SPARC active protein

SPARC Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8120585

• Gene Names: SPARC; ON
• Purity: >98% as determined by SDS-PAGE
• Synonyms: SPARC; SPARC Protein; Human; Recombinant (His Tag); Human Osteonectin/SPARC Protein (His Tag); BM-40 Protein; ON Protein; secreted protein; acidic; cysteine-rich (osteonectin); SPARC active protein

• Host: HEK293 Cells
• Purity/Purification: >98% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Ile303

• Species: Human
• Activity: Measured by its ability to inhibit the cell growth of Mv-1-Lu mink lung epithelial cells. The ED50 for this effect is typically 1.5-7.5ug/mL.
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Ala 18
• Tag: C-His
• Protein Construction: A DNA sequence encoding the human SPARC (NP_003109.1) precursor (Met 1-Ile 303) with a carboxy-terminal polyhistidine tag was expressed.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

Related Product Information for SPARC active protein

Background: Secreted protein acidic and rich in cysteine (SPARC), also known as Osteonectin (ON), is a member of the SPARC family. SPARC consists of three domains: an EF-hand domain, a follistatin-like domain and a Kazal-like domain, and each of which has independent activity and unique properties. The activity of SPARC is context- and cell-type-dependent, which is highlighted by the fact that SPARC has shown seemingly contradictory effects on tumor progression in both clinical correlative studies and in animal models. The location of SPARC in the nuclear matrix of certain proliferating cells, but only in the cytosol of postmitotic neurons, indicates potential functions of SPARC as a nuclear protein, which might be involved in the regulation of cell cycle progression and mitosis. It functions not only to modulate cell-cell and cell-matrix interactions, but its de-adhesive and growth inhibitory properties in non-transformed cells have led to studies to assess its role in cancer. Its divergent actions reflect the complexity of this protein, because in certain types of cancers, such as melanomas and gliomas, SPARC is associated with a highly aggressive tumor phenotype, while in others, mainly ovarian, neuroblastomas and colorectal cancers, SPARC may function as a tumor suppressor. Recent studies have also demonstrated a role for SPARC in sensitizing therapy-resistant cancers. Notably, SPARC is linked to human obesity.

References

Yan Q, et al. (1999) SPARC, a matricellular glycoprotein with important biological functions. J Histochem Cytochem. 47(12): 1495-506.Brekken RA, et al. (2000) SPARC, a matricellular protein: at the crossroads of cell-matrix. Matrix Biol. 19(7): 569-80.Tai IT, et al. (2008) SPARC in cancer biology: its role in cancer progression and potential for therapy. Drug Resist Updat. 11(6): 231-46.Podhajcer OL, et al. (2008) The role of the matricellular protein SPARC in the dynamic interaction between the tumor and the host. Cancer Metastasis Rev. 27(3): 523-37.Kos K, et al. (2010) SPARC: a key player in the pathologies associated with obesity and diabetes. Nat Rev Endocrinol. 6(4): 225-35.

NCBI and Uniprot Product Information

• NCBI GI #: 4507171
• NCBI GeneID: 6678
• NCBI Accession #: NP_003109.1
• NCBI GenBank Nucleotide #: NM_003118.3
• UniProt Accession #: P09486; Q6IBK4; D3DQH9
• Molecular Weight: 34,632 Da
• NCBI Official Full Name: SPARC
• NCBI Official Synonym Full Names: secreted protein, acidic, cysteine-rich (osteonectin)
• NCBI Official Symbol: SPARC
• NCBI Official Synonym Symbols: ON
• NCBI Protein Information: SPARC; BM-40; basement-membrane protein 40; cysteine-rich protein; osteonectin; secreted protein acidic and rich in cysteine
• UniProt Protein Name: SPARC
• Protein Family: SPARC
• UniProt Gene Name: SPARC
• UniProt Synonym Gene Names: ON; BM-40; ON
• UniProt Entry Name: SPRC_HUMAN

NCBI Description

This gene encodes a cysteine-rich acidic matrix-associated protein. The encoded protein is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion. [provided by RefSeq, Dec 2011]

Uniprot Description

SPARC: 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.

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 5q31.3-q32

Cellular Component: extracellular space; platelet alpha granule membrane; nuclear matrix; cell surface; mitochondrion; cytoplasm; plasma membrane; extracellular region; basement membrane

Molecular Function: collagen binding; protein binding; extracellular matrix binding; calcium ion binding

Biological Process: response to peptide hormone stimulus; receptor-mediated endocytosis; response to gravity; platelet activation; extracellular matrix organization and biogenesis; ossification; response to cAMP; heart development; response to glucocorticoid stimulus; response to lipopolysaccharide; signal transduction; response to L-ascorbic acid; negative regulation of angiogenesis; platelet degranulation; response to cadmium ion; response to ethanol; response to cytokine stimulus; response to lead ion; negative regulation of endothelial cell proliferation; regulation of cell morphogenesis; response to calcium ion; blood coagulation; inner ear development; lung development

Disease: Osteogenesis Imperfecta, Type Xvii