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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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SPARC antibody, also known as Secreted protein acidic and rich in cysteine antibody, recognizes a matricellular glycoprotein commonly referred to as Osteonectin and Basement membrane protein 40 in the literature. Secreted protein acidic and rich in cysteine is encoded by the human SPARC gene located on chromosome 5q33.1 and is a member of the SPARC family of matricellular proteins. It is primarily a secreted, extracellular matrix-associated protein that localizes to the extracellular space and basement membranes, where it modulates cell-matrix interactions rather than serving as a structural matrix component.
Secreted protein acidic and rich in cysteine functions as a regulator of cell adhesion, migration, proliferation, and tissue remodeling. It is highly expressed in bone, connective tissue, endothelium, and remodeling tissues, and it plays a critical role in collagen binding and extracellular matrix organization. A SPARC antibody is frequently used in research examining tumor microenvironment remodeling, angiogenesis, fibrosis, and wound healing because of the protein's involvement in regulating interactions between stromal cells and extracellular matrix components.
The SPARC protein contains several well-characterized structural domains, including an acidic N-terminal domain, a follistatin-like domain, and a C-terminal extracellular calcium-binding domain with EF-hand motifs. These domains enable SPARC to bind calcium and interact with collagens, albumin, and growth factors. Through these interactions, Secreted protein acidic and rich in cysteine modulates signaling pathways such as TGF-beta signaling, integrin-mediated adhesion pathways, and extracellular matrix remodeling cascades.
SPARC antibody, also referred to as Osteonectin antibody and BM-40 antibody in published studies, is widely used to investigate stromal activation in cancer. Elevated SPARC expression has been reported in multiple tumor types, including breast, pancreatic, colorectal, and ovarian carcinomas, where it is associated with desmoplastic reactions and extracellular matrix deposition. In some contexts, SPARC expression correlates with tumor invasion and metastatic potential, while in others it may exhibit context-dependent tumor-suppressive properties.
Beyond oncology, Secreted protein acidic and rich in cysteine plays important roles in tissue repair and fibrotic disorders. It is upregulated during wound healing and in fibrotic conditions affecting organs such as liver, lung, and kidney. SPARC participates in collagen fibrillogenesis and regulates matrix stiffness, which can influence cell differentiation and immune cell infiltration. In skeletal biology, Osteonectin is abundant in bone matrix and contributes to mineralization processes.
Developmentally, SPARC is expressed during embryogenesis in tissues undergoing active morphogenesis and extracellular matrix remodeling. It is detected in endothelial cells during vascular development and in mesenchymal lineages that contribute to connective tissue formation. Cell-type specific expression has been observed in fibroblasts, osteoblasts, endothelial cells, and certain epithelial compartments depending on physiological or pathological context.
Clone OSTN/3761 is designed to recognize SPARC in research applications. A SPARC antibody can be used to evaluate extracellular matrix remodeling, stromal composition, and tumor-associated fibroblast activity in a variety of experimental models. This antibody targets SPARC in research applications and supports studies of matrix biology, fibrosis, angiogenesis, and cancer-associated stromal dynamics.
Optimal dilution of the SPARC antibody should be determined by the researcher.
A portion of amino acids 1-200 from human SPARC protein was used as the immunogen for the SPARC antibody.
Aliquot the SPARC antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
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