Key features and details
- Expression system: Native
- Suitable for: SDS-PAGE, IP, ELISA
Product nameNative Human Collagen III protein
See all Collagen III proteins and peptides
Protein lengthFull length protein
Our Abpromise guarantee covers the use of ab7535 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Constituent: 3% Acetic acid
- Alpha 1 type III collagen
- Alpha1 (III) collagen
FunctionCollagen type III occurs in most soft connective tissues along with type I collagen.
Involvement in diseaseDefects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.
Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:130050]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.
Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:100070]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.
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.
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
All lanes : Anti-Collagen III antibody [FH-7A] (ab6310) at 1/500 dilution
Lane 1 : plus ab7535 reduced and denatured
Lane 2 : plus ab7535 native
All lanes : Goat anti-mouse-HRP at 1/2000 dilution
The protein can be used reduced + denaturated (band size ~130 kDa) or native (two bands ~ 130kDa and ~300kDa) The native protein gives a brighter signal.PH of the protein lysate is low - a loading dye with bromphenolblue changes its colour. This does not effect the western blot.
SDS-PAGE analysis of ab7535.
Lane 1: ab7535 Reduced 1 µg.
Lane 2: Pre-stained Molecular Weight Marker.
Lane 3: ab7535 Non-Reduced 1 µg.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab7535 has been referenced in 5 publications.
- Di Francesco S et al. Red grape (Vitis vinifera L.) flavonoids down-regulate collagen type III expression after UV-A in primary human dermal blood endothelial cells. Exp Dermatol 27:973-980 (2018). PubMed: 29742305
- Wang Z et al. Extracellular matrix promotes proliferation, migration and adhesion of airway smooth muscle cells in a rat model of chronic obstructive pulmonary disease via upregulation of the PI3K/AKT signaling pathway. Mol Med Rep 18:3143-3152 (2018). PubMed: 30066869
- Kehlet SN et al. A fragment of SPARC reflecting increased collagen affinity shows pathological relevance in lung cancer - implications of a new collagen chaperone function of SPARC. Cancer Biol Ther 19:904-912 (2018). PubMed: 30067436
- Barbaglio A et al. Ultrastructural and biochemical characterization of mechanically adaptable collagenous structures in the edible sea urchin Paracentrotus lividus. Zoology (Jena) 118:147-60 (2015). PubMed: 25958104
- Syed F et al. Fibroblasts from the growing margin of keloid scars produce higher levels of collagen I and III compared with intralesional and extralesional sites: clinical implications for lesional site-directed therapy. Br J Dermatol 164:83-96 (2011). PubMed: 20849516