Alle Fotos(2)
Wichtige Dokumente
D4138
Deoxyribonuclease II from porcine spleen
Type IV, lyophilized powder, 2,000-6,000 Kunitz units/mg protein (biuret)
Synonym(e):
DNase II, Deoxyribonucleate 3′-oligonucleotido-hydrolase
Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Größe auswählen
20000 UNITS
57,00 €
80000 UNITS
172,00 €
57,00 €
Check Cart for Availability
Alle Fotos(2)
Größe auswählen
Ansicht ändern
20000 UNITS
57,00 €
80000 UNITS
172,00 €
About This Item
57,00 €
Check Cart for Availability
Typ
Type IV
Form
lyophilized powder
Spezifische Aktivität
2,000-6,000 Kunitz units/mg protein (biuret)
Mol-Gew.
45 kDa
Zusammensetzung
Protein, 60-80%
Fremdaktivität
RNase ≤0.05%
Lagertemp.
−20°C
Anwendung
DNase II from Sigma has been used to treat transformed cells during the purification of β-lactamase.[1] It has also been used for the preparation of adenoma tissue in a study that investigated the effect of somatoprim on growth hormone secretion in human adenoma cell cultures (hSA).[2]
Deoxyribonuclease II from porcine spleen has been used in an immunohistological study of the immune system cells in paraffin-embedded tissues. Deoxyribonuclease II from porcine spleen has also been used in a study to investigate its reassociation with the lysosomal membrane.
Biochem./physiol. Wirkung
Einheitendefinition
One Kunitz unit will produce a ΔA260 of 0.001 per min per mL at pH 4.6 at 25°C; [Mg2+] = 0.83 mM
Physikalische Form
Contains sodium chloride
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Hier finden Sie alle aktuellen Versionen:
Analysenzertifikate (COA)
Lot/Batch Number
Die passende Version wird nicht angezeigt?
Wenn Sie eine bestimmte Version benötigen, können Sie anhand der Lot- oder Chargennummer nach einem spezifischen Zertifikat suchen.
Besitzen Sie dieses Produkt bereits?
In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.
Yoko Kato-Toma et al.
The Biochemical journal, 371(Pt 1), 175-181 (2003-01-07)
13C-NMR spectroscopy was used to estimate the p K a values for the Tyr(150) (Y150) residue in wild-type and mutant class C beta-lactamases. The tyrosine residues of the wild-type and mutant lactamases were replaced with (13)C-labelled L-tyrosine ([ phenol -4-(13)C]tyrosine)
F Chianini et al.
Veterinary immunology and immunopathology, 82(3-4), 245-255 (2001-10-06)
The distribution of different cells of the immune system has been studied in formalin-fixed paraffin-embedded tissues from conventionally reared healthy pigs, using immunohistological techniques. The samples collected were: lungs, tonsils, lymph nodes (mediastinal, mesenteric, inguinal and submandibular), pancreas, spleen, liver
T H Liao et al.
Biochimica et biophysica acta, 1007(1), 15-22 (1989-01-23)
Porcine spleen DNase II (EC 3.1.22.1), one of the best-characterized DNases II, is subcellularly located in lysosomes because the enzyme is co-sedimented with two of the lysosomal marker enzymes, cathepsin D and acid phosphatase. The physicochemical properties, including the subunit
Therese Ostberg et al.
Arthritis and rheumatism, 62(10), 2963-2972 (2010-06-10)
High mobility group box chromosomal protein 1 (HMGB-1) is a DNA binding nuclear protein that can be released from dying cells and activated myeloid cells. Extracellularly, HMGB-1 promotes inflammation. Clinical and experimental studies demonstrate that HMGB-1 is a pathogenic factor
Zufeng Ding et al.
Scientific reports, 3, 1077-1077 (2013-01-18)
Our studies in HUVECs show that ox-LDL induced autophagy and damaged mtDNA leading to TLR9 expression. LOX-1 antibody or the ROS inhibitor apocynin attenuated ox-LDL-mediated autophagy, mtDNA damage and TLR9 expression, suggesting that these events are LOX-1 and ROS-dependent phenomena.
Aktive Filter
Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..
Setzen Sie sich mit dem technischen Dienst in Verbindung.
