SPARC
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Official Full Name
secreted protein, acidic, cysteine-rich (osteonectin)
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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
- Cell & Tissue Lysates
- Native Proteins
- Protein Pre-coupled Magnetic Beads
- Bovine
- Chicken
- Human
- Mouse
- Rabbit
- Rat
- Zebrafish
- Bone
- CHO
- E.coli
- HEK293
- HEK293T
- Human Cell
- Insect Cell
- Insect cells
- Insect Cells
- Mammalian Cell
- Mammalian cells
- C
- His
- GST
- His (Fc)
- Avi
- His|T7
- MBP
- Myc
- DDK
- Myc|DDK
- N/A
- N
- T7
- Involved Pathway
- Protein Function
- Interacting Protein
- SPARC Related Articles
- SPARC Related Research Area
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 |
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Binding and Uptake of Ligands by Scavenger Receptors | HPX;Alb;SCGB3A2;NFX1;HYOU1;COL1A1;STAB2;LOC479668;HSPH1 |
ECM proteoglycans | LRP4;MUSK;BGNB;ACAN;SPARC;ASPN;DAG1;VCANB;HAPLN1 |
Extracellular matrix organization | ADAMTS3;CRTAP;ADAM15;FURINA;MMP15;TIMP2B;EFEMP2;DAG1;DDR1 |
Hemostasis | LOC100514666;CABLES2;CAP1;DOCK10;GATA2A;BA1;LRRC16A;MAFF;SLC3A2B |
Platelet activation, signaling and aggregation | ABHD12;PDPN;SCG3;GAS6;TRPC6A;FCER1GL;CAP1;HRG;RHOGA |
Platelet degranulation | AASS;TFA;MMRN1;SCG3;BRPF3;CD9A;CALU;MMRN2A;CAP1 |
Response to elevated platelet cytosolic Ca2+ | SRGN;MMRN1;SERPINF2B;MMRN2A;WDR1;SPARC;F13A1B;CALU;TFA |
Scavenging by Class H Receptors | SPARC;STAB2 |
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 |
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calcium ion binding | MYL6B;EFCAB4B;EYS;S100B;DSC2L;AKR1C1;SLIT1;PCDHB14;PKD2L2 |
collagen binding | DDR1;GP6;NID1;ACHE;MTAP1A;SERPINH1A;FN1;TGFBI;COMP |
extracellular matrix binding | ITGAV;VEGFA;BGN;DMP1;SID4;CYR61;DCN;TGFBI;FBLN2 |
protein binding | PIK3R3;CHTOP;EAF2;ODC1;DCP1A;TMEM106C;SMARCA4;CRTAC1;SSX2 |
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
- Q&As
- Reviews
Q&As (5)
Ask a questionSPARC is associated with cancer progression, as it can influence tumor growth, invasion, and angiogenesis. Its expression levels in tumors are often studied for prognostic and diagnostic purposes.
Yes, SPARC is being explored as a therapeutic target for cancer. Researchers are investigating ways to modulate its activity to hinder tumor progression or enhance the efficacy of existing treatments.
SPARC expression can be detected through techniques like immunohistochemistry, Western blotting, and molecular assays. These methods help assess SPARC levels in tissues or blood samples.
SPARC plays a role in tissue repair by influencing cell-matrix interactions and modulating the extracellular environment. Its involvement in wound healing and tissue regeneration makes it a subject of interest in regenerative medicine.
Yes, there are clinical trials exploring the potential of targeting SPARC in various diseases, including cancer. These trials aim to evaluate the safety and efficacy of SPARC-modulating agents.
Customer Reviews (3)
Write a reviewThe SPARC protein finds great utility in protein electron microscopy structure analysis, consistently delivering exceptional results.
Its remarkable sensitivity and specificity make it a valuable tool for accurate and robust data analysis, bolstering the credibility of research outcomes.
Notably, it exhibits exceptional performance in ELISA assays, providing reliable and precise results in the detection and quantification of target molecules.
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