The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Biological activitySuitable to serve as the substrates for matrix metalloproteinases.
ab123531 should be protected from exposure to light.Suitable to serve as the substrates for matrix metalloproteinases.
FAM (fluorescein derivative) labelled collagen IV results in almost total quenching of the conjugate's fluorescence. Protease-catalyzed hydrolysis relieves this quenching conjugate, yielding brightly green fluorescent dye-labeled peptides. The increase in fluorescence intensity is directly proportional to protease activity. Ab123531 is useful in the development of HTS assays for screening Gelatinase A (MMP-2) and Gelatinase A inhibitors, as well as other gelatinases and collagenases that degrade Collagen IV.
For proteolytic assays, dilute the stock solution in appropriate assay buffer, pH >7.0. Then incubate the FAM-collagen type IV with proteases at 37C for 16-24 hr. Centrifuge the sample at 10,000 x g for 10 min. The protease activity is demonstrated by the increase of fluorescence in the supernatant at Ex/Em=490 nm/520 nm.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C. Store under desiccating conditions.
Constituent: 0.19% Acetic acid
COL4A1 NC1 domain
collagen alpha-1(IV) chain
Collagen IV Alpha 1 Polypeptide
Collagen IV Alpha 2 Polypeptide
Collagen Of Basement Membrane Alpha 1 Chain
Collagen Of Basement Membrane Alpha 2 Chain
Collagen Type IV
Collagen Type IV Alpha 1
Collagen Type IV Alpha 2
Collagen Type IV Alpha 3
Collagen Type IV Alpha 4
Collagen Type IV Alpha 5
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.
Post-translational 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.