Ensuring timely antibody supply during the COVID-19 pandemic - contact us for solutions

Human Type V Collagen-Lyophilized

Cat. No.:
Purified Human Type V Collagen (lyophilized) for use as a coating material and standard.
Size Price (USD) Quantity
0.1 mg $135.00
More Information
Description Collagen is the main structural protein in the extracellular space and is the most abundant protein in the ECM. Collagens are divided into two classes - fibril (types I, II, III, V) and non-fibril (types IV, VI). Type V collagen is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen mutations are associated with Ehlers-Danlos syndrome. Type V collagen is broadly expressed as a two α1(V) chains and one α2(V) chain heterotrimer but also as a α1(V), α2(V), and α3(V) heterotrimer in pancreatic islets, adipose tissue, and skeletal muscle.
Source Placental villi
Purity > 90% by SDS-PAGE
Purification Method Controlled and limited pepsin digestion followed by selective salt precipitation
Buffer Formulation Lyophilized from 500 mM acetic acid
Recommended Storage 2-8°C
Applications ELISA – Quality tested 1-3
SDS-PAGE – Quality tested
Thermal Stability Studies – Reported in literature 4
Coating Material for –
Adhesion Studies – Reported in literature 2-3
ECM Interaction Studies – Reported in literature 5,6

Certificate of Analysis Lookup

Enter the Catalog Number and Lot Number for the Certificate of Analysis you wish to view

Need help with this product?
or call 800.722.2255
  1. 1. Bumann A, Carvalho RS, Schwarzer CL, Yen EH. Collagen synthesis from human PDL cells following orthodontic tooth movement. Eur J Orthod. 1997;19:29-37. (ELISA, Standard Curve)
  2. 2. Saito K, Tanaka T, Kanda H, Ebisuno Y, Izawa D, Kawamoto S, et al. Gene expression profiling of mucosal addressin cell adhesion molecule-1+ high endothelial venule cells (HEV) and identification of a leucine-rich HEV glycoprotein as a HEV marker. J Immunol. 2002;168:1050-9. (ELISA, Coat, Adhesion Studies)
  3. 3. Nagakubo D, Murai T, Tanaka T, Usui T, Matsumoto M, Sekiguchi K, et al. A high endothelial venule secretory protein, mac25/angiomodulin, interacts with multiple high endothelial venule-associated molecules including chemokines. J Immunol. 2003;171:553-61. (ELISA, Coat, Adhesion Studies)
  4. 4. Makareeva E, Mertz EL, Kuznetsova NV, Sutter MB, DeRidder AM, Cabral WA, et al. Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta. J Biol Chem. 2008;283:4787-98. (Thermal Stability Studies)
  5. 5. Bidanset DJ, Guidry C, Rosenberg LC, Choi HU, Timpl R, Hook M. Binding of the proteoglycan decorin to collagen type VI. J Biol Chem. 1992;267:5250-6. (Coat, ECM Interaction Studies)
  6. 6. Hocking AM, Strugnell RA, Ramamurthy P, McQuillan DJ. Eukaryotic expression of recombinant biglycan. Post-translational processing and the importance of secondary structure for biological activity. J Biol Chem. 1996;271:19571-7. (Coat, ECM Interaction Studies)
See All References