Key features and details
- Sensitivity: 0.938 ng/ml
- Range: 1.563 ng/ml - 100 ng/ml
- Sample type: Other biological fluids, Plasma, Serum, Tissue Homogenate
- Detection method: Colorimetric
- Assay type: Sandwich (quantitative)
- Reacts with: Rat
Product nameRat Collagen Type I ELISA Kit
See all Collagen I kits
Intra-assay Sample n Mean SD CV% Overall < 8% Inter-assay Sample n Mean SD CV% Overall < 10%
Sample typeSerum, Plasma, Other biological fluids, Tissue Homogenate
Assay typeSandwich (quantitative)
Sensitivity< 0.938 ng/ml
Range1.563 ng/ml - 100 ng/ml
Assay durationMultiple steps standard assay
Species reactivityReacts with: Rat
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagens are fibrous, extracellular matrix proteins with high tensile strength and are the major components of connective tissue, such as tendons and cartilage. All collagens contain a triple helix domain and frequently show lateral self-association in order to form complex connective tissues. Several collagens also play a role in cell adhesion, important for maintaining normal tissue architecture and function. The extensive family of COL gene products (collagens) is composed of several chain types, including fibril-forming interstitial collagens (types I, II, III and V) and basement membrane collagens (type IV), each type containing multiple isoforms.
This COL1 ELISA kit (ab285314, E4619) is a sandwich ELISA assay for the quantitative measurement of COL1 in rat serum, plasma and cell culture supernatants. The density of color is proportional to the amount of COL1 captured from the samples
PlatformMicroplate (12 x 8 well strips)
Storage instructionsStore at +4°C. Please refer to protocols.
Components 96 tests 25X Wash buffer 1 x 30ml Antibody dilution buffer 1 x 10ml Biotin/Detection antibody (Concentrated) 1 x 120µl HRP-Streptavidin Conjugate (SABC) 1 x 120µl Lyophilized Standard 2 vials Micro ELISA Plate 1 unit Plate Sealer 5 units SABC dilution buffer 1 x 10ml Sample / Standard Dilution Buffer 1 x 20ml Stop Solution 1 x 10ml TMB Substrate 1 x 10ml
FunctionType I collagen is a member of group I collagen (fibrillar forming collagen).
Tissue specificityForms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
Involvement in diseaseDefects in COL1A1 are the cause of Caffey disease (CAFFD) [MIM:114000]; 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) [MIM:130000]; 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) [MIM:130060]; 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) [MIM:166200]. 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 2A (OI2A) [MIM:166210]; 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) [MIM:259420]. 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) [MIM:166220]; 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) [MIM:166710]; 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.
Note=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.
Sequence similaritiesBelongs to the fibrillar collagen family.
Contains 1 fibrillar collagen NC1 domain.
Contains 1 VWFC domain.
modificationsProline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-X-Y) 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.
Cellular localizationSecreted > extracellular space > extracellular matrix.
- Information by UniProt
- Alpha 1 type I collagen
- Alpha 2 type I collagen
- alpha 2 type I procollagen
ab285314 has not yet been referenced specifically in any publications.