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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

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. 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

Certificates of Analysis (COA)

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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)
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)
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
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
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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