Native Human Collagen III protein (ab7535)
Key features and details
- Expression system: Native
- Suitable for: SDS-PAGE, IP, ELISA
Description
-
Product name
Native Human Collagen III protein
See all Collagen III proteins and peptides -
Expression system
Native -
Protein length
Full length protein -
Animal free
No -
Nature
Native -
-
Species
Human
-
Associated products
-
Positive Controls
Specifications
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.
-
Applications
SDS-PAGE
Immunoprecipitation
ELISA
-
Form
Liquid -
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
General Info
-
Alternative names
- Alpha 1 type III collagen
- Alpha1 (III) collagen
- CO3A1_HUMAN
see all -
Function
Collagen type III occurs in most soft connective tissues along with type I collagen. -
Involvement in disease
Defects 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 similarities
Belongs to the fibrillar collagen family.
Contains 1 fibrillar collagen NC1 domain.
Contains 1 VWFC domain. -
Post-translational
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 localization
Secreted > extracellular space > extracellular matrix. - Information by UniProt
Images
-
Western blot - Native Human Collagen III protein (ab7535)Image courtesy of Michaela Leyh by Abreview.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
Secondary
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 - Native Human Collagen III protein (ab7535)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.
Protocols
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.
Datasheets and documents
-
SDS download
-
Datasheet download
References (5)
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