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NSJ Bioreagents

SKU:V9589-20UG

SPARC Antibody / Osteonectin, 20 ug

SPARC Antibody / Osteonectin, 20 ug

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SPARC (for secreted protein acidic and rich in cysteine) is a phosphorylated, acidic, glycine-rich glycoprotein that is secreted by endothelial cells and is present in large amounts in the parietal endoderm of mouse embryos and in human placenta. It is identical to osteonectin, a protein important to bone calcification that is highly conserved between species. SPARC, which can be selectively expressed by the endothelium in response to certain types of injury, induces rounding in adherent endothelial cells in vitro. It regulates endothelial barrier function through F-Actin-dependent changes in cell shape, coincident with the appearance of intercellular gaps, which provide a paracellular pathway for extravasation of macromolecules.

Specifications

Catalog No V9589-20UG
Family Primary antibody
Qty 20 ug
Formulation 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide
Format Purified
Clone OSTN/3759
Host Animal Mouse
Clonality Monoclonal (mouse origin)
Isotype Mouse IgG2c, kappa
Species Reactivity Human
Application WB, IHC-P
Application Details Western blot: 1-2ug/ml,Immunohistochemistry (FFPE): 1-2ug/ml
Application Note Optimal dilution of the SPARC antibody should be determined by the researcher.
Localization Secreted
Immunogen A portion of amino acids 1-200 was used as the immunogen for the SPARC antibody.
Purity Protein A/G affinity
Storage Aliquot the SPARC antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Limitation This SPARC antibody is available for research use only.
Uniprot # P09486
Status Available
PDF Link https://www.nsjbio.com/tds-pdf/sparc-antibody-osteonectin-ostn3759-v9589
Title SPARC Antibody / Osteonectin
Description SPARC (for secreted protein acidic and rich in cysteine) is a phosphorylated, acidic, glycine-rich glycoprotein that is secreted by endothelial cells and is present in large amounts in the parietal endoderm of mouse embryos and in human placenta. It is identical to osteonectin, a protein important to bone calcification that is highly conserved between species. SPARC, which can be selectively expressed by the endothelium in response to certain types of injury, induces rounding in adherent endothelial cells in vitro. It regulates endothelial barrier function through F-Actin-dependent changes in cell shape, coincident with the appearance of intercellular gaps, which provide a paracellular pathway for extravasation of macromolecules.
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