SPARC

  • Official Full Name

    secreted protein, acidic, cysteine-rich (osteonectin)
  • Overview

    SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs . SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages,especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells,SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
  • Synonyms

    ON;BM-40;Osteonectin;Basement-membrane protein 40;Osteonectin (secreted protein, acidic, cysteine-rich);SPARC precursor;Secreted protein acidic and rich in cysteine;cysteine-rich protein;secreted protein, acidic, cysteine-rich (osteonectin);SPRC_HUMAN;SPARC [Precursor];SPARC

Recombinant Proteins

  • Human
  • Mouse
  • Cynomolgus
  • Rat
  • Zebrafish
  • Chicken
  • Rabbit
  • Bovine
  • E.coli
  • HEK293
  • Insect Cell
  • Mammalian cells
  • C-His
  • Mammalian Cell
  • CHO
  • Human Cell
  • Insect Cells
  • Insect cells
  • Bone
  • Human thrombin activated platelets
  • HEK293T
  • GST
  • His
  • Non
  • MBP
  • T7
  • His&T7
  • Myc&DDK
  • His&Fc&Avi
Cat.# Product name Source (Host) Species Tag Protein Length Price
SPARC-2899H Recombinant Human SPARC, GST-tagged E.coli Human GST 1-303aa
SPARC-3193H Recombinant Human SPARC protein, His-tagged HEK293 Human His Ala18-Ile303
Sparc-4034M Active Recombinant Mouse Sparc protein(Met1-Ile302), His-tagged HEK293 Mouse His Met1-Ile302
SPARC-01H Recombinant Human SPARC Protein, His-Tagged Insect Cell Human His 295aa
SPARC-126H Active Recombinant Human SPARC, His-tagged Mammalian cells Human His
Sparc-4030M Active Recombinant Mouse Sparc, His-tagged Mammalian cells Mouse His 18-302 a.a.
SPARC-525H Active Recombinant Human SPARC Protein, His-tagged Mammalian cells Human His Ala18-Ile303
SPARC-1676C Recombinant Cynomolgus SPARC protein, His-tagged C-His Cynomolgus Ala18-Ile303
SPARC-538R Active Recombinant Rat SPARC Protein, His-tagged HEK293 Rat His Met1-Ile301
SPARC-11H Recombinant Human SPARC E.coli Human Non
SPARC-210H Recombinant Human SPARC, His-tagged E.coli Human His
SPARC-263Z Recombinant Zebrafish SPARC Mammalian Cell Zebrafish His
SPARC-30654TH Recombinant Human SPARC, MBP-tagged E.coli Human MBP Full L.
SPARC-30655TH Recombinant Human SPARC, T7 -tagged E.coli Human T7
SPARC-31437TH Active Recombinant Human SPARC Protein, Tag Free CHO Human Non 18-303 a.a.
SPARC-34H Recombinant Full Length Human SPARC protein, MBP-tagged E.coli Human MBP Full L. 1-303 a.a.
SPARC-5683R Recombinant Rat SPARC Protein Mammalian Cell Rat His
SPARC-5980C Recombinant Chicken SPARC Mammalian Cell Chicken His
Sparc-7698M Recombinant Mouse Sparc protein, His-tagged E.coli Mouse His Ala18~Ile302
Sparc-7699R Recombinant Rat Sparc protein, His-tagged E.coli Rat His Ala18~Ile301
SPARC-7700R Recombinant Rabbit SPARC protein, His & T7-tagged E.coli Rabbit His&T7 Ala18~Glu273
SPARC-2120MCL Recombinant Mouse SPARC cell lysate Human Cell Mouse Non
SPARC-2616HCL Recombinant Human SPARC cell lysate Human Cell Human Non
SPARC-001H Recombinant Human SPARC Protein, MBP-tagged E.coli Human MBP 1-303
Sparc-010M Recombinant Mouse Sparc Protein, His-tagged Insect Cells Mouse His 18-302aa
Sparc-034M Recombinant Mouse Sparc Protein, His-tagged Insect cells Mouse His
SPARC-102H Recombinant Human SPARC protein, His-tagged E.coli Human His 314
SPARC-103H Active Recombinant Human SPARC protein E.coli Human Non 18-303 a.a.
SPARC-2503H Recombinant Full Length Human SPARC Protein, MYC/DDK-tagged HEK293 Human Myc&DDK Full L. 1-303 a.a.
SPARC-2725H Recombinant Human SPARC Protein, His-tagged CHO Human His Ala18-Ile303
SPARC-287B Native Bovine Osteonectin Bone Bovine Non
SPARC-30653TH Native Human SPARC Human thrombin activated platelets Human Non Full L. 18-303 a.a.
SPARC-4111H Recombinant Human SPARC Protein, His (Fc)-Avi-tagged HEK293 Human His&Fc&Avi
SPARC-4111H-B Recombinant Human SPARC Protein Pre-coupled Magnetic Beads HEK293 Human
SPARC-5254H Recombinant Human SPARC protein, GST-tagged E.coli Human GST 18-303aa
SPARC-5342R Recombinant Rat SPARC Protein, His (Fc)-Avi-tagged HEK293 Rat His&Fc&Avi
SPARC-5342R-B Recombinant Rat SPARC Protein Pre-coupled Magnetic Beads HEK293 Rat
SPARC-6051H Recombinant Human SPARC Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Human Myc&DDK
Sparc-6073M Recombinant Mouse Sparc Protein, Myc/DDK-tagged HEK293T Mouse Myc&DDK
SPARC-6342H Recombinant Human SPARC Protein (Ala18-Ile303), C-His tagged Mammalian cells Human His Ala18-Ile303
SPARC-6343H Recombinant Human SPARC Protein (Ala18-Ile303), N-His tagged E.coli Human His Ala18-Ile303
Sparc-8608M Recombinant Mouse Sparc Protein, His (Fc)-Avi-tagged HEK293 Mouse His&Fc&Avi
Sparc-8608M-B Recombinant Mouse Sparc Protein Pre-coupled Magnetic Beads HEK293 Mouse

