Recombinant Human SPARC Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0440NP
BL-0440NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0440NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human SPARC Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0440NP
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Product Overview

Description Recombinant Human Secreted Protein Acidic and Rich in Cysteine is produced by our Mammalian expression system and the target gene encoding Ala18-Ile303 is expressed with a 6His tag at the C-terminus.
Accession P09486
Synonym SPARC; Basement-Membrane Protein 40; BM-40; Osteonectin; ON; Secreted Protein Acidic and Rich in Cysteine; SPARC; ON
Gene Background Secreted Protein Acidic and Rich in Cysteine (SPARC) is a secreted, evolutionarily conserved collagen-binding glycoprotein and belongs to the SPARC family. SPARC has 286 amino acids and contains an EF-hand in C-termina domain, a follistatin-like domain with Kazal-like sequences. There are two calcium binding sites, one binds 5 - 8 Ca2+ with a low affinity and other on an EF-hand loop that binds a Ca2+ ion with a high affinity. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC regulate cell growth through interactions with the extracellular matrix (ECM) and cytokines. SPARC bind to numerous proteins of the ECM, affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC also binds several types of collagen, albumin, thrombospondin, PDGF and cell membranes.
Molecular Mass 33.73 KDa
Apmol Mass 36 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function 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.
Subcellular Location Secreted, extracellular space, extracellular matrix, basement membrane. Note=In or around the basement membrane.
Protein Families SPARC family
Database References
Associated Diseases Osteogenesis imperfecta 17 (OI17)

