COL1A1 / Collagen I Alpha 1 Antibody

LifeSpan BioSciences

COL1A1 / Collagen I Alpha 1 Antibody

23

After de-waxing the tissue slices they are treated with 0.2% hyaluronidase (app. 300 U/mg) in TBS 15 minutes at 37°C. Thereafter non-specific binding is blocked by blocking serum or 3% BSA in TBS. For peroxidase systems blocking with 1% peroxide solution in TBS for 30 minutes at RT is recommended. Type I Collagen usually exists as a heterotrimer formed by alpha 1(I) and alpha 2(I) chains and is found in bone, cornea, skin and tendon. In foetal tissues also homotrimers of alpha-1(I) are found, but they are not constituents of normal adult tissues. Collagens consist of a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule consists of a triple-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs. Bovine collagen type I 100%, bovine collagen II, IX, XI <0.1%, sheep collagen type I 50 % (IHC estimated), bovine fibronectin <0.1%, human collagen type I <2%; chicken collagen type I <0.1% (estimates except sheep collagen I from solid phase RIA at a 1:500 dilution ).. ELISA (1:400), IF (1:80), IHC-P (1:1000), RIA, WB After de-waxing the tissue slices they are treated with 0.2% hyaluronidase (app. 300 U/mg) in TBS 15 minutes at 37°C. Thereafter non-specific binding is blocked by blocking serum or 3% BSA in TBS. For peroxidase systems blocking with 1% peroxide solution in TBS for 30 minutes at RT is recommended. Type I Collagen usually exists as a heterotrimer formed by alpha 1(I) and alpha 2(I) chains and is found in bone, cornea, skin and tendon. In foetal tissues also homotrimers of alpha-1(I) are found, but they are not constituents of normal adult tissues. Collagens consist of a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule consists of a triple-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs. Bovine collagen type I 100%, bovine collagen II, IX, XI <0.1%, sheep collagen type I 50 % (IHC estimated), bovine fibronectin <0.1%, human collagen type I <2%; chicken collagen type I <0.1% (estimates except sheep collagen I from solid phase RIA at a 1:500 dilution ).

ImmunoFluorescence, Western Blot, ELISA, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin, RadioImmunoAssay

Research Use Only

Polyclonal

1 mg/ml

Unconjugated

...

COL1A1

collagen type I alpha 1 chain

alpha-1 type I collagen; alpha1(I) procollagen; CAFYD; collagen alpha 1 chain type I; collagen alpha-1(I) chain; collagen alpha-1(I) chain preproprotein; collagen of skin, tendon and bone, alpha-1 chain; collagen, type I, alpha 1; EDSARTH1; EDSC; OI1; OI2; OI3; OI4; pro-alpha-1 collagen type 1; type I proalpha 1; type I procollagen alpha 1 chain

Rabbit

Bovine, Human, Porcine, Sheep

-20°C

12352203