|Application ||WB, IHC|
|Calculated MW||180 KDa|
|Other Names||Collagen alpha-1(I) chain, Alpha-1 type I collagen, COL1A1|
|Target/Specificity||Synthetic peptide corresponding to amino acid residues specific to the collagen 1, alpha 1 propeptide conjugated to KLH.|
|Dilution||WB~~ 1:1000 |
|Antibody Specificity||Specific for the propeptide portion of the ~180 kDa collagen I α1polypeptide in human lung fibroblast extract. The antibody also works well forimmunohistochemistry on paraformaldehyde-fixed sections with a simple antigen-retrievalprotocol (incubate slides for 20 minutes at 90º C in 10 mM sodium citrate (pH 6.0)/ 0.1 %Tween-20). Note that in paraffin sections of formaldehyde-fixed fibrotic mouse lung tissue, theantibody recognizes collagen I molecules that are still associated with the cells in which theywere synthesized.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Collagen I α1 Propeptide Sequence Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
Collagen is an extracellular matrix protein that serves as a scaffold defining the shape and mechanical properties of many tissues and organs including skin, tendon, artery walls, fibrocartilage, bone and teeth. Type 1 collagen is the must abundant protein in mammals. Collagens are synthesized with N-terminal and C-terminal propeptides that are cleaved during maturation and secretion. After cleavage of the propeptides, the most N-terminal and C-terminal remaining sequences are known as telopeptides. Mutations in the collagen 1, alpha 1 gene (COL1A1) are known to cause osteogenesis imperfecta (aka brittle bone disease) (Byers 1989). Furthermore, mutations found in the fist 90 residues of the helical region of alpha 1 collagen have been implicated in the prevention or delayed removal of the procollagen N-propeptide leading to a combined osteogenesis imperfecta and Ehlers-Danlos syndrome (EDS) phenotype (Cabral et al., 2005).
Byers PH (1989) Inherited disorders of collagen gene structure and expression. Am J Med
Cabral WA, Makareeva E, Colige A, Letocha AD, Ty JM, Yeowell HN, Pals G, Leikin S, Marini
JC. (2005) Mutations near amino end of alpha1(I) collagen cause combined osteogenesis
imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing. J Biol Chem.
2005 May 13;280(19):19259-69.
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