D6135
Distamycin A hydrochloride from Streptomyces distallicus
≥90% (TLC)
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About This Item
Empirical Formula (Hill Notation):
C22H27N9O4 · HCl
CAS Number:
Molecular Weight:
517.97
EC Number:
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
Recommended Products
Assay
≥90% (TLC)
Mode of action
DNA synthesis | interferes
storage temp.
−20°C
SMILES string
Cl.Cn1cc(NC=O)cc1C(=O)Nc2cc(C(=O)Nc3cc(C(=O)NCCC(N)=N)n(C)c3)n(C)c2
Biochem/physiol Actions
Reported to specifically inhibit the initiation of RNA synthesis.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Terri G Edwards et al.
Antiviral research, 91(2), 177-186 (2011-06-15)
Human papillomavirus (HPV) causes cervical cancer and other hyperproliferative diseases. There currently are no approved antiviral drugs for HPV that directly decrease viral DNA load and that have low toxicity. We report the potent anti-HPV activity of two N-methylpyrrole-imidazole polyamides
Gaetano Marverti et al.
Amino acids, 42(2-3), 641-653 (2011-08-05)
Acquired resistance to cisplatin (cDDP) is a multifactorial process that represents one of the main problems in ovarian cancer therapy. Distamycin A is a minor groove DNA binder whose toxicity has limited its use and prompted the synthesis of derivatives
Vivian Chagas da Silveira et al.
Journal of inorganic biochemistry, 105(12), 1692-1703 (2011-11-22)
Previous studies on copper(II) complexes with oxindole-Schiff base ligands have shown their potential antitumor activity towards different cells, inducing apoptosis through a preferential attack to DNA and/or mitochondria. Herein, we better characterize the interactions between some of these copper(II) complexes
Mariko Asagi et al.
Biophysical chemistry, 149(1-2), 34-39 (2010-04-17)
Distamycin A (Dst) is an antibiotic which binds to the minor groove of double-stranded DNA at A/T-rich regions. We have examined the affinity and mode of Dst binding to DNA duplexes containing a conserved A/T core and variable terminal A/T
Austin E Smith et al.
Biochemistry, 50(38), 8107-8116 (2011-08-23)
The molecular mechanism for the displacement of HMGA1 proteins from DNA is integral to disrupting their cellular function, which is linked to many metastatic cancers. Chemical shift and NOESY NMR experiments provide structural evidence for the displacement of an AT
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