antibody

Collagen Type I antibody

MBS534330

0.5 mL

650 USD

polyclonal

rabbit

nonconjugated

human, mouse, rat

western blot, immunocytochemistry, immunoprecipitation

Antibody

Collagen Type I antibody

Collagen Type I

Polyclonal Collagen Type I; Anti-Collagen Type I; Collagen type I alpha 1; OI4; Collagen Of Skin Tendon And Bone; Osteogenesis Imperfecta Type IV; Collagen type I alpha 2; Collagen Type 1

collagen, type I, alpha 1, isoform CRA_a; Collagen alpha-1(I) chain; collagen alpha-1(I) chain; collagen, type I, alpha 1; Alpha-1 type I collagen

COL1A1; COL1A1; OI1; OI2; OI3; OI4; EDSC

CO1A1_HUMAN

Polyclonal

Rabbit

Human, Mouse, Rat

885

Supplied as a liquid, no Preservatives, undiluted serum.

Aliquot and store at -70 degree C or lower. Avoid repeated freeze/thaw cycles

Immunofluorescence (IF), Immunoprecipitation (IP), Western Blot (WB)

Biological Significance: Type-I collagen is the most abundant collagen of the human body. It is present in scar tissue, the end product when tissue heals by repair. It is also found in tendons, the endomysium of myofibrils and the organic part of bone.

Immunogen: Collagen type I antibody was raised in rabbit using type I collagen purified from fetal mouse skin as the immunogen.

Cancer

Rabbit polyclonal Collagen Type I antibody

Antibodies and immunohistochemistry in extracellular matrix research; Anthony J. Hayes,, Clare E. Hughes, Bruce Caterson (Methods: Volume: 45 Issue: 1 Page: 10-21 DOI: 10.1016/j.ymeth.2008.01.011)

119615037

EAW94631.1

P02452

138,941 Da

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]

COL1A1: Type I collagen is a member of group I collagen (fibrillar forming collagen). Defects in COL1A1 are the cause of Caffey disease (CAFFD); also known as infantile cortical hyperostosis. Caffey disease is 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. Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1); also known as Ehlers-Danlos syndrome gravis. EDS is 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. Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A); also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1). A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2); also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3). A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4); also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP); also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture. A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. Belongs to the fibrillar collagen family. Protein type: Extracellular matrix; Secreted, signal peptide; Secreted. Chromosomal Location of Human Ortholog: 17q21.33. Cellular Component: Golgi apparatus; extracellular matrix; extracellular space; endoplasmic reticulum lumen; extracellular region; collagen type I; secretory granule. Molecular Function: identical protein binding; protein binding; extracellular matrix structural constituent; metal ion binding; platelet-derived growth factor binding. Biological Process: response to peptide hormone stimulus; extracellular matrix organization and biogenesis; intramembranous ossification; response to cAMP; collagen fibril organization; embryonic skeletal development; positive regulation of transcription, DNA-dependent; response to estradiol stimulus; response to corticosteroid stimulus; extracellular matrix disassembly; protein transport; sensory perception of sound; visual perception; skeletal development; collagen biosynthetic process; endochondral ossification; response to drug; blood vessel development; receptor-mediated endocytosis; platelet activation; skin morphogenesis; osteoblast differentiation; collagen catabolic process; response to hyperoxia; response to hydrogen peroxide; blood coagulation; leukocyte migration; positive regulation of cell migration. Disease: Osteogenesis Imperfecta, Type I; Ehlers-danlos Syndrome, Type Vii, Autosomal Dominant; Osteogenesis Imperfecta, Type Ii; Ehlers-danlos Syndrome, Type I; Osteogenesis Imperfecta, Type Iii; Osteoporosis; Caffey Disease; Osteogenesis Imperfecta, Type Iv

0.5 mL

650 USD