Recombinant human SPARC protein is a Human Full Length protein, in the 18 to 303 aa range, expressed in CHO, with >98% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes The recombinant protein migrates at an apparent MWt of 43.7 kDa due to the effect of glycosylation. |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.
ON, SPARC, Basement-membrane protein 40, Osteonectin, Secreted protein acidic and rich in cysteine, BM-40
Recombinant human SPARC protein is a Human Full Length protein, in the 18 to 303 aa range, expressed in CHO, with >98% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
Constituents: 0.164% Sodium phosphate
Purity is greater than 98% by SDS-PAGE gel and HPLC analyses.
Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.
Belongs to the SPARC family.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
SPARC also known as Secreted Protein Acidic and Rich in Cysteine or osteonectin is a glycoprotein with a molecular mass of approximately 32 to 43 kDa. It is widely expressed in various tissues notably within the bone skin and extracellular matrix. SPARC influences cell-matrix interactions and modulates cellular functions such as proliferation and migration. The protein plays a role in tissue remodeling and wound healing by interacting with structural components of the matrix and regulating cell adhesion.
SPARC impacts processes related to cell communication and matrix dynamics. It does not form part of large complexes but functions through interactions with matrix molecules and receptors. SPARC regulates collagen fibrillogenesis and influences the bioavailability of growth factors. It further affects angiogenesis through its ability to alter cellular adhesion and spreading which impacts vascular development and repair processes.
SPARC integrates into regulatory cascades such as the WNT signaling and TGF-β pathways. These pathways are essential for cellular growth repair and differentiation. In the context of the TGF-β signaling pathway SPARC modulates interactions with proteins like integrins and collagens impacting fibrotic processes and matrix assembly.
Alterations in SPARC expression show associations with cancer and fibrosis. The protein functions in tumor progression where it can influence tumor cell interactions with the stroma and affect cell migration and invasion. Furthermore in fibrotic diseases SPARC regulates the deposition and organization of collagen contributing to tissue stiffening. Connections are evident between SPARC and other matrix proteins like fibronectin known for their roles in these pathological conditions.
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