buffered formalin. Coverslips were washed in PBS, mounted upside down onto microscope slides, and imaged with a 20X objective.
Collagen I, rat tail SDS-PAGE
Coomassie stained SDS-PAGE. Lane 1, Molecular weight marker. Lane 2, 1.0µg Collagen I, rat tail.
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Collagen I, rat tail CHO Collagen I, rat tail SDS-PAGE

Product Literature References

Modeling Gas Plasma-Tissue Interactions in 3D Collagen-Based Hydrogel Cancer Cell Cultures: L. Miebach, et al.; Bioengineering (Basel) 10, 367 (2023), Abstract;
A TNF receptor 2 agonist ameliorates neuropathology and improves cognition in an Alzheimer’s disease mouse model: N.O. Casan, et al.; PNAS 119, e2201137119 (2022), Abstract;
Axon guidance receptor ROBO3 modulates subtype identity and prognosis via AXL-associated inflammatory network in pancreatic cancer: N. Krebs, et al.; JCI Insight 7, e154475 (2022), Abstract;
Cooperative interaction between ERα and the EMT-inducer ZEB1 reprograms breast cancer cells for bone metastasis: N.M. Ghahhari, et al.; Nat. Commun. 13, 2104 (2022), Abstract;
Efficacy of probiotic Streptococcus thermophilus in counteracting TGF-β1-induced fibrotic response in normal human dermal fibroblasts: F. Lombardi, et al.; J. Inflamm. 19, 27 (2022), Abstract;
SIRT1-mediated deacetylation of FOXO3a transcription factor supports pro-angiogenic activity of interferon-deficient tumor-associated neutrophils: S. Bordbari, et al.; Int. J. Cancer 150, 1198 (2022), Abstract;
Integrin β3 targeting biomaterial preferentially promotes secretion of bFGF and viability of iPSC-derived vascular smooth muscle cells: B. C. Dash, et al.; Biomater. Sci. 9, 5319 (2021), Abstract;
Low nanogel stiffness favors nanogel transcytosis across an in vitro blood-brain barrier: L. Ribovski, et al.; Nanomedicine 34, 102377 (2021), Abstract;
Low nanogel stiffness favors nanogel transcytosis across an in vitro blood–brain barrier: L. Ribovski, et al.; Nanomedicine 34, 102377 (2021), Abstract;
A new perfusion culture method with a self-organized capillary network: K. Sugihara, et al.; PLoS One 15, e0240552 (2020), Abstract; Full Text
Induced pluripotent stem cell-derived smooth muscle cells increase angiogenesis and accelerate diabetic wound healing: J. Gorecka, et al.; Regen. Med. 15, 1277 (2020), Abstract; Full Text
A filter-free blood-brain barrier model to quantitatively study transendothelial delivery of nanoparticles by fluorescence spectroscopy: E. De Jong, et al.; J. Control. Release 289, 14 (2018), Abstract;
Effects of selexipag and its active metabolite in contrasting the profibrotic myofibroblast activity in cultured scleroderma skin fibroblasts: M. Cutolo, et al.; Arthritis Res. Ther. 20, 77 (2018), Abstract; Full Text

General Literature References

Reconstituted rat-tail collagen used as substrate for tissue cultures on coverslips in maximow slides and roller tube: M.B. Bornstein, et al.; Lab. Invest. 134, (1958),

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