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Onjisaponin B


  • Brand : BIOFRON

  • Catalogue Number : AV-H25205

  • Specification : 98%

  • CAS number : 35906-36-6

  • Formula : C75H112O35

  • Molecular Weight : 1573.69

  • PUBCHEM ID : 21669942

  • Volume : 20mg

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Catalogue Number


Analysis Method






Molecular Weight



White crystalline powder

Botanical Source

Polygala tenuifolia Willd./ Polygala senega and Polygala tenuifolia

Structure Type



Standards;Natural Pytochemical;API




6-Deoxy-α-L-mannopyranosyl-(1->3)-[β-D-galactopyranosyl-(1->4)-β-D-xylopyranosyl-(1->4)-6-deoxy-α-L-mannopyranosyl-(1->2)]-6-deoxy-1-O-[(2β,3β)-3-(β-D-glucopyranosyloxy)-2,23,27 -trihydroxy-23,28-dioxoolean-12-en-28-yl]-4-O-[(2E)-3-(4-methoxyphenyl)-2-propenoyl]-β-D-galactopyranose/onjisaponin B/Onjisaponin-B/β-D-Galactopyranose, O-6-deoxy-α-L-mannopyranosyl-(1->3)-O-[O-β-D-galactopyranosyl-(1->4)-O-β-D-xylopyranosyl-(1->4)-6-deoxy-α-L-mannopyranosyl-(1->2)]-6-deoxy-1-O-[(2β,3β)-3-(b η-D-glucopyranosyloxy)-2,23,27-trihydroxy-23,28-dioxoolean-12-en-28-yl]-4-O-[(2E)-3-(4-methoxyphenyl)-1-oxo-2-propen-1-yl]-


(2S,3R,4S,4aR,6aR,6bR,8aS,12aS,14aR,14bR)-8a-[(2S,3R,4S,5S,6R)-3-[(2S,3R,4S,5R,6S)-5-[(2S,3R,4R,5R)-3,4-dihydroxy-5-[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,4-dihydroxy-6-methyloxan-2-yl]oxy-5-[(E)-3-(4-methoxyphenyl)prop-2-enoyl]oxy-6-methyl-4-[(2S,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxyoxan-2-yl]oxycarbonyl-2-hydroxy-6b-(hydroxymethyl)-4,6a,11,11,14b-pentamethyl-3-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-1,2,3,4a,5,6,7,8,9,10,12,12a,14,14a-tetradecahydropicene-4-carboxylic acid


Onjisaponin B is a natural product derived from Radix Polygalae. Onjisaponin B enhances autophagy and accelerates the degradation of mutant α-synuclein and huntingtin in PC-12 cells, and exbibits potential therapeutic effects on Parkinson disease and Huntington disease[1].


1.5±0.1 g/cm3



Flash Point

Boiling Point

Melting Point



InChl Key


WGK Germany


HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:35906-36-6) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.




Salt plays an essential role in the progression of chronic kidney disease and hypertension. However, the mechanisms underlying pathogenesis of salt-induced kidney damage remain largely unknown. Here, Sprague-Dawley rats, that underwent 5/6 nephrectomy (5/6Nx, a model of advanced kidney damage) or sham operation, were treated for 2 weeks with a normal or high-salt diet. We employed aTiO2 enrichment, iTRAQ labeling and liquid-chromatography tandem mass spectrometry strategy for proteomic and phosphoproteomic profiling of the renal cortex. We found 318 proteins differentially expressed in 5/6Nx group relative to sham group, and 310 proteins significantly changed in response to salt load in 5/6Nx animals. Totally, 1810 unique phosphopeptides corresponding to 550 phosphoproteins were identified. We identified 113 upregulated and 84 downregulated phosphopeptides in 5/6Nx animals relative to sham animals. Salt load induced 78 upregulated and 91 downregulated phosphopeptides in 5/6Nx rats. The differentially expressed phospholproteins are important transporters, structural molecules, and receptors. Protein-protein interaction analysis revealed that the differentially phosphorylated proteins in 5/6Nx group, Polr2a, Srrm1, Gsta2 and Pxn were the most linked. Salt-induced differential phosphoproteins, Myh6, Lmna and Des were the most linked. Altered phosphorylation levels of lamin A and phospholamban were validated. This study will provide new insight into pathogenetic mechanisms of chronic kidney disease and salt sensitivity.

The prevention and treatment of chronic kidney disease has become one of the important public health problems in the world1, and advanced kidney damage with a severe decrease in the glomerular filtration rate is likely to be accompanied with the complications of kidney disease such as high blood pressure, anemia, bone disease, and cardiovascular diseases. Most advanced kidney damage patients suffer from varying degrees of hypertension, and persistent high blood pressure will accelerate the progress of chronic kidney disease, creating a vicious cycle. Therefore, actively controlling blood pressure has important implications for the treatment of advanced kidney damage2.

Salt is one of the most important environmental factors that promote the development of hypertension3. Since 1976, it has been well recognized that patients and animal models with advanced kidney damage are often salt sensitive4,5. Further, salt plays an essential role in the progression of chronic kidney disease, and prolonged salt load was known to cause renal injury including proteinuria, renal fibrosis and renal hypertrophy, in blood pressure-dependent and -independent ways6,7. Dietary salt restriction has been shown to reduce albuminuria, renal fibrosis and blood pressure8. However, the mechanisms underlying the pathogenesis of salt-induced kidney damage remain largely unknown.

