antibody

Rat anti Heparan Sulphate Proteoglycan

MBS570091

0.1 mg

330 USD

monoclonal

rat

nonconjugated

A7L6

human, mouse, rat, cow

western blot, immunohistochemistry, immunocytochemistry, immunoprecipitation, immunohistochemistry - paraffin section, immunohistochemistry - frozen section

Antibody

Rat anti Heparan Sulphate Proteoglycan

Heparan Sulphate Proteoglycan

heparan sulphate proteoglycan; Glypican-3; glypican-3; secreted glypican-3; glypican proteoglycan 3; intestinal protein OCI-5; heparan sulphate proteoglycan; glypican 3; GTR2-2; Intestinal protein OCI-5; MXR7

GPC3; GPC3; SGB; DGSX; MXR7; SDYS; SGBS; OCI-5; SGBS1; GTR2-2; GPC3; OCI5

GPC3_HUMAN

Monoclonal

IgG2a

A7L6

Rat

Bovine, Human, Mouse, Rat, Cod and Wolffish.

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.

The vial contains 100 ul 1 mg/ml monoclonal purified antibody in PBS containing 0.09% sodium azide.

Store at 4 degree C, or in small aliquots at -20 degree C.

Immunocytochemistry (IHC), Immunohistochemistry (IHC) (frozen), Immunohistochemistry (IHC) (paraffin), Immunoprecipitation (IP), Western Blot (WB)

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.

Source Note: 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.

Warning and Caution: 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.

Extracellular matrix

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.

Couchman, J.R. (1987). Heterogeneous distribution of a basement membrane heparin sulfate proteoglycan in Rat tissues. The Journal of Cell Biology 105, 1901-16. 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. 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. 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. 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. Tingbø, 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.

1245417

P51654

A Tetrasaccharide Linker Sequence Is Required For GAG Synthesis Pathway (645305); Chondroitin Sulfate/dermatan Sulfate Metabolism Pathway (645308); Glycosaminoglycan Metabolism Pathway (645297); Glypican 3 Network Pathway (138084); Glypican Pathway (138083); HS-GAG Biosynthesis Pathway (645306); HS-GAG Degradation Pathway (645307); Heparan Sulfate/heparin (HS-GAG) Metabolism Pathway (645304); Metabolism Pathway (477135); Metabolism Of Carbohydrates Pathway (106196)

Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation. The protein encoded by this gene can bind to and inhibit the dipeptidyl peptidase activity of CD26, and it can induce apoptosis in certain cell types. Deletion mutations in this gene are associated with Simpson-Golabi-Behmel syndrome, also known as Simpson dysmorphia syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq]

GPC3: Cell surface proteoglycan that bears heparan sulfate. Inhibits the dipeptidyl peptidase activity of DPP4. May be involved in the suppression/modulation of growth in the predominantly mesodermal tissues and organs. May play a role in the modulation of IGF2 interactions with its receptor and thereby modulate its function. May regulate growth and tumor predisposition. Defects in GPC3 are the cause of Simpson-Golabi-Behmel syndrome type 1 (SGBS1); also known as Simpson dysmorphia syndrome (SDYS). SGBS is a condition characterized by pre- and postnatal overgrowth (gigantism) with visceral and skeletal anomalies. Belongs to the glypican family. Protein type: Membrane protein, GPI anchor; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: Xq26.1. Cellular Component: lysosomal lumen; proteinaceous extracellular matrix; extracellular space; anchored to plasma membrane; integral to plasma membrane; Golgi lumen; plasma membrane. Molecular Function: heparan sulfate proteoglycan binding; protein binding. Biological Process: phototransduction, visible light; anatomical structure morphogenesis; glycosaminoglycan metabolic process; negative regulation of peptidase activity; pathogenesis; positive regulation of endocytosis; osteoclast differentiation; embryonic hindlimb morphogenesis; body morphogenesis; bone mineralization; chondroitin sulfate metabolic process; positive regulation of glucose import; glycosaminoglycan biosynthetic process; glycosaminoglycan catabolic process; ureteric bud branching; negative regulation of smoothened signaling pathway; carbohydrate metabolic process; positive regulation of protein catabolic process; positive regulation of smoothened signaling pathway; retinoid metabolic process; positive regulation of BMP signaling pathway; lung development; negative regulation of epithelial cell proliferation; anterior/posterior axis specification; negative regulation of growth. Disease: Simpson-golabi-behmel Syndrome, Type 1; Wilms Tumor 1

0.1 mg

330 USD