Key features and details
- Expression system: Native
- Purity: > 95% n/a
- Suitable for: WB, IP, ELISA, IHC-P
Product nameNative Human Collagen VI protein
See all Collagen VI proteins and peptides
Purity> 95 % n/a.
This product has been prepared from human placenta and is chromatographically and immunologically pure.
Protein lengthFull length protein
Additional sequence informationPrepared from Human Placenta.
Our Abpromise guarantee covers the use of ab7538 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)
This product is free from other collagens, human serum proteins and non-collagen extracellular matrix proteins. This product reacts with anti-Collagen Type VI. Reaction with anti-Collagen I, II, III, IV or V is negligible (typically less than 1% cross reactivity was detected by ELISA).
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C. Diluted stock solutions should be used immediately and not be frozen. Please see notes section. Store undiluted.
Preservative: 0.01% Sodium azide
Constituent: 3% Acetic acid
- Alpha 1 (VI) chain (61 AA)
FunctionCollagen VI acts as a cell-binding protein.
Involvement in diseaseDefects in COL6A1 are a cause of Bethlem myopathy (BM) [MIM:158810]. BM is a rare autosomal dominant proximal myopathy characterized by early childhood onset (complete penetrance by the age of 5) and joint contractures most frequently affecting the elbows and ankles.
Defects in COL6A1 are a cause of Ullrich congenital muscular dystrophy (UCMD) [MIM:254090]; also known as Ullrich scleroatonic muscular dystrophy. UCMD is an autosomal recessive congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.
Sequence similaritiesBelongs to the type VI collagen family.
Contains 3 VWFA domains.
modificationsProlines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Cellular localizationSecreted > extracellular space > extracellular matrix.
- Information by UniProt
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.
ab7538 has been referenced in 4 publications.
- Holm Nielsen S et al. A Fragment of Collagen Type VI alpha-3 chain is Elevated in Serum from Patients with Gastrointestinal Disorders. Sci Rep 10:5910 (2020). PubMed: 32245981
- Wishart AL et al. Decellularized extracellular matrix scaffolds identify full-length collagen VI as a driver of breast cancer cell invasion in obesity and metastasis. Sci Adv 6:N/A (2020). PubMed: 33087348
- Spiers RM et al. Donor age significantly influences the Raman spectroscopic biomolecular fingerprint of human pancreatic extracellular matrix proteins following collagenase-based digestion. Acta Biomater 99:269-283 (2019). PubMed: 31525537
- Veidal SS et al. MMP Mediated Degradation of Type VI Collagen Is Highly Associated with Liver Fibrosis - Identification and Validation of a Novel Biochemical Marker Assay. PLoS One 6:e24753 (2011). PubMed: 21935455