Collagen I Native Protein

Western Blot: Collagen I Native Protein [NBP1-97266] - Western blot of Human Collagen I. Lane 1: Human Collagen 1. Lane 2: None. Load: 50 ng per lane. Primary antibody: Collagen I antibody at 1:1,000 overnight at 4C. Secondary antibody: DyLight 649 rabbit secondary antibody at 1:20,000 for 30 min at RT. Block for 30 min at RT. Predicted/Observed molecular weight: 139 & 130 kDa, 139 & 130 kDa for Collagen I. Other Band(s): Collagen I splice variants and isoforms.

SDS-Page: Collagen I Native Protein [NBP1-97266] - SDS-PAGE Results of Human Collagen I. Lane 1: Human Collagen I Reduced (5.0ug). Lane 2: Opal Prestained Molecular Weight Marker. Lane 3: Human Collagen I Non-Reduced (5.0ug). 7.5% Gel, Coomassie Stained. Observed MW: Type I trimer, Type I dimer a1, a2, Type I monomer a1, a2.

• Reactivity: Hu
• Applications: WB, ELISA, IHC, PAGE

Collagen I Native Protein Summary

• Description: Native Human Collagen I (COL1A1 & COL1A2 subunits)
  
  Source: Human placenta (Accession #:P02452, P08123)
  
  Store vial at 4C prior to opening. This product is stable at 4C as an undiluted liquid. Dilute only prior to immediate use.
  
  No test method can provide total assurance that the hepatitis B virus, hepatitis C virus, human immunodeficiency virus, or any other infectious agents are absent. Thus, all blood products, including purified proteins derived from human blood sources, should be handled at Biosafety Level 2 as recommended by the CDC\NIH manual entitled Biosafety in Microbiological and Biomedical Laboratories for potentially infectious human serum, blood specimens or proteins derived from same. Source material for the human blood product supplied to your facility has been tested for the detection of HIV antibody, Hepatitis B surface antigen, antibody to Hepatitis C, HIV 1 antigen(s), antibody to HTLV - I/II, and syphilis by FDA guidelines. All units were found to be non-reactive/negative for these tests. All human blood source material is collected in FDA licensed centers and is tested with FDA approved test kits.
• Preparation Method: Prepared from human placenta and is chromatographically and immunologically pure. This product is free from other collagens, human serum proteins and non-collagen extracellular matrix proteins.
• Protein/Peptide Type: Native Protein
• Gene: COL1A1
• Purity: Multi-step

Applications/Dilutions

• Dilutions:
  • ELISA 1:10000
  • Immunohistochemistry 1:100-1:500
  • SDS-Page
  • Western Blot 1:1000
• Application Notes: This product has been tested in SDS-PAGE. This product is suitable for western blot, ELISA, and 2D culture. Collagen type I is recognized by type specific anti-collagen antibodies that recognize a native three-dimensional structure.

Packaging, Storage & Formulations

• Storage: Store at 4C. Do not freeze.
• Buffer: 0.5 M Acetic Acid
• Preservative: 0.01% Sodium Azide
• Purity: Multi-step

Alternate Names for Collagen I Native Protein

• Alpha-1 type I collagen
• alpha1(I) procollagen
• CAFYD
• COL1A1
• Collagen 1
• collagen alpha 1 chain type I
• collagen alpha-1(I) chain preproprotein
• collagen alpha-1(I) chain
• Collagen I
• collagen of skin, tendon and bone, alpha-1 chain
• collagen, type I, alpha 1
• EDSARTH1
• EDSC
• OI1
• OI2
• OI3
• OI4
• pro-alpha-1 collagen type 1
• type I proalpha 1
• Type I Procollagen Alpha 1 Chain

Background

Collagen I is one of the most abundant extracellular matrix (ECM) proteins in mammals and is an important structural component in connective tissues, bones, teeth, skin, heart, and lungs (1, 2). Collagen I is commonly used for biomedical purposes including providing an ECM microenvironment for cell attachment, proliferation, and mesenchymal stem cell growth and differentiation to the osteogenic lineage (1, 3, 4). Furthermore, type I Collagen hydrogels are a promising scaffold for engineering tissues and tumors (4). Collagen type I can be extracted from numerous sources including mammals, most commonly bovine and porcine, fish, amphibians, and birds (1, 4). Structurally, Collagen I is a heterotrimer comprised of two alpha-1 chains and one alpha-2 chain that together forms a triple helix (1, 3, 5). Each alpha chain is primarily formed by glycine, proline, and hydroxyproline repeats with the alpha-1 chains having a theoretical molecular weight of 139 kDa and 129 kDa for the alpha-2 chain (3). The dimeric form of Collagen I has a theoretical molecular weight of ~270 kDa while the trimeric form is >400 kDa (3, 5).

