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SPARC (Osteonectin) ELISA Kit, Antibody, Recombinant
Search for SPARC Products and order it online please visiting www.aviscerabioscience.com

Alternative name:

  • secreted protein, acidic, cysteine-rich (SPARC)
  • Osteonectin
  • Basement-membrane protein 40
  • BM40
Secreted protein acidic and rich in cysteine/osteonectin/BM40, or SPARC, is a matrix-associated protein that elicits changes in cell shape, inhibits cell-cycle progression, and influences the synthesis of extracellular matrix (ECM).
SPARC regulates cell growth through interactions with the extracellular matrix and cytokines. SPARC 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.

Human SPARC ELISA Kit SK00766-06 was used by Dr. Lee SH on following paper

Lee SH et al. Obesity (Silver Spring). 2013 Nov;21(11):2296-302. doi: 10.1002/oby.20183. Epub 2013 May 13.

Human SPARC ELISA Kit SK00766-06 was used by Dr. Lee YJ on following paer.

Background Remodeling of the extracellular matrix (ECM) of adipose tissue is regarded as part of the pathophysiology of obesity. Secreted protein acidic and rich in cysteine (SPARC) was the first ECM protein described in adipose tissue. Matrix metalloproteinases (MMPs) also play a role in ECM remodeling, and MMP-2 and MMP-9 may be associated with abnormal ECM metabolism. Here, we investigated changes in serum SPARC, MMP-2, and MMP-9 concentrations after bariatric surgery in obese adults. Methods We recruited 34 obese patients who were scheduled to undergo bariatric surgery for weight loss. We analyzed changes in serum SPARC, MMP-2, and MMP-9 concentrations before and 9 months after bariatric surgery and any associations between changes in SPARC, MMP-2, and MMP-9 concentrations and obesity-related parameters. Results Serum leptin levels significantly decreased, and the serum adiponectin level significantly increased after bariatric surgery. The serum SPARC concentration decreased significantly from 165.0 ± 18.2 to 68.7 ± 6.7 ng/mL (p< 0.001), and the MMP-2 concentration also decreased significantly from 262.2 ± 15.2 to 235.9 ± 10.5 ng/mL (p< 0.001). Changes in the serum SPARC concentration were significantly correlated with HOMA-IR changes, and changes in the serum MMP-9 concentration were found to inversely correlate with serum adiponectin changes. Conclusion These findings show that significant decreases in serum SPARC and MMP-2 concentrations occur after bariatric surgery. Our results thus suggest that weight loss via bariatric surgery could alter the ECM environment, and that these changes are related to certain metabolic changes.
Lee YJ et al. Obes Surg. 2014 Apr;24(4):604-10.
OBJECTIVE: Several epidemiological studies have shown that regular exercise can prevent the onset of colon cancer, although the underlying mechanism is unclear. Myokines are secreted skeletal muscle proteins responsible for some exercise-induced health benefits including metabolic improvement and anti-inflammatory effects in organs. The purpose of this study was to identify new myokines that contribute to the prevention of colon tumorigenesis.
METHODS: To identify novel secreted muscle-derived proteins, DNA microarrays were used to compare the transcriptome of muscle tissue in sedentary and exercised young and old mice. The level of circulating secreted protein acidic and rich in cysteine (SPARC) was measured in mice and humans that performed a single bout of exercise. The effect of SPARC on colon tumorigenesis was examined using SPARC-null mice. The secretion and function of SPARC was examined in culture experiments.
RESULTS: A single bout of exercise increased the expression and secretion of SPARC in skeletal muscle in both mice and humans. In addition, in an azoxymethane-induced colon cancer mouse model, regular low-intensity exercise significantly reduced the formation of aberrant crypt foci in wild-type mice but not in SPARC-null mice. Furthermore, regular exercise enhanced apoptosis in colon mucosal cells and increased the cleaved forms of caspase-3 and caspase-8 in wild-type mice but not in SPARC-null mice. Culture experiments showed that SPARC secretion from myocytes was induced by cyclic stretch and inhibited proliferation with apoptotic effect of colon cancer cells.
CONCLUSIONS: These findings suggest that exercise stimulates SPARC secretion from muscle tissues and that SPARC inhibits colon tumorigenesis by increasing apoptosis.
SPARC (secreted protein acidic and rich in cysteine, also known as osteonectin or BM-40) is a widely expressed profibrotic protein with pleiotropic roles, which have been studied in a variety of conditions. Notably, SPARC is linked to human obesity; SPARC derived from adipose tissue is associated with insulin resistance and secretion of SPARC by adipose tissue is increased by insulin and the adipokine leptin. Furthermore, SPARC is associated with diabetes complications such as diabetic retinopathy and nephropathy, conditions that are ameliorated in the Sparc-knockout mouse model. As a regulator of the extracellular matrix, SPARC also contributes to adipose-tissue fibrosis. Evidence suggests that adipose tissue becomes increasingly fibrotic in obesity. Fibrosis of subcutaneous adipose tissue may restrict accumulation of triglycerides in this type of tissue. These triglycerides are, therefore, diverted and deposited as ectopic lipids in other tissues such as the liver or as intramyocellular lipids in skeletal muscle, which predisposes to insulin resistance. Hence, SPARC may represent a novel and important link between obesity and diabetes mellitus. This Review is focused on whether SPARC could be a key player in the pathology of obesity and its related metabolic complications.
Kos K, Wilding JP.Nat Rev Endocrinol. 2010 Apr;6(4):225-35. Epub 2010 Mar 2.
The cardiac interstitium is a unique and adaptable extracellular matrix (ECM) that provides a milieu in which myocytes, fibroblasts, and endothelial cells communicate and function. The composition of the ECM in the heart includes structural proteins such as fibrillar collagens and matricellular proteins that modulate cell:ECM interaction. Secreted Protein Acidic and Rich in Cysteine (SPARC), a collagen-binding matricellular protein, serves a key role in collagen assembly into the ECM. Recent results demonstrated increased cardiac rupture, dysfunction and mortality in SPARC-null mice in response to myocardial infarction that was associated with a decreased capacity to generate organized, mature collagen fibers. In response to pressure overload induced-hypertrophy, the decrease in insoluble collagen incorporation in the left ventricle of SPARC-null hearts was coincident with diminished ventricular stiffness in comparison to WT mice with pressure overload. This review will focus on the role of SPARC in the regulation of interstitial collagen during cardiac remodeling following myocardial infarction and pressure overload with a discussion of potential cellular mechanisms that control SPARC-dependent collagen assembly in the heart.
McCurdy S, et al. J Mol Cell Cardiol. 2010 Mar;48(3):544-9. Epub 2009 Jul 3.
Proteins involved in platelet signaling are differentially regulated in acute coronary syndrome: a proteomic study