Protein phosphorylation plays a key role in many cellular events including metabolism, secretion, homeostasis, transcriptional and translational regulation, and cellular signaling9. There is some evidence that phosphorylation of proteins and related phosphorylation events are essential to regulate renal signaling pathways such as transforming growth factor (TGF)-10, lysine deficient protein kinase (WNK)-11, arginine vasopressin (AVP)-associated ones12, which participate in the maintenance of renal function and the development of kidney diseases. However, the molecular details in such a process are not well understood. Hence, identifying phosphoproteins and phosphorylated molecules that might contribute to the salt sensitivity using large-scale and high throughput approaches may provide us an insightful understanding of salt sensitivity.

Mass spectrometry (MS)-based proteomics in combination with phosphoprotein enrichment technique has enabled us to globally analyze intracellular signaling events as well as the common post-translational modification-phosphorylation without prior knowledge of function or distribution13. Isobaric tags for relative and absolute quantification (iTRAQ) is a stable isotope-labeled, relative and absolute quantitative proteomics technology, with high accuracy and precision in quantification, higher repeatability and simultaneously quantitative analysis on multiple samples. Furthermore, due to the new stable isobaric labeling technique, iTRAQ has been applied more widely to study post-translational modifications than other proteomic approaches14. Several studies have been performed on quantitative phosphoproteomics of renal proximal and distal tubule15, renal collecting duct cells16, or renal thick ascending limb cells17. However, there are so far no phosphoproteomics studies on salt-induced kidney injury. Therefore, in this study, we aim to investigate proteomic and phosphoproteomic changes of renal cortex in a rat model of advanced kidney damage in response to salt load by using iTRAQ technology and TiO2 phosphopeptide enrichment method18 coupled with tandem MS [liquid chromatography (LC)-MS/MS]19,20,21.


Proteomic and phosphoproteomic analysis of renal cortex in a salt-load rat model of advanced kidney damage


Shaoling Jiang,1,* Hanchang He,2,* Lishan Tan,1 Liangliang Wang,3 Zhengxiu Su,1 Yufeng Liu,1 Hongguo Zhu,1 Menghuan Zhang,1 Fan Fan Hou,1 and Aiqing Lia,1

Publish date





CKD leads to disturbances in multiple interrelated hormones that regulate bone and mineral metabolism. The renal handling of mineral metabolism hormones in humans is incompletely understood. We determined the single-pass renal clearance of parathyroid hormone, fibroblast growth factor 23, vitamin D metabolites, and phosphate from paired blood samples collected from the abdominal aorta and renal vein in 17 participants undergoing simultaneous right and left heart catheterization and estimated associations of eGFR with the renal elimination of metabolites. The mean age ±SD of the study population was 71.4±10.0 years and 11 participants (65%) were male. We found a relatively large mean±SD single-pass renal extraction of parathyroid hormone (44.2%±10.3%) that exceeded the extraction of creatinine (22.1%±7.9%). The proportionate renal extraction of parathyroid hormone correlated with eGFR. The renal extraction of fibroblast growth factor 23 was, on average, lower than that of parathyroid hormone with greater variability across individuals (17.1%±19.5%). There were no differences in the mean concentrations of vitamin D metabolites across the renal vein and artery. In summary, we demonstrate substantial single-pass renal extraction of parathyroid hormone at a rate that exceeds glomerular filtration. Impaired renal clearance of parathyroid hormone may contribute to secondary hyperparathyroidism in CKD.


renal clearance, extraction, mineral metabolism biomarkers


Renal Clearance of Mineral Metabolism Biomarkers


Adriana J. van Ballegooijen,corresponding author* Eugene P. Rhee,†‡ Sammy Elmariah,§? Ian H. de Boer,* and Bryan Kestenbaum*

Publish date

2016 Feb




Tumor necrosis factor (TNF) receptor-associated factor-2 (TRAF2) binds to cIAP1 and cIAP2 (cIAP1/2) and recruits them to the cytoplasmic domain of several members of the TNF receptor (TNFR) superfamily, including the TNF-TNFR1 ligand-receptor complex. Here, we define a cIAP1/2-interacting motif (CIM) within the TRAF-N domain of TRAF2, and we use TRAF2 CIM mutants to determine the role of TRAF2 and cIAP1/2 individually, and the TRAF2-cIAP1/2 interaction, in TNFR1-dependent signaling. We show that both the TRAF2 RING domain and the TRAF2 CIM are required to regulate NF-κB-inducing kinase stability and suppress constitutive noncanonical NF-κB activation. Conversely, following TNFR1 stimulation, cells bearing a CIM-mutated TRAF2 showed reduced canonical NF-κB activation and TNF-induced RIPK1 ubiquitylation. Remarkably, the RING domain of TRAF2 was dispensable for these functions. However, like the TRAF2 CIM, the RING domain of TRAF2 was required for protection against TNF-induced apoptosis. These results show that TRAF2 has anti-apoptotic signaling roles in addition to promoting NF-κB signaling and that efficient activation of NF-κB by TNFR1 requires the recruitment of cIAP1/2 by TRAF2.


TRAF2 Must Bind to Cellular Inhibitors of Apoptosis for Tumor Necrosis Factor (TNF) to Efficiently Activate NF-κB and to Prevent TNF-induced ApoptosisAn external file that holds a picture, illustration, etc. Object name is sbox.jpg


James E. Vince,‡,1 Delara Pantaki,‡ Rebecca Feltham,‡ Peter D. Mace,§,2 Stephanie M. Cordier,¶ Anna C. Schmukle,¶ Angelina J. Davidson,‡ Bernard A. Callus,‡,3 Wendy Wei-Lynn Wong,‡ Ian E. Gentle,‡ Holly Carter,‡ Erinna F. Lee,?,4 Henning Walczak,¶ Catherine L. Day,§ David L. Vaux,‡,5 and John Silke‡,6

Publish date

2009 Dec 18;