antibody

Anti-Collagen I alpha1 Propeptide Sequence

MBS502155

0.1 mL

345 USD

polyclonal

rabbit

nonconjugated

human, mouse

western blot, immunohistochemistry

Antibody

Anti-Collagen I alpha1 Propeptide Sequence

Collagen 1, alpha 1 propeptide

collagen alpha-1(I) chain preproprotein; Collagen alpha-1(I) chain; collagen alpha-1(I) chain; collagen alpha-1(I) chain; alpha-1 type I collagen; pro-alpha-1 collagen type 1; collagen alpha 1 chain type I; collagen alpha-1(I) chain preproprotein; collagen of skin, tendon and bone, alpha-1 chain; collagen, type I, alpha 1; Alpha-1 type I collagen

COL1A1

COL1A1; COL1A1; OI4

CO1A1_HUMAN

Polyclonal

Rabbit

Human, mouse

1464

Specific for the propeptide portion of the ~180 kDa collagen I alpha1 polypeptide in human lung fibroblast extract. The antibody also works well for immunohistochemistry on paraformaldehyde-fixed sections with a simple antigen-retrieval protocol (incubate slides for 20 minutes at 90 degree 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, the antibody recognizes collagen I molecules that are still associated with the cells in which they were synthesized.

Affinity Purified

100 ul in PBS. Adequate amount of material to conduct 10-mini Western Blots.

Store at -20 degree C; stable for at least one year.

Western Blot (WB), Immunohistochemistry (IHC)

Quality Control: Western blots performed on each lot. WB: 1:1000. IHC: 1:100

Antigen: Synthetic peptide taken from the C-terminal region of human collagen I alpha1 propeptide sequence. Immunogen Information: Synthetic peptide corresponding to amino acid residues specific to the collagen 1, alpha 1 propeptide conjugated to KLH. Immunogen Species: Human

Reactivity Assumed Based on 100% Sequence Homology: Most mammals, birds, amphibians and fishes. Species Reactivity Note: The antibody has been directly tested for reactivity in human, mouse and rat. Based on the homology of the antigen this antibody is expected to recognize the collagen I alpha1 polypeptide in most, if not all, species of mammals, birds, amphibians, and fishes. Biological Significance: 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).

Rabbit polyclonal antibody

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.

110349772

NP_000079.2

NM_000088.3

P02452

180

Amoebiasis Pathway (167324); Amoebiasis Pathway (167191); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (730306); Binding And Uptake Of Ligands By Scavenger Receptors Pathway (771599); Collagen Biosynthesis And Modifying Enzymes Pathway (645289); Collagen Formation Pathway (645288); ECM-receptor Interaction Pathway (83068); ECM-receptor Interaction Pathway (479); Extracellular Matrix Organization Pathway (576262); Focal Adhesion Pathway (198795)

This gene encodes the pro-alpha1 chains of type I collagen whose triple helix comprises two alpha1 chains and one alpha2 chain. Type I is a fibril-forming collagen found in most connective tissues and is abundant in bone, cornea, dermis and tendon. Mutations in this gene are associated with osteogenesis imperfecta types I-IV, Ehlers-Danlos syndrome type VIIA, Ehlers-Danlos syndrome Classical type, Caffey Disease and idiopathic osteoporosis. Reciprocal translocations between chromosomes 17 and 22, where this gene and the gene for platelet-derived growth factor beta are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans, resulting from unregulated expression of the growth factor. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008]

Function: Type I collagen is a member of group I collagen (fibrillar forming collagen). Subunit structure: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 . By similarity. Interacts with TRAM2. Ref.33. Subcellular location: Secreted extracellular space extracellular matrix . By similarity. Tissue specificity: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. Domain: The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function . By similarity. Post-translational modification: Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. Involvement in disease: Caffey disease (CAFFD) [MIM:114000]: Characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.89 Ref.90 Ref.91Ehlers-Danlos syndrome 1 (EDS1) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.88 Ref.89 Ref.90 Ref.97Ehlers-Danlos syndrome 7A (EDS7A) [MIM:130060]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.89 Ref.90Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.44 Ref.55 Ref.59 Ref.62 Ref.68 Ref.89 Ref.90 Ref.93 Ref.94 Ref.96 Ref.99 Ref.101Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.25 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.56 Ref.60 Ref.61 Ref.63 Ref.64 Ref.67 Ref.69 Ref.70 Ref.71 Ref.73 Ref.74 Ref.76 Ref.79 Ref.83 Ref.85 Ref.89 Ref.90 Ref.94 Ref.95 Ref.101 Ref.102Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.42 Ref.44 Ref.52 Ref.57 Ref.65 Ref.70 Ref.71 Ref.75 Ref.78 Ref.80 Ref.82 Ref.87 Ref.89 Ref.90 Ref.92 Ref.101Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.53 Ref.57 Ref.66 Ref.70 Ref.72 Ref.77 Ref.84 Ref.89 Ref.90 Ref.92 Ref.94 Ref.99Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs.Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.81 Ref.86 Ref.89 Ref.90A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. Ref.89 Ref.90. Sequence similarities: Belongs to the fibrillar collagen family.Contains 1 fibrillar collagen NC1 domain.Contains 1 VWFC domain. Sequence caution: The sequence BAD92834.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

0.1 mL

345 USD