Recombinant Rabbit monoclonal primary
COL1A1/Collagen Ⅰ Recombinant Rabbit Monoclonal Antibody [ST58-04] (ET1609-68)
Human placenta tissue lysates, human kidney tissue, human uterus tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Alpha 1 type I collagen antibody; Alpha 2 type I collagen antibody; alpha 2 type I procollagen antibody; alpha 2(I) procollagen antibody; alpha 2(I)-collagen antibody; Alpha-1 type I collagen antibody; alpha1(I) procollagen antibody; CO1A1_HUMAN antibody; COL1A1 antibody; COL1A2 antibody; collagen alpha 1 chain type I antibody; Collagen alpha-1(I) chain antibody; collagen alpha-1(I) chain preproprotein antibody; Collagen I alpha 1 polypeptide antibody; Collagen I alpha 2 polypeptide antibody; collagen of skin, tendon and bone, alpha-1 chain antibody; collagen of skin, tendon and bone, alpha-2 chain antibody; Collagen type I alpha 1 antibody; Collagen type I alpha 2 antibody; EDSC antibody; OI1 antibody; OI2 antibody; OI3 antibody; OI4 antibody; pro-alpha-1 collagen type 1 antibody; type I proalpha 1 antibody; type I procollagen alpha 1 chain antibody; Type I procollagen antibody
Belongs to the fibrillar collagen family.
Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
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.
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. 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.