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N-Benzyloleamide

$655

  • Brand : BIOFRON

  • Catalogue Number : AV-B04360

  • Specification : 95%

  • CAS number : 101762-87-2

  • Formula : C25H41NO

  • Molecular Weight : 371.6

  • PUBCHEM ID : 49865534

  • Volume : 5mg

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Catalogue Number

AV-B04360

Analysis Method

HPLC,NMR,MS

Specification

95%

Storage

2-8°C

Molecular Weight

371.6

Appearance

Powder

Botanical Source

Structure Type

Aliphatics

Category

Standards;Natural Pytochemical;API

SMILES

CCCCCCCCC=CCCCCCCCC(=O)NCC1=CC=CC=C1

Synonyms

(9Z)-N-Benzyl-9-octadecenamide/9-Octadecenamide, N-(phenylmethyl)-, (9Z)-/N-Benzyloctadecenamide

IUPAC Name

(Z)-N-benzyloctadec-9-enamide

Density

0.923±0.06 g/cm3

Solubility

Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.

Flash Point

330.9±12.0 °C

Boiling Point

534.2±39.0 °C at 760 mmHg

Melting Point

58-59 ºC

InChl

InChI=1S/C25H41NO/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-19-22-25(27)26-23-24-20-17-16-18-21-24/h9-10,16-18,20-21H,2-8,11-15,19,22-23H2,1H3,(H,26,27)/b10-9-

InChl Key

QHXGFOCPQQADIF-KTKRTIGZSA-N

WGK Germany

RID/ADR

HS Code Reference

2933990000

Personal Projective Equipment

Correct Usage

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

Meta Tag

provides coniferyl ferulate(CAS#:101762-87-2) 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.

PMID

30884364

Abstract

Although experimental studies have shown that global cerebral hypoperfusion leads to amyloid deposition in the hemisphere with carotid artery occlusion in rodents, the results of such occurrence are controversial in humans. Hence, we aim to determine whether global cerebral hypoperfusion leading to decreased blood flow relative to metabolic demand [increased oxygen extraction fraction (OEF), misery perfusion] is associated with increases in amyloid deposition in the hemisphere with atherosclerotic major cerebral artery disease in patients. We evaluated the distribution of β-amyloid plaques using positron emission tomography and a [18F]-pyridylbenzofuran derivative (18F-FPYBF-2) in 13 patients with unilateral atherosclerotic disease of the internal carotid artery (ICA) or middle cerebral artery (MCA) disease and no cortical infarction. The distribution volume ratio (DVR) of 18F- FPYBF-2 was calculated using dynamic data and Logan graphical analysis with reference tissue and was correlated with the cerebral blood flow (CBF), cerebral metabolic rate of oxygen (CMRO2), and OEF, obtained from 15O-gas PET. The mean cortical value was calculated as the mean value within the frontal, posterior cingulate, precuneus, parietal, and lateral temporal cortical regions. Significant reductions in CBF and CMRO2 and increases in OEF were found in the hemisphere ipsilateral to the arterial lesion compared with the contralateral hemisphere. There was no significant difference for 18F-FPYBF-2 DVR between hemispheres. The ipsilateral to contralateral ratio of the 18F- FPYBF-2 DVR was increased in 3 patients, while the ipsilateral to contralateral OEF ratio was increased in 4 patients. The incidence of an increased hemispheric DVR ratio was significantly higher in patients with an increased hemispheric OEF ratio (3/4) than in patients without (0/9) (p?

KEYWORDS

Amyloid, Cerebrovascular disease, Positron emission tomography, Misery perfusion

Title

Misery perfusion and amyloid deposition in atherosclerotic major cerebral artery disease

Author

Hiroshi Yamauchi,a,? Shinya Kagawa,a Masaaki Takahashi,a Naoya Oishi,b Masahiro Ono,c and Tatsuya Higashia,d

Publish date

2019;

PMID

31594538

Abstract

Background
The stability of p53 is mainly controlled by ubiquitin-dependent degradation, which is triggered by the E3 ubiquitin ligase MDM2. The chromatin modifier lymphoid-specific helicase (LSH) is essential for DNA methylation and cancer progression as a transcriptional repressor. The potential interplay between chromatin modifiers and transcription factors remains largely unknown.