BACKGROUND: Platelets play a fundamental role in pathological events underlying acute coronary syndrome (ACS). Because platelets do not have a nucleus, proteomics constitutes an optimal approach to follow platelet molecular events associated with the onset of the acute episode.
METHODOLOGY/PRINCIPAL FINDINGS: We performed the first high-resolution two-dimensional gel electrophoresis-based proteome analysis of circulating platelets from patients with non-ST segment elevation ACS (NSTE-ACS). Proteins were identified by mass spectrometry and validations were by western blotting. Forty protein features (corresponding to 22 unique genes) were found to be differentially regulated between NSTE-ACS patients and matched controls with chronic ischemic cardiopathy. The number of differences decreased at day 5 (28) and 6 months after the acute event (5). Interestingly, a systems biology approach demonstrated that 16 of the 22 differentially regulated proteins identified are interconnected as part of a common network related to cell assembly and organization and cell morphology, processes very related to platelet activation. Indeed, 14 of those proteins are either signaling or cytoskeletal, and nine of them are known to participate in platelet activation by αIIbβ3 and/or GPVI receptors. Several of the proteins identified participate in platelet activation through post-translational modifications, as shown here for ILK, Src and Talin. Interestingly, the platelet-secreted glycoprotein SPARC was down-regulated in NSTE-ACS patients compared to stable controls, which is consistent with a secretion process from activated platelets.
CONCLUSIONS/SIGNIFICANCE: The present study provides novel information on platelet proteome changes associated with platelet activation in NSTE-ACS, highlighting the presence of proteins involved in platelet signaling. This investigation paves the way for future studies in the search for novel platelet-related biomarkers and drug targets in ACS.

