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  • Brand : BIOFRON

  • Catalogue Number : BN-O1093

  • Specification : 98%(HPLC)

  • CAS number : 2162-74-5

  • Formula : C25H34N2

  • Molecular Weight : 362.5

  • PUBCHEM ID : 75100

  • Volume : 5mg

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Catalogue Number


Analysis Method





Molecular Weight



Botanical Source

Structure Type





N,N'-Methanetetraylbis(2,6-bis(1-methylethyl)benzenamine)/di-(2,6-di-isopropylphenyl)-carbodiimide/DiipNCNDiip/N,N'-Bis(2,6-diisopropylphenyl)carbodiimide/Staboxol 1/Bis(2,6-diisopropylphenyl)carbodiimide/DipN=C=NDip/Carbodiimide,bis(2,6-diisopropylphenyl)-(7CI,8CI)/benzenamine, N-[[2,6-bis(1-methylethyl)phenyl]carbonimidoyl]-2,6-bis(1-methylethyl)-/N,N'-bis(2,6-diisopropylphenyl) carbodiimide/Benzenamine, N,N'-methanetetraylbis[2,6-bis(1-methylethyl)-/N,N'-bis[2,6-di(propan-2-yl)phenyl]carbodiimide/2,2',6,6'-Tetraisopropyldiphenylcarbodiimide/N,N'-Methanediylidenebis(2,6-diisopropylaniline)/Carbo D



1.0±0.1 g/cm3


Flash Point

235.6±29.6 °C

Boiling Point

477.7±45.0 °C at 760 mmHg

Melting Point

49 - 51ºC


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#:2162-74-5) 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.




A conditional lethal, temperature-sensitive mutant of vaccinia, defective in assembly of the virus envelope and maturation, was characterized and shown to mimic exactly the aberrations produced by rifampicin. Analyses of the infection at restrictive and permissive temperatures were conducted with electron microscopy, isotopic pulse-chase experiments in which polypeptides were separated by polyacrylamide slab gels, and assays of core enzymatic activities. The data collected by several approaches reveal that assembly and maturation of vaccinia involves a tightly coupled sequence of interrelated events including the assembly of the envelope, post-translational cleavage of several virion polypeptides, and induction of the core enzymes.


Biogenesis of poxviruses: analysis of the morphogenetic sequence using a conditional lethal mutant defective in envelope self-assembly.


W Stern, B G Pogo, and S Dales

Publish date

1977 May




The intercellular transfer of alpha-synuclein (α-syn) has been implicated in the progression of Parkinson’s disease (PD) and multiple system atrophy (MSA). The cellular mechanisms underlying this process are now beginning to be elucidated. In this study, we demonstrate that the gap junction protein connexin-32 (Cx32) is centrally involved in the preferential uptake of α-syn oligomeric assemblies (oα-syn) in neurons and oligodendrocytes. In vitro, we demonstrate a clear correlation between Cx32 expression and oα-syn uptake. Pharmacological and genetic strategies targeting Cx32 successfully blocked oα-syn uptake. In cellular and transgenic mice modeling PD and MSA, we observed significant upregulation of Cx32 which correlates with α-syn accumulation. Notably, we could also demonstrate a direct interaction between α-syn and Cx32 in two out of four human PD cases that was absent in all four age-matched controls. These data are suggestive of a link between Cx32 and PD pathophysiology. Collectively, our results provide compelling evidence for Cx32 as a novel target for therapeutic intervention in PD and related α-synucleinopathies.

Electronic supplementary material
The online version of this article (10.1007/s00401-019-02007-x) contains supplementary material, which is available to authorized users.


Parkinson’s disease (PD), Multiple system atrophy (MSA), Alzheimer’s disease (AD), Cell-to-cell transfer, Prion-like transfer, Gap junction proteins, Cx32, GJB1, alpha-Synuclein (α-syn)


Binding of α-synuclein oligomers to Cx32 facilitates protein uptake and transfer in neurons and oligodendrocytes


Juan F. Reyes, Christopher Sackmann, Alana Hoffmann, Per Svenningsson, Jurgen Winkler, Martin Ingelsson, Martin Hallbeck

Publish date





Studies conducted over the last decade demonstrated variable therapeutic efficacy of angiotensin converting enzyme (ACE) inhibitor on the progression of glomerular diseases, including IgA nephropathy. In this study, among patients with biopsy-proven IgA nephropathy, 53 patients in whom creatinine clearance had been monitored over 5 yr were recruited for study. These patients were classified into two groups according to whether or not renal function had declined as determined by the slope of creatinine clearance against time: group 1 had stable renal function; group 2 had declining renal function (average: -6.7 +/- 1.3 ml/min/yr). 21 of 53 patients were treated with ACE inhibitor and followed for 48 wk. Gene polymorphism consisting of insertion (I) or deletion (D) of a 287-bp DNA fragment (presumed to be a silencer element) of the ACE gene was determined by PCR. 46 age-matched individuals without history of proteinuria were analyzed as controls. The DD genotype was significantly more frequent in group 2 (43%) than in controls (7%) or group 1 patients with stable renal function (16%). 48 wk after ACE inhibitor administration, proteinuria significantly decreased in patients with DD genotype but not in those with ID or II genotypes. The results indicate that deletion polymorphism in the ACE gene, particularly the homozygote DD, is a risk factor for progression to chronic renal failure in IgA nephropathy. Moreover, this deletion polymorphism predicts the therapeutic efficacy of ACE inhibition on proteinuria and, potentially, on progressive deterioration of renal function.


Role of the deletion of polymorphism of the angiotensin converting enzyme gene in the progression and therapeutic responsiveness of IgA nephropathy.


H Yoshida, T Mitarai, T Kawamura, T Kitajima, Y Miyazaki, R Nagasawa, Y Kawaguchi, H Kubo, I Ichikawa, O Sakai

Publish date

1995 Nov;

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