Product nameNative Human Collagen V protein
See all Collagen V proteins and peptides
Protein lengthFull length protein
Amino Acid Sequence
Molecular weight184 kDa
Additional sequence informationPrepared from Human Placenta and is chromatographically and immunologically pure.
Our Abpromise guarantee covers the use of ab7537 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Biological activityCollagen taken from human species.
This product is free from other collagens, human serum proteins and non-collagen extracellular matrix proteins. This product reacts with anti-Collagen Type V. Reaction with anti-Collagen I, II, III, IV or VI is negligible (typically less than 1% cross reactivity was detected by ELISA).
Collagen taken from human species.
Denaturing and reducing conditions will greatly diminish reactivity and selectivity of this protein.
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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.
Preservative: 0.01% Sodium azide
Constituent: 0.06% Acetic acid
- AB collagen
- Alpha 1 type V collagen
- Alpha 2 type V collagen
FunctionType V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
Involvement in diseaseEhlers-Danlos syndrome 1
Ehlers-Danlos syndrome 2
Sequence similaritiesBelongs to the fibrillar collagen family.
Contains 1 fibrillar collagen NC1 domain.
Contains 1 laminin G-like domain.
DomainThe C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.
modificationsProlines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Sulfated on 40% of tyrosines.
Cellular localizationSecreted > extracellular space > extracellular matrix.
- Information by UniProt
ab7537 has not yet been referenced specifically in any publications.