Key features and details
- Biotin Rabbit polyclonal to Collagen I
- Suitable for: IHC-P, Flow Cyt (Intra)
- Reacts with: Human
- Conjugation: Biotin
- Isotype: IgG
Product nameBiotin Anti-Collagen I antibody
See all Collagen I primary antibodies
DescriptionBiotin Rabbit polyclonal to Collagen I
SpecificityNegligible cross-reactivity with Type II, III, IV, V or VI collagens. Non-specific cross reaction of anti-collagen antibodies with other human serum proteins or non-collagen extracellular matrix proteins is negligible.
Tested applicationsSuitable for: IHC-P, Flow Cyt (Intra)more details
Species reactivityReacts with: Human
Predicted to work with: Mammals
Full length native protein (purified) corresponding to Collagen I. Collagen Type I from human and bovine placenta.
- Flow Cyt (Intra): Primary adult human dermal fibroblast cells.
General notesAt least 11 genetically distinct gene products are collectively referred to as 'collagen types' or other proteins and proteoglycans of the extracellular matrix. In humans, collagens are composed of about 20 unique protein chains which under go various types of post-translational modifications and are ultimately assembled into a triple helix. This results in great diversity between collagen types. Collagens are highly conserved throughout evolution and are characterized by an uninterrupted "Glycine-X-Y" triplet repeat that is a necessary part of the triple helical structure. For these reasons it is often extremely difficult to generate antibodies with specificities to collagens. The development of type specific antibodies is dependent on NON-DENATURED three-dimensional epitopes. This preparation results in a native conformation of the protein.
This antibody is well suited to detect extracellular matrix proteins in normal as well as disease state tissues. Disruption of tissue organization is the hallmark of neoplasia. Malignant lesions can be distinguished from benign by examining the breakdown of basement membranes and loss of 3-dimensional architecture. Malignant cells are presumed to use matrix metalloproteases to degrade barriers created by the extracellular matrix which then allows metastasis to occur. Collagenases, stomelysins and gelatinases can collectively degrade all of the various components of the extracellular matrix, including fibrillar and non-fibrillar collagens and basement membrane glycoproteins.
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.01% Sodium azide
Constituents: 0.44% Sodium chloride, 1% BSA, 0.15% EDTA, 4.8% Sodium borate
Concentration information loading...
PurityImmunogen affinity purified
Purification notesImmunoaffinity chromatography using immobilized antigens followed by extensive cross-adsorption against other collagens, human serum proteins and non-collagen extracellular matrix proteins to remove any unwanted specificities.
Primary antibody notesThis antibody is well suited to detect extracellular matrix proteins in normal as well as disease state tissues. Disruption of tissue organization is the hallmark of neoplasia. Malignant lesions can be distinguished from benign by examining the breakdown of basement membranes and loss of 3-dimensional architecture. Malignant cells are presumed to use matrix metalloproteases to degrade barriers created by the extracellular matrix which then allows metastasis to occur. Collagenases, stomelysins and gelatinases can collectively degrade all of the various components of the extracellular matrix, including fibrillar and non-fibrillar collagens and basement membrane glycoproteins.
The Abpromise guarantee
Our Abpromise guarantee covers the use of ab6577 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/50 - 1/200.
|Flow Cyt (Intra)||
Use a concentration of 5 µg/ml.
1/50 - 1/200.
Flow Cyt (Intra)
Use a concentration of 5 µg/ml.
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 antibody
- Alpha 2 type I collagen antibody
- alpha 2 type I procollagen antibody
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human skin tissue sections at pH9 labeling Collagen I with ab6577 10 µg/mL for 1 h at RT. Secondary antibody: Peroxidase rabbit secondary antibody at 1/10,000 for 45 min at RT. Localization: Collagen Type I is secreted in the extracellular matrix. Staining: Collagen Type I as precipitated brown signal (A) with hematoxylin purple nuclear counterstain. With corresponding negative conrol (B).
Flow Cytometry analysis of primary adult human dermal fibroblast cells labeling Collagen I with ab6577 5µg/mL for 45 min at 4°C. Secondary antibody: Rabbit Streptavidin, R-PE antibody at 1/500 for 15 min at RT.
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human skin tissue sections at pH6 labeling Collagen I with ab6577 10 µg/mL for 1 h at RT. Secondary antibody: Peroxidase rabbit secondary antibody at 1/10,000 for 45 min at RT. Localization: Collagen Type I is secreted in the extracellular matrix. Staining: Collagen Type I as precipitated brown signal (A) with hematoxylin purple nuclear counterstain. With corresponding negative conrol (B).
ab6577 has been referenced in 9 publications.
- Weng Y et al. Effects of high glucose on proliferation and function of circulating fibrocytes: Involvement of CXCR4/SDF-1 axis. Int J Mol Med 44:927-938 (2019). PubMed: 31257476
- Zhu F et al. STAT3 Inhibition Partly Abolishes IL-33-Induced Bone Marrow-Derived Monocyte Phenotypic Transition into Fibroblast Precursor and Alleviates Experimental Renal Interstitial Fibrosis. J Immunol 203:2644-2654 (2019). PubMed: 31591147
- Kargar-Abarghouei E et al. Characterization, recellularization, and transplantation of rat decellularized testis scaffold with bone marrow-derived mesenchymal stem cells. Stem Cell Res Ther 9:324 (2018). PubMed: 30463594
- Hassanpour A et al. Decellularized human ovarian scaffold based on a sodium lauryl ester sulfate (SLES)-treated protocol, as a natural three-dimensional scaffold for construction of bioengineered ovaries. Stem Cell Res Ther 9:252 (2018). PubMed: 30257706
- Jarman ER et al. A translational preclinical model of interstitial pulmonary fibrosis and pulmonary hypertension: mechanistic pathways driving disease pathophysiology. Physiol Rep 2:N/A (2014). Flow Cyt ; Rat . PubMed: 25214520
- Gumucio JP et al. Targeted inhibition of TGF-ß results in an initial improvement but long-term deficit in force production after contraction-induced skeletal muscle injury. J Appl Physiol (1985) 115:539-45 (2013). PubMed: 23766498
- Wen L et al. Mild Electrical Pulse Current Stimulation Upregulates S100A4 and Promotes Cardiogenesis in MSC and Cardiac Myocytes Coculture Monolayer. Cell Biochem Biophys 65:43-55 (2013). PubMed: 22941361
- Maghsoudlou P et al. Preservation of micro-architecture and angiogenic potential in a pulmonary acellular matrix obtained using intermittent intra-tracheal flow of detergent enzymatic treatment. Biomaterials 34:6638-48 (2013). PubMed: 23727263
- Kordes C et al. Differential and synergistic effects of platelet-derived growth factor-BB and transforming growth factor-beta1 on activated pancreatic stellate cells. Pancreas 31:156-67 (2005). PubMed: 16025003