Technical Data
L1350-02
Large Proteoglycan, GAG beta domain (Versican)
Description:
Versican is a large multi-domain chondroitin sulfate proteoglycan. It is secreted by fibroblasts and other types of cells. It has a N-terminal hyaluronic acid (HA) binding domain. This domain has homology with the G1 and G2 domains of aggrecan, (G1 is the hyaluronic acid binding region), to cartilage link protein which stabilizes the binding of aggrecan to hyaluronic acid, and, to the hyaluronate receptor CD44. In addition, versican also has a lectin like domain, a C-terminal compliment repeat, and two EGF-like repeats, all of which can be found in aggrecan. Versican has an apparent molecular mass of ~1000kD, of which the core contributes 400kD from the 2409 amino acids, and the 12-15 covalently attached chondroitin sulfate chains make up the rest.

Applications:
Suitable for use in ELISA, Immunohistochemistry, Western Blot and Immunoprecipitation. Other applications have not been tested.

Recommended Dilutions:
Immunohistochemistry (FFPE): 10ug/ml. Tissues must be treated with Chondroitinase before staining.
Western Blot: 0.5ug/ml
Optimal dilutions to be determined by the researcher.

Recommended Positive Control:
Immunohistochemistry: Surrounding cartilage
Western Blot: Total 13 day mouse embryo

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
50ug-20CBlue IceMouseRabbit
Concentration:
~0.5mg/ml
Immunogen:
GST fusion protein containing aa1360-1439 of mouse versican.
Purity:
Purified by affinity chromatography.
Form
Supplied as a liquid in PBS.
Specificity:
Recognizes mouse versican GAG beta domain.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Sobue, M., et al., Histochemical J. 21: 455 (1989).