    Background

    What is SPARC protein?

    SPARC (Secreted Protein Acidic and Rich in Cysteine), also known as osteonectin, is a protein that is expressed in various tissues and has diverse biological functions. It belongs to the matricellular protein family, which influences cell-matrix interactions and tissue remodeling.

    The SPARC protein is primarily found in the extracellular matrix, where it regulates cell adhesion, migration, proliferation, and tissue development. It interacts with different types of cells, including fibroblasts, endothelial cells, and immune cells, and plays a role in tissue remodeling during embryonic development, wound healing, and tissue repair.

    What is the function of SPARC protein?

    Modulates cell-matrix interactions: It binds collagen and other ECM components to regulate how cells interact with and respond to the surrounding microenvironment.

    Inhibits cell adhesion: SPARC promotes cell detachment from the ECM by interfering with adhesion receptors like integrins. This affects cell spreading, migration, proliferation.

    Remodels extracellular matrix: It regulates deposition and rearrangement of ECM components like collagen and their crosslinking by involving in ECM turnover processes.

    Regulates growth factors: SPARC binds various growth factors like VEGF, PDGF, FGFs and alters their ECM retention and presentation to cells, thus modulating their downstream signaling.

    SPARC related signaling pathway

    MAPK/ERK pathway: SPARC binds to components like FGF to activate ERK signaling, regulating processes like cell proliferation and differentiation.

    TGF-β pathway: It interacts with TGF-β1 and facilitates its signaling by retaining it in the ECM. This affects processes like fibrosis and EMT.

    Wnt/β-catenin pathway: SPARC modulates Wnt ligand availability and signaling strength via interaction with FZD receptors and LRP co-receptors.

    Notch pathway: It regulates cleavage and signaling of Notch receptors affecting cell-fate decisions during development and disease.

    SPARC Related Diseases

    •  Cancers: Altered levels in many cancers like breast, brain, prostate, linked to invasiveness, metastasis, and prognosis.
    •  Pulmonary fibrosis: Implicated in pathogenesis by promoting collagen deposition and ECM remodeling in lungs.
    •  Cardiovascular diseases: Associated with atherosclerotic plaque formation and instability. Role in post-MI cardiac remodeling.
    •  Renal diseases: Involved in tubulointerstitial fibrosis during AKI and CKD through TGF-β modulation.
    •  Arthritis: Expression upregulated in osteoarthritic and rheumatoid arthritis joints contributing to cartilage degradation.
    •  Cancer therapy: Developing SPARC inhibitors/antagonists as anti-cancer drugs to target tumors dependent on SPARC function.
    •  Anti-fibrotics: Investigating SPARC modulation as an approach to treat fibrotic diseases of lungs, kidneys, liver by interfering with ECM deposition.
    •  Wound healing: Studying the role of SPARC in modulating wound repair processes like contraction, scar formation to improve outcomes.
    •  Tissue engineering: Using knowledge of SPARC to develop biomaterials for regenerative approaches by regulating interactions between graft and host tissues.
    •  Cancer therapy: Developing SPARC inhibitors/antagonists as anti-cancer drugs to target tumors dependent on SPARC function.
    •  Anti-fibrotics: Investigating SPARC modulation as an approach to treat fibrotic diseases of lungs, kidneys, liver by interfering with ECM deposition.
    •  Wound healing: Studying the role of SPARC in modulating wound repair processes like contraction, scar formation to improve outcomes.
    •  Tissue engineering: Using knowledge of SPARC to develop biomaterials for regenerative approaches by regulating interactions between graft and host tissues.