Results
Here, we present data suggesting that LSH regulates p53 in cis through two pathways: prevention proteasomal degradation through its deubiquitination, which is achieved by reducing the lysine 11-linked, lysine 48-linked polyubiquitin chains (K11 and K48) on p53; and revival of the transcriptional activity of p53 by forming a complex with PKM2 (pyruvate kinase 2). Furthermore, we confirmed that the LSH-PKM2 interaction occurred at the intersubunit interface region of the PKM2 C-terminal region and the coiled-coil domains (CC) and ATP-binding domains of LSH, and this interaction regulated p53-mediated transactivation in cis in lipid metabolism, especially lipid catabolism.

Conclusion
These findings suggest that LSH is a novel regulator of p53 through the proteasomal pathway, thereby providing an alternative mechanism of p53 involvement in lipid metabolism in cancer.

Title

LSH, P53, DUB, PKM2, Lipid metabolism

Author

DNA methylation modifier LSH inhibits p53 ubiquitination and transactivates p53 to promote lipid metabolism

Publish date

Ling Chen,1,2,3,8 Ying Shi,1,2 Na Liu,1,2 Zuli Wang,1,2 Rui Yang,1,2 Bin Yan,1,2,4 Xiaoli Liu,1,2 Weiwei Lai,1,2 Yating Liu,1,2 Desheng Xiao,5 Hu Zhou,6 Yan Cheng,7 Ya Cao,1,2 Shuang Liu,4 Zanxian Xia,corresponding author8,9 and Yongguang Taocorresponding author1,2,3,4,5

PMID

25860929

Abstract

FBXW7 mutations occur in a variety of human cancers including colorectal cancer (CRC). Elucidating its mechanism of action has become crucial for cancer therapy; however, it is also complicated by the fact that FBXW7 can influence many pathways due to its role as an E3-ubiquitin ligase in proteasome degradation. FBXW7 and TP53 are tumour suppressors intensively implicated in colorectal carcinogenesis. Deletion mutations in these two genes in animal models mark the progression from adenoma to carcinoma. Although still largely unknown, the last defense mechanism against CRC at the molecular level could be through a synergistic effect of the two genes. The underlying mechanism requires further investigation. In our laboratory, we have used a phospho-kinase profiler array to illustrate a potential molecular link between FBXW7 and p53 in CRC cells. In vitro and in vivo assessments demonstrated aberrant induction of phosphorylated p53 at Serine 15 [phospho-p53(Ser15)] in human FBXW7-deficient CRC cells as compared to their FBXW7-wild-type counterparts. FBXW7 loss in HCT116 cells promoted resistance to oxaliplatin. Immunoblotting data further confirmed that reduction of phospho-p53(Ser15) may contribute to the decreased efficacy of therapy in FBXW7-mutated CRC cells. The findings may suggest the applicability of phospho-p53(Ser15) as an indicative marker of FBXW7-mutations. Phospho-p53(Ser15) regulation by FBXW7 E3-ligase activity could provide important clues for understanding FBXW7 behavior in tumour progression and grounds for its clinical applicability thereafter.

KEYWORDS

FBXW7, phopsho-P53(Ser15), colorectal cancer, drug resistance, CK1α

Title

FBXW7-mutated colorectal cancer cells exhibit aberrant expression of phosphorylated-p53 at Serine-15

Author

Ningning Li,#1,2 Federica Lorenzi,#1 Eliana Kalakouti,#1,3 Makhliyo Normatova,1 Roya Babaei-Jadidi,1 Ian Tomlinson,4 and Abdolrahman S. Nateri1

Publish date

2015 Apr 20


Description :

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