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K3763

Kanamycin sulfate from Streptomyces kanamyceticus

Name: Kanamycin sulfate from <I>Streptomyces kanamyceticus</I>
Brand: SIGMA

Biotechnology Performance Certified, suitable for cell culture

Synonym(s):

Kanamycin A, Kanamycin sulfate salt

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About This Item

Empirical Formula (Hill Notation):

C₁₈H₃₆N₄O₁₁ · H₂O₄S

CAS Number:

25389-94-0

Molecular Weight:

582.58

EC Number:

246-933-9

UNSPSC Code:

51101500

MDL number:

MFCD00070253

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grade

Biotechnology Performance Certified

technique(s)

cell culture | mammalian: suitable

impurities

endotoxin, tested

antibiotic activity spectrum

mycobacteria

mode of action

protein synthesis | interferes

storage temp.

2-8°C

SMILES string

OS(O)(=O)=O.NC[C@H]1O[C@H](O[C@@H]2[C@@H](N)C[C@@H](N)[C@H](O[C@H]3O[C@H](CO)[C@@H](O)[C@H](N)[C@H]3O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O

InChI

1S/C18H36N4O11.H2O4S/c19-2-6-10(25)12(27)13(28)18(30-6)33-16-5(21)1-4(20)15(14(16)29)32-17-11(26)8(22)9(24)7(3-23)31-17;1-5(2,3)4/h4-18,23-29H,1-3,19-22H2;(H2,1,2,3,4)/t4-,5+,6-,7-,8+,9-,10-,11-,12+,13-,14-,15+,16-,17-,18-;/m1./s1

InChI key

OOYGSFOGFJDDHP-KMCOLRRFSA-N

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General description

Chemical structure: aminoglycoside

Application

Use in biotechnology applications to inhibit protein synthesis.

Biochem/physiol Actions

Mode of Action: The product acts by binding to the 70S ribosomal subunit, inhibiting translocation and eliciting miscoding.

Mode of Resistance:Aminoglycoside-modifying enzymes (including acetyltransferase, phosphotransferase, nucleotidyltransferase) can alter this antibiotic, preventing its interaction with ribosomes.

Antimicrobial spectrum: Kanamycin sulfate is effective against gram-negative and gram-postiive bacteria, and mycoplasma.

pictograms

GHS08

signalword

Danger

hcodes

H360D

pcodes

P201 - P202 - P280 - P308 + P313 - P405 - P501

Hazard Classifications

Repr. 1B

Storage Class

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

wgk

WGK 2

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

涉药品监管产品

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Efficacy of repeated intravenous administration of peramivir against highly pathogenic avian influenza A (H5N1) virus in cynomolgus macaques.

Mitsutaka Kitano et al.

Antimicrobial agents and chemotherapy, 58(8), 4795-4803 (2014-06-11)

Highly pathogenic avian influenza A (H5N1) viruses cause severe and often fatal disease in humans. We evaluated the efficacy of repeated intravenous dosing of the neuraminidase inhibitor peramivir against highly pathogenic avian influenza virus A/Vietnam/UT3040/2004 (H5N1) infection in cynomolgus macaques.

Dual function of CD70 in viral infection: modulator of early cytokine responses and activator of adaptive responses.

Atef Allam et al.

Journal of immunology (Baltimore, Md. : 1950), 193(2), 871-878 (2014-06-11)

The role of the TNF family member CD70 in adaptive T cell responses has been intensively studied, but its function in innate responses is still under investigation. In this study, we show that CD70 inhibits the early innate response to

Intravenous peramivir inhibits viral replication, and leads to bacterial clearance and prevention of mortality during murine bacterial co-infection caused by influenza A(H1N1)pdm09 virus and Streptococcus pneumoniae.

Motoyasu Onishi et al.

Antiviral research, 117, 52-59 (2015-03-11)

Influenza virus infection increases susceptibility to bacterial infection and mortality in humans. Although the efficacy of approved intravenous peramivir, a neuraminidase (NA) inhibitor, against influenza virus infection has been reported, its efficacy against bacterial co-infection, which occurs during the period

Heterogeneity of molecular resistance patterns in antimony-resistant field isolates of Leishmania species from the western Mediterranean area.

Fakhri Jeddi et al.

Antimicrobial agents and chemotherapy, 58(8), 4866-4874 (2014-06-11)

Antimonials remain the first-line treatment for the various manifestations of leishmaniasis in most areas where the disease is endemic, and increasing cases of therapeutic failure associated with parasite resistance have been reported. In this study, we assessed the molecular status

Stable expression and characterization of monomeric and dimeric recombinant hybrid-IgG/IgA immunoglobulins specific for Shiga toxin.

Koki Iwata et al.

Biological & pharmaceutical bulletin, 37(9), 1510-1515 (2014-07-06)

Antigen-specific immunoglobulin A (IgA) may be useful for preventing infectious diseases through passive immunization on the mucosal surface. We previously established mouse IgA and IgG monoclonal antibodies (mAbs) specific for the binding subunit of Shiga toxin 1 (Stx1B). We also

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