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Collagen I Antibody

Novus Biologicals, part of Bio-Techne | Catalog # NBP3-43313

Novus Biologicals, part of Bio-Techne
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NBP3-43313

Key Product Details

Species Reactivity

Human

Applications

Immunocytochemistry/ Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot

Label

Unconjugated

Antibody Source

Polyclonal Rabbit

Concentration

0.3 mg/ml

Product Specifications

Immunogen

Immunized with recombinant Human Collagen I (Uniprot#: P02452; Arg253~Ala471)

Clonality

Polyclonal

Host

Rabbit

Applications for Collagen I Antibody

Application
Recommended Usage

Immunocytochemistry/ Immunofluorescence

5-20 ug/mL

Immunohistochemistry

5-20 ug/mL

Western Blot

0.5-2ug/mL

Formulation, Preparation, and Storage

Purification

Antigen and protein A Affinity-purified

Formulation

0.01M PBS, pH7.4, 50% glycerol.

Preservative

0.05% Proclin 300

Concentration

0.3 mg/ml

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.

Background: Collagen I

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

Alternate Names

Alpha-1 type I collagen, alpha1(I) procollagen, CAFYD, COL1A1, Collagen 1, collagen alpha 1 chain type I, collagen alpha-1(I) chain, collagen alpha-1(I) chain preproprotein, 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

Gene Symbol

COL1A1

Additional Collagen I Products

Product Documents for Collagen I Antibody

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Product Specific Notices for Collagen I Antibody

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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