Mouse Anti-COL1A1 Recombinant Antibody (CBMAB-0606-LY)

Mouse

Sheep, Cattle, Dog, Chicken, Human, Mouse, Pig, Rabbit, Rat, Frog, Zebrafish

IgG1

ELISA, FFPE, IF, IHC, WB

Amino propeptide amino acids 1-9

Sheep, Cattle, Dog, Chicken, Human, Mouse, Pig, Rabbit, Rat, Frog, Zebrafish

IgG1

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Liquid

> 95% Purity determined by SDS-PAGE.

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Collagen Type I Alpha 1 Chain

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.

OI4

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Blood coagulation Source: Reactome
Blood vessel development Source: UniProtKB
Bone trabecula formation Source: Ensembl
Cartilage development involved in endochondral bone morphogenesis Source: Ensembl
Cellular response to amino acid stimulus Source: Ensembl
Cellular response to epidermal growth factor stimulus Source: Ensembl
Cellular response to fibroblast growth factor stimulus Source: Ensembl
Cellular response to fluoride Source: Ensembl
Cellular response to mechanical stimulus Source: Ensembl
Cellular response to retinoic acid Source: Ensembl
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Cellular response to tumor necrosis factor Source: Ensembl
Cellular response to vitamin E Source: Ensembl
Collagen-activated tyrosine kinase receptor signaling pathway Source: GO_Central
Collagen biosynthetic process Source: UniProtKB
Collagen fibril organization Source: UniProtKB
Embryonic skeletal system development Source: UniProtKB
Endochondral ossification Source: Ensembl
Extracellular matrix organization Source: GO_Central
Face morphogenesis Source: Ensembl
Intramembranous ossification Source: Ensembl
Leukocyte migration Source: Reactome
Negative regulation of cell-substrate adhesion Source: Ensembl
Ossification Source: GO_Central
Osteoblast differentiation Source: Ensembl
Platelet activation Source: Reactome
Positive regulation of canonical Wnt signaling pathway Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of epithelial to mesenchymal transition Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Protein localization to nucleus Source: UniProtKB
Protein transport Source: Ensembl
Regulation of immune response Source: Reactome
Response to cAMP Source: Ensembl
Response to corticosteroid Source: Ensembl
Response to drug Source: Ensembl
Response to estradiol Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to hyperoxia Source: Ensembl
Response to mechanical stimulus Source: GO_Central
Response to peptide hormone Source: Ensembl
Sensory perception of sound Source: UniProtKB
Skeletal system development Source: UniProtKB
Skin development Source: GO_Central
Skin morphogenesis Source: UniProtKB
Tooth eruption Source: Ensembl
Tooth mineralization Source: UniProtKB
Visual perception Source: UniProtKB

Extracellular matrix

Caffey disease (CAFYD):
An autosomal dominant disorder 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.
Ehlers-Danlos syndrome, classic type, 1 (EDSCL1):
A form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. The main features of classic Ehlers-Danlos syndrome are joint hypermobility and dislocation, and fragile, bruisable skin. EDSCL1 inheritance is autosomal dominant.
Ehlers-Danlos syndrome, arthrochalasia type, 1 (EDSARTH1):
A form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDSARTH1 is an autosomal dominant form characterized by frequent congenital hip dislocation and extreme joint laxity with recurrent joint subluxations and minimal skin involvement.
Osteogenesis imperfecta 1 (OI1):
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.
Osteogenesis imperfecta 2 (OI2):
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.
Osteogenesis imperfecta 3 (OI3):
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.
Osteogenesis imperfecta 4 (OI4):
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.
Osteoporosis (OSTEOP):
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.

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.