Key features and details
- Biotin Rabbit polyclonal to Collagen IV
- Suitable for: IHC-P
- Reacts with: Cow, Human
- Conjugation: Biotin
- Isotype: IgG
Product nameBiotin Anti-Collagen IV antibody
See all Collagen IV primary antibodies
DescriptionBiotin Rabbit polyclonal to Collagen IV
Specificitynegligible cross-reactivity with Type I, II, III, 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-Pmore details
Species reactivityReacts with: Cow, Human
Predicted to work with: Mammals
Collagen Type IV from human and bovine placenta
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.
These antibodies are 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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We are also updating the applications & species that this product has been “predicted to work with,” however this information is not covered by our Abpromise guarantee.
Applications & species from publications and Abreviews that have not been tested in our own labs or in those of our suppliers are not covered by the Abpromise guarantee.
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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, 4.77% Sodium borate, 0.146% EDTA
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 notesThese antibodies are 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.
Our Abpromise guarantee covers the use of ab6581 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||1/1000 - 1/5000.|
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.
- Information by UniProt
- Arresten antibody
- BSVD antibody
- CO4A1_HUMAN antibody
Immunohistochemical analysis of formalin-fixed paraffin-embedded human tissue sections, labelling Collagen IV with ab6581 at a concentration of 10 µg/mL for 1 hour at room temperature. The left panel is human kidney sections with the right panel being human liver sections. Antigen retrival was performed with 0.01 M sodium citrate buffer at pH 6.0 at 99°C for 20 mins. The secondary used was a rabbit peroxidase secondary antibody at a 1/10,000 dilution incubated for 45 mins at room temperature. Counterstaining against nuclear DNA was hematoxylin.
ab6581 has been referenced in 7 publications.
- 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
- Buno KP et al. In Vitro Multitissue Interface Model Supports Rapid Vasculogenesis and Mechanistic Study of Vascularization across Tissue Compartments. ACS Appl Mater Interfaces 8:21848-60 (2016). PubMed: 27136321
- Zhou J et al. Qianliening capsules influence the apoptosis of benign prostatic hyperplasia epithelial-1 cells by regulating the extracellular matrix. Mol Med Rep 11:3734-40 (2015). PubMed: 25592406
- Whittington CF et al. Collagen-polymer guidance of vessel network formation and stabilization by endothelial colony forming cells in vitro. Macromol Biosci 13:1135-49 (2013). IHC . PubMed: 23832790
- Vandenbroucke RE et al. Matrix metalloprotease 8-dependent extracellular matrix cleavage at the blood-CSF barrier contributes to lethality during systemic inflammatory diseases. J Neurosci 32:9805-16 (2012). IHC ; Mouse . PubMed: 22815495
- Thomas SN et al. Impaired humoral immunity and tolerance in K14-VEGFR-3-Ig mice that lack dermal lymphatic drainage. J Immunol 189:2181-90 (2012). PubMed: 22844119