 Fernández Parguiña A, et al. PLoS One. 2010 Oct 14;5(10):e13404.

Identification of Adipocyte Genes Regulated by Caloric Intake

Context: Changes in energy intake have marked and rapid effects on metabolic functions, and some of these effects may be due to changes in adipocyte gene expression that precede alterations in body weight. Objective: The aim of the study was to identify adipocyte genes regulated by changes in caloric intake independent of alterations in body weight. Research Design and Methods: Obese subjects given a very low-caloric diet followed by gradual reintroduction of ordinary food and healthy subjects subjected to overfeeding were investigated. Adipose tissue biopsies were taken at multiple time-points, and gene expression was measured by DNA microarray. Genes regulated in the obese subjects undergoing caloric restriction followed by refeeding were identified using two-way ANOVA corrected with Bonferroni. From these, genes regulated by caloric restriction and oppositely during the weight-stable refeeding phase were identified in the obese subjects. The genes that were also regulated, in the same direction as the refeeding phase, in the healthy subjects after overfeeding were defined as being regulated by caloric intake. Results were confirmed using real-time PCR or immunoassay. Results: Using a significance level of P < 0.05 for all comparisons, 52 genes were down-regulated, and 50 were up-regulated by caloric restriction and regulated in the opposite direction by refeeding and overfeeding. Among these were genes involved in lipogenesis (ACLY, ACACA, FASN, SCD), control of protein synthesis (4EBP1, 4EBP2), {beta}-oxidation (CPT1B), and insulin resistance (PEDF, SPARC). Conclusions: Metabolic genes involved in lipogenesis, protein synthesis, and insulin resistance are central in the transcriptional response of adipocytes to changes in caloric intake.

Niclas Franck et al. Journal of Clinical Endocrinology & Metabolism , doi:10.1210/jc.2009-2534. published online onNovember 3, 2010
human sparc elisa kit sk00766-06 is enable to measure human sparc on serum samples. that is available in aviscera bioscience
 
   
Human SPARC(Osteonectin) ELISA
Code No.: SK00766-08
Size: 96 T
Price: $460.00 USD
Standard Range:0.19-12.5 ng/ml
Sensitivity:0.10 ng/ml
Specificity: Human SPARC
Calibration: recombinant human SPARC (HEK293 derived)
Sample Type: serum
Dilution Factor: 40
IntraCV: 6-8%
InterCV: 10-12%
Protocol: PDF
human sparc elisa kit
Human SPARC(Osteonectin) ELISA
Code No.: SK00766-06
Size: 96 T
Price: $420.00 USD
Standard Range:0.39-25 ng/ml
Sensitivity:0.15 ng/ml
Specificity: Human SPARC
Calibration: recombinant human SPARC (HEK293 derived)
Sample Type: serum
Dilution Factor: 40
IntraCV: 6-8%
InterCV: 10-12%
Protocol: PDF
   
rat SPARC ELISA Kit is available in stock Rat/MousePARC(Osteonectin) ELISA
Code No.: SK00766-02
Size: 96 T
Price: $420.00 USD
Standard Range:0.128-2000 ng/ml
Dynamic Range: 0.64- 2000 ng/ml
Sensitivity:0.128 ng/ml
Sample Type: serum, EDTA plasma
Sample requres: 120 ul, 50 ul per well
Dilution Factor: 2~4 (Optimal dilutions should be determined by each laboratory for each application)
IntraCV: 4-6%
InterCV: 8-10%
Protocol: PDF
human sparc recombinant from aviscera bioscience
Human Osteonectin/SPARC Recombinant
Code No.: 00766-06-10
Size: 10 ug
Price: $250.00 USD
Protein ID:P09486
Gene ID: 6678
MW:45 KD
Tag: His Tag on C-Terminus
Expressed: 293 cells
Purity: 95%
Data Sheet: PDF

