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Collagen I α1 Propeptide Sequence Antibody
Rabbit polyclonal antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC |
|---|---|
| Primary Accession | P02452 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | polyclonal |
| Calculated MW | 180 KDa |
| Gene ID | 1277 |
|---|---|
| Gene Name | COL1A1 |
| 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 IHC~~ 1:100 |
| Format | Affinity purified |
| 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. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
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).
References
Byers PH (1989) Inherited disorders of collagen gene structure and expression. Am J Med
Genet. 34(1):72-80.
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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