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
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.
3927303
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.
A nonmitogenic pituitary function of fibroblast growth factor: regulation of thyrotropin and prolactin secretion.
A Baird, P Mormede, S Y Ying, W B Wehrenberg, N Ueno, N Ling, and R Guillemin
1985 Aug;
3039460
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.
Site-specific DNA binding of nuclear factor I: effect of the spacer region.
R M Gronostajski
1987 Jul 24;
2848008
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.
Cytochrome components of nitrate- and sulfate-respiring Desulfovibrio desulfuricans ATCC 27774.
M C Liu, C Costa, I B Coutinho, J J Moura, I Moura, A V Xavier, and J LeGall
1988 Dec;