    Case Study

    Immunoblotting of SPARC in Ewing sarcoma.jpg

    (Guillem Pascual-Pasto, 2022)

    Fig2. Immunoblotting of SPARC in Ewing sarcoma, rhabdomyosarcoma (RMS) and osteosarcoma (OS) PDXs. Sample names are coded as described previously, but the codes in the figure omit the prefix HSJD for clarity purposes [22]. α-Tubulin was the loading control. Numbers below represent the signal ratio of SPARC relative to α-tubulin.

    Relative SPARC mRNA expression levels.jpg

    (Jie Yin, 2010)

    Fig3.Relative SPARC mRNA expression levels. Autoradiographs were scanned and analyzed by densitometry followed by quantitation relative to β-actin. Results are shown as expression (in %) relative to β-actin and are means (± SD) of 3

    Quality Guarantee

    High Purity

    SDS-PAGE Sparc-7699R.jpg

    Fig1. SDS-PAGE (Cat. No.: Sparc-7699R)

    Involved Pathway

    SPARC involved in several pathways and played different roles in them. We selected most pathways SPARC participated on our site, such as Binding and Uptake of Ligands by Scavenger Receptors,ECM proteoglycans,Extracellular matrix organization, which may be useful for your reference. Also, other proteins which involved in the same pathway with SPARC were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    ECM proteoglycans MUSK,FMOD,PTPRS,BGNA,ASPN,DMP1,MATN4,MATN1,COL9A3,VCANB
    Binding and Uptake of Ligands by Scavenger Receptors STAB2,COL1A1,IGKC,SCGB3A2,APOBB.1,AMBP,IGKV1-5,Alb,HYOU1,COL1A2
    Platelet degranulation CD9A,CALU,BRPF3,CAP1,TFA,MMRN1,F13A1B,SERPINF2B,IGF2B,MMRN2A
    Scavenging by Class H Receptors STAB2
    Hemostasis LOC100514666,CABLES1,SLC7A6,GATA1A,CENPE,TRPC3,GRB7,MAFGA,SERPINE2,KIF5A
    Platelet activation, signaling and aggregation CALU,RHOGA,CLEC1B,BRPF3,ABHD6B,SRGN,C6orf25,HRG,CLU,STXBP3A
    Response to elevated platelet cytosolic Ca2+ STXBP3,HRG,CAP1,CD9B,STXBP3A,SRGN,SCG3,CALU,PLEK,CD9A
    Extracellular matrix organization FBN2,FBN1,TLL2,COL9A1A,LOXL4,MMP19,SERPINH1,CTSD,MFAP2,PTPRS

    Protein Function

    SPARC has several biochemical functions, for example, calcium ion binding,collagen binding,extracellular matrix binding. Some of the functions are cooperated with other proteins, some of the functions could acted by SPARC itself. We selected most functions SPARC had, and list some proteins which have the same functions with SPARC. You can find most of the proteins on our site.

    Function Related Protein
    protein binding GAGE1,EBF2,LCA5,TXN,ARHGAP9,RAB1B,RBBP4,BAG1,UNKL,DYRK1B
    collagen binding ADAM9,LACRT,GP6,NID1,SRGN,RELL2,CD44,CHADL,MMP9,PCOLCE2
    extracellular matrix binding SPP1,DMP1,BGN,ITGB3,VEGFA,FBLN2,ITGA2B,ITGAV,DCN,TGFBI
    calcium ion binding NECAB2,DGKB,NCALDA,PCDH15,PCDH2G4,PCDH2G17,PLS1,GSNB,PKD2L2,BMP1

    Interacting Protein

    SPARC has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SPARC here. Most of them are supplied by our site. Hope this information will be useful for your research of SPARC.

    faf;XRCC6;fusA;ZNF579

    Resources

    References

    • Onoz, M; Basaran, R; et al. Correlation between SPARC (Osteonectin) expression with immunophenotypical and invasion characteristics of pituitary adenomas. APMIS 123:199-204(2015).
    • Peixoto, E; Atorrasagasti, C; et al. SPARC (secreted protein acidic and rich in cysteine) knockdown protects mice from acute liver injury by reducing vascular endothelial cell damage. GENE THERAPY 22:9-19(2015).

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