Versican Antibody: ATTO 594

Category: Antibodies
Catalog
SMC-439D-A594
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Product Name Versican Antibody: ATTO 594
Description Versican (chondroitin sulfate proteoglycan 2) is a large extracellular matrix proteoglycan involved in cell growth and differentiation. Important as a structural molecule, versican creates loose and hydrated matrices during key events in development and disease. The protein contains hyaluronic acid and glycosminoglycan-binding domains, epidermal growth factor-like repeats, a Lectinlike sequence and a complement regulatory protein-like domain. Splice variants differ greatly in length anddegree of modification by glycoaminoglycan chains. Accumulation around smooth muscle cells in lesions of athero-sclerosis suggests a role for versican in atherogenesis. Versican, differentially expressed in human melanoma, plays a role in tumor development and may be a reliable marker for clinical diagnosis. The organization of HA- and versican-rich pericellular matrices may faciliatate migration and mitosis by diminishing cell surface adhesivity and affecting cell shape through steric exclusion and the viscous properties of HA proteoglycan gels. Mouse Anti-Mouse Versican Monoclonal IgG1
Synonyms Chondroitin sulfate proteoglycan 2 Antibody, CSPG2 Antibody, ERVR Antibody, GHAP Antibody, PG-M Antibody, VCAN Antibody, Chondroitin sulfate proteoglycan 2 Antibody, Chondroitin sulfate proteoglycan core protein 2 Antibody, Glial hyaluronate binding prote
Host Mouse
Clone S351-23
Immunogen Fusion protein amino acids 362-585 (glycosaminoglycan alpha domain) of mouse Versican core protein
Isotype IgG1
Specificity Detects >350kDa.
Reactivity Human, Mouse, Rat
Applications ICC, IF, WB
Form Purified, in PBS pH7.4, 50% glycerol, 0.1% sodium azide
Gene Id AAH96495. 13003
Uniprot Q62059
Background Versican (chondroitin sulfate proteoglycan 2) is a large extracellular matrix proteoglycan involved in cell growth and differentiation. Important as a structural molecule, versican creates loose and hydrated matrices during key events in development and disease. The protein contains hyaluronic acid and glycosminoglycan-binding domains, epidermal growth factor-like repeats, a Lectinlike sequence and a complement regulatory protein-like domain. Splice variants differ greatly in length anddegree of modification by glycoaminoglycan chains. Accumulation around smooth muscle cells in lesions of athero-sclerosis suggests a role for versican in atherogenesis. Versican, differentially expressed in human melanoma, plays a role in tumor development and may be a reliable marker for clinical diagnosis. The organization of HA- and versican-rich pericellular matrices may faciliatate migration and mitosis by diminishing cell surface adhesivity and affecting cell shape through steric exclusion and the viscous properties of HA proteoglycan gels.
Supplier Stressmarq Biosciences

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