A variety of disease pathologies have been associated with mutations in or disruptions in collagen type I. Osteogenesis imperfecta, also known as brittle bone disease, is caused by autosomal dominant mutations in Collagen type I encoding genes and characterized by fragile bones and skeletal deformities (6). Ehlers-Danlos syndromes (EDS) is another disorder that affects soft connective tissue and its various clinical subtypes are associated with different mutations in Collagen I (7).

Alternative names for Collagen I includes alpha-1 type I collagen, alpha1(I) procollagen, CAFYD, COL1A1, collagen alpha 1 chain type I, collagen alpha-1(I) chain, EDSARTH1, EDSC, OI1, OI2, OI3, OI4, pro-alpha-1 collagen type 1, type I proalpha 1, and type I procollagen alpha 1 chain.

References

1. Chowdhury, S. R., Mh Busra, M. F., Lokanathan, Y., Ng, M. H., Law, J. X., Cletus, U. C., & Binti Haji Idrus, R. (2018). Collagen Type I: A Versatile Biomaterial. Advances in experimental medicine and biology. https://doi.org/10.1007/978-981-13-0947-2_21

2. Kisling, A., Lust, R. M., & Katwa, L. C. (2019). What is the role of peptide fragments of collagen I and IV in health and disease?. Life sciences. https://doi.org/10.1016/j.lfs.2019.04.042

3. Kwon, D., Kang, G. S., Han, D. K., Park, K., Kim, J. H., & Lee, S. H. (2014). Establishment and characterization of human engineered cells stably expressing large extracellular matrix proteins. Archives of pharmacal research. https://doi.org/10.1007/s12272-013-0294-0

4. Antoine, E. E., Vlachos, P. P., & Rylander, M. N. (2014). Review of collagen I hydrogels for bioengineered tissue microenvironments: characterization of mechanics, structure, and transport. Tissue engineering. Part B, Reviews. https://doi.org/10.1089/ten.TEB.2014.0086

5. Leon-Lopez, A., Morales-Penaloza, A., Martinez-Juarez, V. M., Vargas-Torres, A., Zeugolis, D. I., & Aguirre-alvarez, G. (2019). Hydrolyzed Collagen-Sources and Applications. Molecules (Basel, Switzerland). https://doi.org/10.3390/molecules24224031

6. Marini, J. C., Forlino, A., Bachinger, H. P., Bishop, N. J., Byers, P. H., Paepe, A., Fassier, F., Fratzl-Zelman, N., Kozloff, K. M., Krakow, D., Montpetit, K., & Semler, O. (2017). Osteogenesis imperfecta. Nature reviews. Disease primers. https://doi.org/10.1038/nrdp.2017.52

7. Callewaert, B., Malfait, F., Loeys, B., & De Paepe, A. (2008). Ehlers-Danlos syndromes and Marfan syndrome. Best practice & research. Clinical rheumatology, 22(1), 165-189. https://doi.org/10.1016/j.berh.2007.12.005

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Publications for Collagen I Native Protein (NBP1-97266)(2)

Publications using NBP1-97266

• Iwai M, Tulafu M, Togo S et al. Cancer-associated fibroblast migration in non-small cell lung cancers is modulated by increased integrin ?11 expression Molecular Oncology 2021-05-01 [PMID: 33682233] (Immunohistochemistry, Human)
• Russo V, klein T, Lim DJ et al. Granzyme B is elevated in autoimmune blistering diseases and cleaves key anchoring proteins of the dermal-epidermal junction. Sci Rep. 2018-06-26 [PMID: 29946113] (IF/IHC, Human)

Bioinformatics

• Gene Symbol: COL1A1
• Uniprot:
  • P02452()
  • P02452()
  • P02452()
  • P02452()