Rabbit Polyclonal COL4A1 antibody - conjugated to Biotin. Suitable for IP, ELISA, WB, IHC-P and reacts with Human, Cow samples. Cited in 8 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human COL4A1.
Preservative: 0.01% Sodium azide
Constituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution
IP | ELISA | WB | IHC-P | |
---|---|---|---|---|
Human | Expected | Expected | Expected | Expected |
Cow | Expected | Expected | Expected | Predicted |
Mammals | Predicted | Predicted | Predicted | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human, Cow | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mammals | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human, Cow | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mammals | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info - | Notes Not recommended for use under denaturing conditions. |
Species Cow | Dilution info - | Notes Not recommended for use under denaturing conditions. |
Species | Dilution info | Notes |
---|---|---|
Species Mammals | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/1000 - 1/5000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mammals, Cow | Dilution info - | Notes - |
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Type 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.
Collagen alpha-1(IV) chain, COL4A1
Rabbit Polyclonal COL4A1 antibody - conjugated to Biotin. Suitable for IP, ELISA, WB, IHC-P and reacts with Human, Cow samples. Cited in 8 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human COL4A1.
Preservative: 0.01% Sodium azide
Constituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution
Anti-Collagen Type IV has been prepared by immunoaffinity 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. Some class-specific anti-collagens may be specific for three-dimensional epitopes which may result in diminished reactivity with denatured collagen or formalin-fixed, paraffin embedded tissues. This antibody reacts with most mammalian Type IV collagens and has negligible cross-reactivity with Type I, II, III, V and VI collagens. Non-specific cross-reaction of anti-collagen antibodies with other human serum proteins or non-collagen extracellular matrix proteins is negligible.
Anti-Collagen Type IV has been prepared by immunoaffinity 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.
At 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.
Collagen IV also known as COL4A1 or collagen type IV is a structural protein essential to the basement membrane in tissues. The molecular weight of collagen type 4 varies but it generally forms a high-molecular-weight complex. This protein expresses prominently in various tissues especially in the kidneys lens capsule of the eye and skin. Collagen IV comprises six different alpha chains where its distinctiveness lies in its non-fibrillar network-forming structure which serves as a supportive scaffold for tissues and contributes to tissue regeneration and cell adhesion.
The highly organized network of collagen type IV plays a supreme role in maintaining the integrity and functionality of the basement membrane. It exists predominantly as part of a supramolecular complex associating with laminin nidogen and perlecan forming a multifunctional platform. This platform facilitates cellular signaling tissue elasticity and filtration functions. The basement membrane's selective permeability heavily relies on this network structure to regulate the exchange of molecules between tissues like blood vessels and epithelial sheets.
Collagen IV contributes to several critical functions within the extracellular matrix organization and cell-matrix adhesion pathways. Specifically it interacts intimately with integrins and matrix metalloproteinases (MMPs) playing roles in angiogenesis and tissue repair. Additionally its interactions with other collagens and integrins within these pathways enhance cellular responses to mechanical stress and contribute to structural resilience in tissues.
Mutations or abnormalities in collagen IV are linked closely with hereditary conditions such as Alport syndrome and Goodpasture syndrome. These conditions often result in compromised structural integrity and function of the basement membrane particularly affecting the kidneys and lungs. Alterations in collagen IV can influence interactions with other proteins like collagen type IV-associated proteins altering normal physiological functions and leading to tissue dysfunction and disease manifestations.
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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.
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