Anti-Collagen IV antibody [COL-94] (ab6311)
- Product nameAnti-Collagen IV antibody [COL-94]See all Collagen IV primary antibodies ...
- DescriptionMouse monoclonal [COL-94] to Collagen IV
- SpecificitySpecifically recognizes native, undenatured, human collagen type IV . Shows no cross reactivity with collagen types I, II, III, V, VI, VII, human vitronectin, fibronectin, or chondroitin sulfate A. B and C. No reactivity with denatured or denatured-reduced collagen in immunoblots.
- Tested applicationsWB, ELISA, IHC-FoFr, IHC-P, Dot Blot, ICC/IF, IHC-Fr more details
- Species reactivityReacts with: Human
Predicted to work with: Non Human Primates
Does not react withRat, Sheep, Goat, Chicken, Cat
Full length native protein (purified) (Human).
- EpitopeRecognises an epitope located on the alpha 1 and/or alpha 2 chains of human collage type IV.
- Positive controlHuman tissue.
- Storage instructionsStore at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: 15mM Sodium Azide
Constituents: Ascites fluid
- Concentration information loading...
- Clonality Monoclonal
- Clone numberCOL-94
- Research Areas
Our Abpromise guarantee covers the use of ab6311 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ELISA: Use at an assay dependent dilution.
IHC-P: 1/300 (PMID 18843029).
WB: Use at an assay dependent dilution.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
- FunctionType IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.
- Tissue specificityHighly expressed in placenta.
- Involvement in diseaseDefects in COL4A1 are a cause of brain small vessel disease with hemorrhage (BSVDH) [MIM:607595]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.
Defects in COL4A1 are the cause of hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]. The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.
Defects in COL4A1 are a cause of porencephaly familial (PCEPH) [MIM:175780]. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect or arrest in the development of the cerebral ventricles.
- Sequence similaritiesBelongs to the type IV collagen family.
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.
- DomainAlpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.
modificationsLysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.
Proteolytic processing produces the C-terminal NC1 peptide, arresten.
- Cellular localizationSecreted > extracellular space > extracellular matrix > basement membrane.
- Entrez Gene: 1284 Human
- Entrez Gene: 1285 Human
- Entrez Gene: 1287 Human
- Entrez Gene: 1286 Human
- Entrez Gene: 1282 Human
- Omim: 120130 Human
- Omim: 120090 Human
- Omim: 120070 Human
- Omim: 303630 Human
- Omim: 120131 Human
- SwissProt: P08572 Human
- SwissProt: Q01955 Human
- SwissProt: P29400 Human
- SwissProt: P53420 Human
- SwissProt: P02462 Human
- Unigene: 570065 Human
- Unigene: 591645 Human
- Unigene: 369089 Human
- Unigene: 17441 Human
- Arresten antibodyCanstatin antibodyCO4A1_HUMAN antibody
- COL4A1 antibodyCOL4A1 NC1 domain antibodyCOL4A2 antibodyCOL4A3 antibodyCOL4A4 antibodyCOL4A5 antibodyCollagen Alpha 1(IV) Chain antibodyCollagen Alpha 2(IV) Chain antibodycollagen alpha-1(IV) chain antibodyCollagen IV Alpha 1 Polypeptide antibodyCollagen IV Alpha 2 Polypeptide antibodyCollagen Of Basement Membrane Alpha 1 Chain antibodyCollagen Of Basement Membrane Alpha 2 Chain antibodyCollagen Type IV Alpha 1 antibodyCollagen Type IV Alpha 2 antibodyCollagen Type IV Alpha 3 antibodyCollagen Type IV Alpha 4 antibodyCollagen Type IV Alpha 5 antibodyDKFZp686I14213 antibodyFLJ22259 antibody
Anti-Collagen IV antibody [COL-94] images
Immunofluorescence analysis of Human endothelial cells, staining Collagen IV with ab6311.
Cells were fixed with formaldehyde and permeabilized with acetone. Samples were incubated with primary antibody (0.5 µg/ml in diluent) for 18 hours at 4°C. An AlexaFluor®488-conjugated goat anti-mouse polyclonal IgG (5 µg/ml) was used as the secondary antibody.
References for Anti-Collagen IV antibody [COL-94] (ab6311)
This product has been referenced in:
- Thomson SE et al. A novel primate model of delayed wound healing in diabetes: dysregulation of connective tissue growth factor. Diabetologia 53:572-83 (2010). IHC-P ; Baboon . Read more (PubMed: 20091023) »
- Nath AK et al. Proteomic-based detection of a protein cluster dysregulated during cardiovascular development identifies biomarkers of congenital heart defects. PLoS One 4:e4221 (2009). ICC/IF ; Human . Read more (PubMed: 19156209) »