Overview
- Product nameAnti-Collagen I antibodySee all Collagen I primary antibodies ...
- DescriptionRabbit polyclonal to Collagen I
- SpecificityThis antibody is specific to Mouse Collagen Type I (100%) by RIA, and typically showed less than 1% reactivity against other types of mouse collagen types (II, III and IV).
- Tested applicationsIHC-Fr, RIA, ELISA, WB, IHC-P more details
- Species reactivityReacts with: Mouse
Does not react with
Rat, Chicken, Human - Immunogen
Collagen type I extracted and purified from mouse skin.
- Positive controlFrozen mouse liver for IF.
Properties
- FormLiquid
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
-
Concentration information loading... - Purification notesPurified by Ion exchange chromatography (DEAE-Trisacryl).
- Clonality Polyclonal
- IsotypeIgG
- Research Areas
Applications
Our Abpromise guarantee covers the use of ab21286 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Notes |
|---|---|
| IHC-Fr | IHC-Fr: 1/40. Tested using a FITC-labeled anti-rabbit IgG secondary. |
| RIA | RIA: 1/200. |
| ELISA | ELISA: Use at an assay dependent dilution. |
| WB | WB: Use at an assay dependent dilution. |
| IHC-P | IHC-P: 1/250. Tested using an HRP-labeled anti-rabbit IgG secondary. |
Target
- 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. - Post-translational
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.
-
Database links
- Entrez Gene: 12843 Mouse
- Entrez Gene: 12842 Mouse
- SwissProt: Q01149 Mouse
- SwissProt: P11087 Mouse
- Unigene: 277735 Mouse
- Unigene: 458212 Mouse
Target information above from: UniProt accession
P02452
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010)
.
-
Alternative names
- Alpha 1 type I collagen antibodyAlpha 2 type I collagen antibodyAlpha-1 type I collagen antibody
- CO1A1_HUMAN antibodyCOL1A1 antibodyCOL1A2 antibodyCollagen alpha-1(I) chain antibodyCollagen I alpha 1 polypeptide antibodyCollagen I alpha 2 polypeptide antibodyCollagen Of Skin Tendon And Bone antibodyCollagen Type 1 antibodyCollagen type I alpha 1 antibodyCollagen type I alpha 2 antibodyOI4 antibodyOsteogenesis Imperfecta Type IV antibodyPro alpha 1(I) collagen antibodyType I procollagen antibody
see all
Anti-Collagen I antibody images
-
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Collagen I antibody (ab21286)This image is courtesy of an anonymous Abreviewab21286 at 1/200 staining mouse embryonic lung tissue by IHC-P. The tissue was paraformaldehyde fixed and blocked with serum. A heat mediated antigen retrieval step was performed and the tissue was then stained with the antibody for 15 hours. A biotinylated goat anti-rabbit IgG antibody was used as the secondary. -
Immunohistochemistry (Frozen sections) - Collagen I antibody (ab21286)This image is courtesy of an anonymous abreview.ab21286 at a 1/200 dilution staining Collagen I in mouse parietal tissue by Immunohistochemistry (PFA fixed, frozen sections), incubated for 16 hours at 4°C. Permeabilized with 0.1% Triton. Blocked using 20% serum for 1 hour at room temperature. Secondary used polyclonal donkey conjugated to Alexa Fluor 555 (green). -
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Collagen I antibody (ab21286)This image is courtesy of an anonymous Abreviewab21286 staining collagen 1 in Mouse small intestine tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed, paraffin-embedded sections). Tissue was fixed with paraformaldehyde and blocked with 10% serum for 20 minutes at 23°C; antigen retrieval was by heat mediation. Samples were incubated with primary antibody (1/250 in TBS (1% Tween) + 10% Goat Serum) for 24 hours at 4°C. An Alexa Fluor®488-conjugated Goat anti-rabbit IgG polyclonal was used as the secondary antibody. -
Western blot - Anti-Collagen I antibody (ab21286)Anti-Collagen I antibody (ab21286) at 1/250 dilution + Mouse tail tendon collagen at 4 µg
Secondary
goat anti-rabbit IgG-IRDye 800 conjugated at 1/2500 dilution
Performed under non-reducing conditions.
Observed band size : 115,120 kDa (why is the actual band size different from the predicted?)
Exposure time : 3 minutes
References for Anti-Collagen I antibody (ab21286)
This product has been referenced in:
- Haist V et al. Distinct spatio-temporal extracellular matrix accumulation within demyelinated spinal cord lesions in Theiler's murine encephalomyelitis. Brain Pathol 22:188-204 (2012). IHC-P ; Mouse . Read more (PubMed: 21767322) »
- Schwarz MA et al. Lung self-assembly is modulated by tissue surface tensions. Am J Respir Cell Mol Biol 44:682-91 (2011). Read more (PubMed: 20616358) »
