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D4138

Sigma-Aldrich

Deoxyribonuclease II from porcine spleen

Type IV, lyophilized powder, 2,000-6,000 Kunitz units/mg protein (biuret)

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Synonym(s):
DNase II, Deoxyribonucleate 3′-oligonucleotido-hydrolase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

type

Type IV

Quality Level

form

lyophilized powder

specific activity

2,000-6,000 Kunitz units/mg protein (biuret)

mol wt

45 kDa

composition

Protein, 60-80%

foreign activity

RNase ≤0.05%

storage temp.

−20°C

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This Item
D8764D4513D4527
specific activity

2,000-6,000 Kunitz units/mg protein (biuret)

specific activity

≥1,000 units/mg protein

specific activity

≥2,000 units/mg protein

specific activity

≥2,000 units/mg protein

mol wt

45 kDa

mol wt

38 kDa

mol wt

~31 kDa

mol wt

~31 kDa

foreign activity

RNase ≤0.05%

foreign activity

RNase ≤0.1%

foreign activity

Chymotrypsin ≤0.01%, Protease ≤0.005%, RNase ≤0.01%

foreign activity

Chymotrypsin ≤0.01%, Protease ≤0.005%, RNase ≤0.01%

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

300

Quality Level

300

Application

DNase II from Sigma has been used to treat transformed cells during the purification of β-lactamase. 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).
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 Actions

The enzyme is a lysosomal acid hydrolase that hydrolyzes DNA to 3′-phosphoryl oligonucleotides in the absence of metal ions, under acidic conditions. It is a non-covalently linked α·β heterodimer of approximately 45,000 Da molecular mass.

Unit Definition

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

Physical form

Contains sodium chloride

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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
U Plöckinger et al.
European journal of endocrinology, 166(2), 223-234 (2011-11-09)
Somatostatin analogues (SSA) reduce autonomous GH secretion by activating somatostatin receptors (sst) 2 and 5 in 50-60% of acromegalic patients. However, by inhibiting insulin secretion these SSA reduce glucose tolerance. DG3173 is a novel SSA with additional binding to sst4
C C Wang et al.
The Journal of biological chemistry, 273(27), 17192-17198 (1998-06-27)
Porcine spleen DNase II, a lysosomal acid hydrolase, is a noncovalently linked alpha.beta heterodimer (Liao, T.-H. (1985) J. Biol. Chem. 260, 10708-10713). The alpha subunit, after disulfide cleavage, yields two chains, alpha1 and alpha2. The complete amino acid sequences of
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.
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

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