Gene Functions References

  1. Hepatic SPARC expression is associated with liver injury and fibrogenic processes in non-alcoholic fatty liver disease. PMID: 29335425
  2. Plasma samples from lung cancer patients and healthy heavy-smokers controls were tested for levels of COL11A1 and COL10A1 (n = 57 each) and SPARC (n = 90 each). Higher plasma levels of COL10A1 were detected in patients (p PMID: 30227835
  3. The authors have confirmed the presence of SPARC expression in melanoma, Kaposi sarcomas (KS), leiomyosarcomas (LMS) and angiosarcomas (AS) and also detected it for the first time in atypical fibroxanthomas (AFX). PMID: 29660567
  4. Results revealed that hypermethylation of the SPARC promoter was the primary mechanism of SPARC downregulation in prostate cancer. SPARC expression was frequently lost during the promoter hypermethylation but could be restored by 5-Aza-Cdr. PMID: 29207175
  5. Stromal SPARC expression was a useful biomarker for predicting prognosis in patients with resected pancreatic ductal adenocarcinoma. PMID: 29295776
  6. SPARC is closely related to the development of breast cancer and can be used as a tumor marker for breast cancer recurrence. PMID: 29237913
  7. SPARC expression was inversely associated with the degree of malignancy and it had a negative correlation with VEGF-C and VEGF-D expression. Results suggest SPARC might function as a tumor suppressor inhibiting angiogenesis and lymphangiogenesis in ovarian cancer by reducing the expression of VEGF-C and VEGF-D. PMID: 29075785
  8. SPARC may be involved in gastric cancer metastasis by effecting on tumor microenvironment PMID: 29077165
  9. SPARC treatment enhances the epithelial mesenchymal transition signaling pathway via activation of AKT, and exogenous SPARC and tumor expressing SPARC might be associated with tumor progression in head and neck cancers. PMID: 28718842
  10. The epicardial adipose tissue expresses the mRNA of osteopontin, osteoprotegerin, and osteonectin genes that have been implicated in the calcification process; such expression is statistically associated with some components of HDL subclasses in coronary artery disease patients. PMID: 28821297
  11. detection of SPARC mRNA and protein expression levels may facilitate early diagnosis and prognosis assessment of esophageal squamous cell carcinoma. PMID: 28713937
  12. SPARC rs17718347 and rs2347128 single nucleotide polymorphisms are associated with progression-free survival in locally advanced and metastatic pancreatic cancer patients. PMID: 28687963
  13. results demonstrated that loss of miR-211 expression and thus uncontrolled SPARC overexpression might drive progression of hepatocellular carcinoma (HCC), which may provide a novel therapeutic strategy for the treatment of HCC. PMID: 27230656
  14. Data suggest that plasma SPARC levels may be biomarker for vascular complications among Chinese type 2 diabetic patients; patients in lowest SPARC tertile have increased odds of aortic stiffness but reduced odds of peripheral arterial disease. PMID: 28479157
  15. The profiled circulating tumour cells also expressed elevated levels of stem cell markers, and the extracellular matrix protein, SPARC. The expression of SPARC might correspond to an epithelial-mesenchymal transition in pancreatic circulating tumour cells PMID: 28569190
  16. Data suggest that both osteonectin and FGF21 levels in serum are associated with early nephropathy in type 2 diabetes, albeit with different patterns; persistent hyperglycemia may inhibit bone formation leading to osteoporosis. (FGF21 = fibroblast growth factor 21) PMID: 27916484
  17. These results suggest that increased SPARC expression may be an indicator of greater aggressiveness, and may serve as a prognostic factor for triple-negative breast cancer. PMID: 27421134
  18. High expression of SPARC is related to worse prognosis in rectal cancer patients. PMID: 28009327
  19. Tumors with stroma-derived SPARC displayed suppressed growth, inhibited angiogenesis and increased lipid accumulation. Based on the described chaperone function of SPARC, authors hypothesized that SPARC binds albumin complexed with fatty acids and transports them to tumors. PMID: 27776337
  20. Weekly NAB-paclitaxel might be effective for heavily pretreated non-small-cell lung cancer patients. SPARC expression in tumor stroma cells might be a potential negative predictor of NAB-paclitaxel. PMID: 28304139
  21. SPARC-associated signaling pathways are associated with lymphangiogenesis and lymph node metastases of hypopharyngeal cancer. PMID: 29374693
  22. Stromal SPARC expression correlated with the prognosis of patients with resectable biliary carcinoma, and its significance was enhanced in patients treated with adjuvant gemcitabine-based chemotherapy. PMID: 28342122
  23. Studies revealed that SPARC plays a critical role in regulating bone remodeling and maintaining bone mass and quality. The mechanisms by which SPARC influences bone formation, maintenance, and repair might occur through multiple pathways that include the regulation of procollagen processing and assembly in the bone matrix, crosslinking, mineralization, and/or osteoblast/osteoclast differentiation and activity. [review] PMID: 26851678
  24. This study indicates that germline PTCH1 heterozygous mutations play a major role in bone metabolism in patients with NBCCS, in particular in those with PTCH1 protein truncation mutations. SPARC may represent an important downstream modulator of PTCH1 mediation of bone metabolism. PMID: 26890308
  25. The SPARC drives pathological responses in non-small cell lung cancer and idiopathic pulmonary fibrosis by promoting microvascular remodelling and excessive deposition of ECM proteins. PMID: 27759879
  26. proCOL11A1, fibroblast-activated protein, secreted protein acidic and rich in cysteine, and periostin expression was significantly increased in the intratumoral stroma of pancreatic ductal adenocarcinomas compared to paired non-neoplastic pancreata PMID: 29025374
  27. The mRNA and protein levels of SPARC were 5.78-fold higher in cancer tissues compared with the case-matched normal epithelium. High expression levels of SPARC in esophageal squamous cell carcinoma parenchyma were related to lymph node metastasis and poor prognosis (p = 0.049 and p = 0.04). PMID: 28818666
  28. SPARC can serve a dual function role as both predictor for prognosis and potentially biomarker for lymph node metastasis in resected pancreatic cancer patients. PMID: 28119265
  29. SPARC appears to be an important modulator of the actin cytoskeleton, implicating maintenance of muscular function PMID: 27908613
  30. that SPARC-mediated degradation of the extracellular matrix, and its possible association with MMPs, might contribute to progression of phyllodes tumors PMID: 27909812
  31. WIN-dependent increase in the level of SPARC plays a critical role in sensitizing osteosarcoma cells to TRAIL action PMID: 26698404
  32. high SPARC-expression was a significant predictor of poor OS in HPV-negative OPSCC patients using Kaplan-Meier analysis and the log-rank test PMID: 26523779
  33. We identified five new biomarkers: GDF15, osteonectin, TRAP5, TWEAK, and YKL40 as being promising markers for monitoring bone metastases. PMID: 27069189
  34. SPARC levels were not associated with efficacy in patients with MPC. This exploratory analysis does not support making treatment decisions regarding nab-paclitaxel plus gemcitabine or gemcitabine alone in MPC based on SPARC expression. PMID: 26169969
  35. CD90 is upregulated in gastric cancer and inhibits gastric cancer cell apoptosis by modulating the expression level of SPARC protein. PMID: 26329007
  36. SPARC might be an unfavorable indicator in patients with pancreatic cancer, especially in the stroma.[Review] PMID: 26731428
  37. tracheal aspirate SPARC levels predicted development of bronchopulmonary dysplasia or death. PMID: 26656750
  38. SPARC is associated with carcinogenesis of oral squamous epithelium. PMID: 25311631
  39. Studies indicate that SPARC (secreted protein acidic and rich in cysteine) gene is involved in the development and progression of pancreatic ductal adenocarcinoma (PDAC). PMID: 26335014
  40. MLKL upregulation in SPARC overexpressed cells treated with Ara-C, indicates necrosis as a possible cell death process for the SKM-1 cells under these stringent conditions. PMID: 26165695
  41. up-regulation of SPARC by oxLDL is independent of Runx2, and it may be mediated by other transcription factors PMID: 26025968
  42. Tumor-produced SPARC and VCAM1 are regulators of cancer extravasation. PMID: 25925867
  43. miR-29a and miR-29b enhance cell migration and invasion in nasopharyngeal carcinoma progression by regulating SPARC and COL3A1 gene expression. PMID: 25786138
  44. SNP1599 differentially regulates osteonectin expression and contributes to variability in bone mass, by a mechanism that may involve differential targeting by miR-433 PMID: 25262637
  45. Reduced expression of SPARC in colorectal cancer tissue is associated with poor prognosis and aggressive clinicopathological features. PMID: 26044224
  46. Three functional SPARC SNPs are associated with an increased risk of coal workers' pneumoconiosis in a Chinese population. PMID: 25126876
  47. reduced expression in the bone marrow biopsy specimen in patients with aplastic anemia PMID: 25032754
  48. SPARC promoter methylation as an important factor in the tumorigenesis of gastric carcinomas. PMID: 25516351
  49. SCD5 impairs SPARC and cathepsin B secretion in human melanoma cells and intracellular pH acidification. PMID: 25802234
  50. High SPARC expression of the primary tumor is associated with a higher chance of achieving a pathological complete remission after TAC or TAC-NX chemotherapy. PMID: 25355716

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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