human osteonectin/sparc recombinant

Human Osteonectin/SPARC Recombinant
Code No.: 00766-01-100
Size: 100 ug
Price: $240.00 USD
Protein ID:P09486
Gene ID: 6678
MW:36 KD
Tag: His Tag on N-Terminus
Expressed: E. Coli
Purity: 95%
Data Sheet: PDF
rat sparc recombinant Rat Osteonectin/SPARC Recombinant
Code No.: 00766-03-100
Size: 100 ug
Price: $360.00 USD
Protein ID:P16975
Gene ID: 24791
MW:50 KD
Tag: His Tag on N-Terminus
Expressed: E. Coli
Purity: 95%
Data Sheet: PDF
  Mouse Osteonectin/SPARC Recombinant
Code No.: 00766-07-10
Size: 10 ug
Price: $100.00 USD
Protein ID:NP_033268
Gene ID: NM_009242
MW:45 KD
Tag: His Tag on C-Terminus
Expressed: 293 cells
Purity: 95%
Data Sheet: PDF
anti human osteonectin antibody
Anti Human Osteonectin/SPARC IgG
Code No.: A00766-01-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen: human SPARC Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC
Working Dilution: 2 ug/ml)
Data Sheet: PDF
anti human osteonectin antibody
Anti Human Osteonectin/SPARC IgG
Code No.: A00766-01-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen: human SPARC Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC
Working Dilution: 2 ug/ml)
Data Sheet: PDF

anti human SPARC antibody

Anti Human Osteonectin/SPARC IgG
Code No.: A00766-01-100
Size: 100 ug
Price: $220.00 USD
Host: Rabbit
Antigen: human SPARC Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: E, IHC
Working Dilution: 2 ug/ml)
Data Sheet: PDF
Anti Rat Osteonectin/SPARC IgG
Code No.: A00766-20-100
Size: 100 ug
Price: $300.00 USD
Host: Rabbit
Antigen: rat SPARC Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: WB,E, IHC
Working Dilution: WB (0.25-0.5 ug/ml)
Data Sheet: PDF
anti rat SPARC antibody Anti Rat Osteonectin/SPARC IgG
Code No.: A00766-20-100
Size: 100 ug
Price: $300.00 USD
Host: Rabbit
Antigen: rat SPARC Rec.
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: WB,E, IHC
Working Dilution: WB (0.25-0.5 ug/ml)
Data Sheet: PDF
anti sparc antibody for immunohistochemistry Anti  Osteonectin/SPARC IgG
Code No.: A00766-20-100
Size: 100 ug
Price: $300.00 USD
Host: Rabbit
Antigen: rat SPARC Rec.
Specificity: human, rat, Mouse
Ab Type: Polyclonal IgG
Purification: Protein A
Applications: WB,E, IHC
Working Dilution: WB (0.25 ug/ml)
Data Sheet: PDF

 

 

