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Chimonanthine

$1,120

  • Brand : BIOFRON

  • Catalogue Number : BD-P0234

  • Specification : 99.0%(HPLC)

  • CAS number : 5545-89-1

  • Formula : C22H26N4

  • Molecular Weight : 346.48

  • PUBCHEM ID : 3083909

  • Volume : 25mg

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Catalogue Number

BD-P0234

Analysis Method

HPLC,NMR,MS

Specification

99.0%(HPLC)

Storage

2-8°C

Molecular Weight

346.48

Appearance

Powder

Botanical Source

Structure Type

Alkaloids

Category

SMILES

CN1CCC2(C1NC3=CC=CC=C32)C45CCN(C4NC6=CC=CC=C56)C

Synonyms

(3aS,8bS)-8b-[(3aS,8bS)-3-methyl-1,2,3a,4-tetrahydropyrrolo[2,3-b]indol-8b-yl]-3-methyl-1,2,3a,4-tetrahydropyrrolo[2,3-b]indole

IUPAC Name

(3aS,8bS)-8b-[(3aS,8bS)-3-methyl-1,2,3a,4-tetrahydropyrrolo[2,3-b]indol-8b-yl]-3-methyl-1,2,3a,4-tetrahydropyrrolo[2,3-b]indole

Applications

Density

Solubility

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

Flash Point

Boiling Point

Melting Point

InChl

InChI=1S/C22H26N4/c1-25-13-11-21(15-7-3-5-9-17(15)23-19(21)25)22-12-14-26(2)20(22)24-18-10-6-4-8-16(18)22/h3-10,19-20,23-24H,11-14H2,1-2H3/t19-,20-,21+,22+/m0/s1

InChl Key

HOYXPMHLHJOGHD-FNAHDJPLSA-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#:5545-89-1) 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

3927303

Abstract

The addition of fibroblast growth factor (FGF) to primary cultures of rat anterior pituitary cells modifies their response to thyrotropin-releasing factor in a dose-dependent manner. While the pituitary response to the other releasing factors (corticotropin-releasing factor, growth hormone-releasing factor, and gonadotropin-releasing factor) is not altered, FGF increases both the sensitivity of the cells to thyrotropin-releasing factor and the amounts of prolactin and thyrotropin released. A minimum of 24 hr of preincubation with FGF is required to modify the pituitary response, and maximal effects were observed with 48 and 72 hr of preincubation. The effective doses of FGF are similar to those described for its mitogenic activity (i.e., 1-100 pM), but inhibition of cell growth with 5-fluorodeoxyuridine does not modify the effect of FGF on thyrotropin and prolactin release. These results suggest a novel paracrine, if not autocrine, role of pituitary FGF in the homeostatic mechanisms that regulate the secretion of prolactin and thyrotropin. They also suggest that the biological significance of the presence of FGF in various tissues may not be directly related to its in vitro mitogenic activity.

Title

A nonmitogenic pituitary function of fibroblast growth factor: regulation of thyrotropin and prolactin secretion.

Author

A Baird, P Mormede, S Y Ying, W B Wehrenberg, N Ueno, N Ling, and R Guillemin

Publish date

1985 Aug;

PMID

3039460

Abstract

This article has been cited by other articles in PMC.
Abstract
Nuclear factor I (NFI) is a site-specific DNA binding protein required for the replication of adenovirus type 2 DNA in vitro and in vivo. To study sequence requirements for the interaction of NFI with DNA, we have measured the binding of the protein to a variety of synthetic sites. Binding sites for NFI (FIB sites) were previously shown to contain a consensus sequence composed of 2 motifs, TGG (Motif 1), and GCCAA (Motif 2), separated by a 6 or 7bp spacer region. To assess conserved sequences in the spacer region and flanking sequences which affect NFI binding, we have isolated clones from oligonucleotide libraries that contain the two motifs flanked by 3 degenerate nucleotides and separated by degenerate spacer regions of 6 or 7 nucleotides. With a 6bp spacer region, a strong bias exists for a C or A residue in the first position of the spacer. Sites with a 7bp spacer region contain a G and C or A residue at the first and second positions, respectively, of the spacer, but also possess conserved residues at other positions of the site.

Title

Site-specific DNA binding of nuclear factor I: effect of the spacer region.

Author

R M Gronostajski

Publish date

1987 Jul 24;

PMID

2848008

Abstract

Three multiheme c-type cytochromes–the tetraheme cytochrome c3 (molecular weight [MW] 13,500), a dodecaheme cytochrome c (MW 40,800), and a “split-Soret” cytochrome c (MW 51,540), which is a dimer with 2 hemes per subunit (MW 26,300)–were isolated from the soluble fraction of Desulfovibrio desulfuricans (ATCC 27774) grown under nitrate- or sulfate-respiring conditions. Two of them, the dodecaheme and the split-Soret cytochromes, showed no similarities to any of the c-type cytochromes isolated from other sulfate-reducing bacteria, while the tetraheme cytochrome c3 appeared to be analogous to the cytochrome c3 found in other sulfate-reducing bacteria. For all three multiheme c-type cytochromes isolated, the homologous proteins from nitrate- and sulfate-grown cells were indistinguishable in amino acid composition, physical properties, and spectroscopic characteristics. It therefore appears that the same c-type cytochrome components are present when D. desulfuricans ATCC 27774 cells are grown under either condition. This is in contrast to the considerable difference found in Pseudomonas perfectomarina (Liu et al., J. Bacteriol. 154:278-286, 1983), a marine denitrifier, when the cells are grown on nitrate or oxygen as the terminal electron acceptor. In addition, two spectroscopy methods capable of revealing minute structural variations in proteins provided identical information about the tetraheme cytochrome c3 from nitrate-grown and sulfate-grown cells.

Title

Cytochrome components of nitrate- and sulfate-respiring Desulfovibrio desulfuricans ATCC 27774.

Author

M C Liu, C Costa, I B Coutinho, J J Moura, I Moura, A V Xavier, and J LeGall

Publish date

1988 Dec;