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R6000

Sigma-Aldrich

Ribonuclease S from bovine pancreas

Grade XII-S

Synonym(s):

RNase S, pancreatic RNase, protease-modified RNase A

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About This Item

CAS Number:
9001-99-4
EC Number:
232-646-6
MDL number:
MFCD00132188
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

200

type

Grade XII-S

form

powder

specific activity

≥60 Kunitz units/mg solid

mol wt

13.7 kDa

storage temp.

−20°C

InChI

1S/C9H14N4O3/c10-2-1-8(14)13-7(9(15)16)3-6-4-11-5-12-6/h4-5,7H,1-3,10H2,(H,11,12)(H,13,14)(H,15,16)

InChI key

CQOVPNPJLQNMDC-UHFFFAOYSA-N

Application

Ribonuclease S from bovine pancreas has been used in a study to assess the hybridase activity of human ribonuclease-1. Ribonuclease S from bovine pancreas has also been used in a study to investigate a new approach to obtaining high-activity RNase, DNase, cholesterolesterase, and trypsin from cattle pancreas.

Other Notes

Protease-modified RNase A

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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Beata Schmidt et al.
Journal of chromatography. A, 1018(2), 155-167 (2003-11-19)
The overall topic of the investigation was the separation of basic proteins by cation exchange displacement chromatography. For this purpose two principal column morphologies were compared for the separation of ribonuclease A and alpha-chymotrypsinogen, two proteins found in the bovine
A new approach to obtaining high-activity RNase, DNase, cholesterolesterase, and trypsin from cattle pancreas.
V V Khomov et al.
Doklady. Biochemistry and biophysics, 400, 61-64 (2005-04-26)
Nicoletta Potenza et al.
Nucleic acids research, 34(10), 2906-2913 (2006-06-02)
Human ribonuclease-1 (hRNase-1) is an extracellular enzyme found in exocrine pancreas, blood, milk, saliva, urine and seminal plasma, which has been implicated in digestion of dietary RNA and in antiviral host defense. The enzyme is characterized by a high catalytic
The preparation of subtilisn-modified ribonuclease and the separation of the peptide and protein components.
F M RICHARDS et al.
The Journal of biological chemistry, 234(6), 1459-1465 (1959-06-01)
Evgeny Onischenko et al.
Cell, 171(4), 904-917 (2017-10-17)
Nuclear pore complexes (NPCs) are ∼100 MDa transport channels assembled from multiple copies of ∼30 nucleoporins (Nups). One-third of these Nups contain phenylalanine-glycine (FG)-rich repeats, forming a diffusion barrier, which is selectively permeable for nuclear transport receptors that interact with
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