Rat anti Heparan Sulphate Proteoglycan
| Code | Size | Price |
|---|
| MUB0801P | 0.1 mg | £326.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Rat
Antibody Isotype: IgG2a
Antibody Clonality: Monoclonal
Antibody Clone: A7L6
Regulatory Status: RUO
Target Species:
- Bovine (Cattle)
- Cod
- Human
- Mouse
- Rat
- Wolffish
Applications:
- Immunocytochemistry (ICC)
- Immunohistochemistry (IHC)
- Immunoprecipitation (IP)
- Western Blot (WB)
Storage:
Store at 4°C or in small aliquots at -20°C.
Documents
Further Information
Applications Description:
A7L6 is useful for immunoprecipitation, immunoblotting, immunocytochemistry and immuno-histochemistry on frozen and paraffin-embedded tissues. Optimal antibody dilution should be determined by titration; recommended range is 1:25 ? 1:200 for immunohistochemistry with avidin-biotinylated Horseradish peroxidase complex (ABC) as detection reagent, and 1:100 ? 1:1000 for immunoblotting applications.
Background:
Proteoglycans are macromolecules consisting of a variety of core proteins with covalently attached one or several polysaccharide chains of the glycosaminoglycan type (heparan sulphate, heparin, chondroitin sulphate, dermatan sulphate or keRatan sulphate). At least two forms of basement membrane heparan sulphate proteoglycan (HSPG) have been identified. One with a large core protein (> 400 kD) and one with a small core protein (30 kD). The large HSPG is probably the most abundant basement membrane proteoglycan. It is loCated predominantly in the lamina lucida, where it forms clustered aggregates and interacts with other basement membrane components to form the matrix. In addition, it also plays a critical role in attachment of cells to the basal membrane via integrin receptors.
Caution:
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.
This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.
This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
Field of Interest:
Extracellular matrix
Formulation:
The vial contains 100 ul 1 mg/ml monoclonal purified antibody in PBS containing 0.09% sodium azide.
Product:
The vial contains 100 ul 1 mg/ml monoclonal purified antibody in PBS containing 0.09% sodium azide.
Source:
A7L6 is a Rat monoclonal IgG2a antibody derived by fusion of X63 Ag8.653 Mouse myeloma cells with spleen cells from a Fisher Rat immunized with high molecular mass material derived from the Engelbreth-Holm-Swarm (EHS) tumor matrix containing laminin, entactin and HSPG.
Specificity:
A7L6 recognizes domain IV of the core protein of the large heparan sulphate proteoglycan or perlecan. The reactivity is independent of the galactosaminoglycan moieties. Therefore, the epitope is not sensitive to heparitinase treatment.
UniProt:
P98160
References
1. Couchman, J.R. (1987). Heterogeneous distribution of a basement membrane heparin sulfate proteoglycan in Rat tissues. The Journal of Cell Biology 105, 1901-16.
2. Couchman, J. R., and Ljubimov, A. V. (1989). Mammalian tissue distribution of a large heparan sulfate proteoglycan detected by monoclonal antibodies. Matrix 9, 311-21.
3. Horiguchi, Y., Couchman, J. R., Ljubimov, A. V., Yamasaki, H., and Fine, J. D. (1989). Distribution, ultrastructural localization, and ontogeny of the core protein of a heparan sulfate proteoglycan in Human skin and other basement membranes.
4. J Histochem Cytochem 37, 961-70. Ljubimov, A. V., Bartek, J., Couchman, J. R., Kapuller, L. L., Veselov, V. V., Kovarik, J., Perevoshchikov, A. G., and Krutovskikh, V. A. (1992). Distribution of individual components of basement membrane in Human colon polyps and adenocarcinomas as revealed by monoclonal antibodies. Int J Cancer 50, 562-66.
5. Couchman, J. R., Ljubimov, A. V., Sthanam, M., Horchar, T., and Hassell, J. R. (1995). Antibody mapping and tissue localization of globular and cysteine-rich regions of perlecan domain III. J Histochem Cytochem 43, 955-63.
6. Tapanadechopone, P., Hassell, J. R., Rigatti, B., and Couchman, J. R. (1999). Localization of glycosaminoglycan substitution sites on domain V of Mouse perlecan. Biochem Biophys Res Commun 265, 680-90.
7. Tingb?, M. G., Kolset, S. O., Ofstad, R., Enersen, G., Hannesson, K. O. (2006). IdentifiCation and distribution of heparan sulfate proteoglycans in the white muscle of Atlantic cod (Gadus morhua) and spotted wolffish (Anarhichas minor). Comparative Biochemistry and Physiology Part B 143,441-52.
2. Couchman, J. R., and Ljubimov, A. V. (1989). Mammalian tissue distribution of a large heparan sulfate proteoglycan detected by monoclonal antibodies. Matrix 9, 311-21.
3. Horiguchi, Y., Couchman, J. R., Ljubimov, A. V., Yamasaki, H., and Fine, J. D. (1989). Distribution, ultrastructural localization, and ontogeny of the core protein of a heparan sulfate proteoglycan in Human skin and other basement membranes.
4. J Histochem Cytochem 37, 961-70. Ljubimov, A. V., Bartek, J., Couchman, J. R., Kapuller, L. L., Veselov, V. V., Kovarik, J., Perevoshchikov, A. G., and Krutovskikh, V. A. (1992). Distribution of individual components of basement membrane in Human colon polyps and adenocarcinomas as revealed by monoclonal antibodies. Int J Cancer 50, 562-66.
5. Couchman, J. R., Ljubimov, A. V., Sthanam, M., Horchar, T., and Hassell, J. R. (1995). Antibody mapping and tissue localization of globular and cysteine-rich regions of perlecan domain III. J Histochem Cytochem 43, 955-63.
6. Tapanadechopone, P., Hassell, J. R., Rigatti, B., and Couchman, J. R. (1999). Localization of glycosaminoglycan substitution sites on domain V of Mouse perlecan. Biochem Biophys Res Commun 265, 680-90.
7. Tingb?, M. G., Kolset, S. O., Ofstad, R., Enersen, G., Hannesson, K. O. (2006). IdentifiCation and distribution of heparan sulfate proteoglycans in the white muscle of Atlantic cod (Gadus morhua) and spotted wolffish (Anarhichas minor). Comparative Biochemistry and Physiology Part B 143,441-52.