Name
Code No.
Size
Price ($)
SPARC / Osteonectin (Human) ELISA Kit
96 T
460.00
SPARC / Osteonectin (Human) ELISA Kit
96 T
420.00
Rat/Mouse SPARC ELISA Kit SK00766-02 96 T 420.00
SPARC/Osteonectin (Human) Rec.
00766-01-50
50 ug
150.00
SPARC/Osteonectin (Human) Rec.
100 ug
240.00
SPARC/Osteonectin (Human) Rec.
00766-01-1000
1000 ug
1400.00
SPARC/Oosteonectin (Human),293 cell derived
10 ug
250.00
SPARC/Osteonectin (Rat), Rec. 00766-03-100 100 ug 360.00 
Anti SPARC/Osteonectin (Human) IgG
100 ug
220.00
Anti SPARC/Osteonectin (Human) IgG , Cy3 conjugated
A00766-01-50C3
50 ug
395.00
Anti SPARC/Osteonectin (Human) IgG , Cy5 conjugated
A00766-01-50C5
50 ug
395.00
Anti SPARC/Osteonectin (Human) IgG , FAM conjugated
A00766-01-50F
50 ug
360.00
Anti SPARC/Osteonectin (Human) IgG , Rhodamine B conjugated
A00766-01-50RH
50 ug
360.00
Anti SPARC/Osteonectin (Human) IgG , Biotinylated conjugated
50 ug
360.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
360.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
300.00
Anti SPARC/Osteonectin (Human) Monoclonal IgG, Biotinylated
A00766-04-50B
50 ug
395.00
Anti SPARC/Osteonectin (Human) Monoclonal IgG, Cy3 conjugated
A00766-04-50C3
50 ug
460.00
Anti SPARC/Osteonectin (Human) Monoclona lAntibody
100 ug
300.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
300.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
300.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
300.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
300.00
Anti SPARC/Osteonectin (Human) Monoclonal Antibody
100 ug
300.00
Anti Rat SPARC/Osteonectin IgG A00766-20-100 100 ug 300.00
Anti SPARC/Osteonectin (Rat) Monoclonal Antibody
100 ug
300.00
Anti SPARC/Osteonectin (Rat) Monoclonal Antibody
100 ug
300.00

1: Nie J,et al. Inactivation of SPARC enhances high-fat diet-induced obesity in mice. Connect Tissue Res. 2010 Jul 8. [Epub ahead of print]
2: Witkiewicz AK, et al. Stromal CD10 and SPARC expression in ductal carcinoma in situ (DCIS) patients predicts disease recurrence. Cancer Biol Ther. 2010 Aug 21;10(4). [Epub ahead of print]
3: Trombetta JM, Bradshaw AD. SPARC/osteonectin Functions to Maintain Homeostasis of the Collagenous Extracellular Matrix in the Periodontal Ligament. J Histochem  Cytochem. 2010 Jun 21. [Epub ahead of print]
4: Liang JF, et al. Relationship and prognostic significance of SPARC and VEGF protein expression in colon cancer. J Exp Clin Cancer Res. 2010 Jun 16;29:71. PubMed PMID: 20565704;
5: Miyoshi K, et al. SPARC mRNA expression as a prognostic marker for pancreatic adenocarcinoma patients. Anticancer Res. 2010 Mar;30(3):867-71.
6: Nagai MA, et al. Prognostic value of NDRG1 and SPARC protein expression in breast cancer patients. Breast Cancer Res Treat. 2010 Apr 6. [Epub ahead of print]
7: Hsiao YH, et al. SPARC (osteonectin) in  breast tumors of different histologic types and its role in the outcome of invasive ductal carcinoma. Breast J. 2010 May-Jun;16(3):305-8. Epub 2010 Feb 23.
8: Kos K, Wilding JP. SPARC: a key player in the pathologies associated with obesity and diabetes. Nat Rev Endocrinol. 2010 Apr;6(4):225-35. Epub 2010 Mar 2. Review.
9: Capper D, et al. Secreted protein, acidic and rich in cysteine (SPARC) expression in astrocytic tumour cells negatively correlates with proliferation, while vascular SPARC expression is associated with patient survival. Neuropathol Appl Neurobiol. 2010
Apr;36(3):183-97. Epub 2010 Feb 4.
10: Shen LC, et al. Expression of osteonectin/secreted protein acidic and rich in cysteine and matrix metalloproteinases in ameloblastoma. J Oral Pathol Med. 2010 Mar;39(3):242-9. Epub 2010 Jan 11.
11: Inoue M, et al. Identification of SPARC as a candidate target antigen for immunotherapy of
various cancers. Int J Cancer. 2010 Sep 1;127(6):1393-403.