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A3233

L-Arginase from bovine liver

Protein ≥70 % by biuret, powder

Synonyme(s) :

L-Arginine amidinase, L-Arginine amidino-hydrolase

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A propos de cet article

Numéro CAS:
9000-96-8
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-570-3
MDL number:
MFCD00081368
Numéro CE :
3.5.3.1 (BRENDA, IUBMB)
Specific activity:
≥100 units/mg protein
Biological source:
bovine liver
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biological source

bovine liver

Quality Segment

200

form

powder

specific activity

≥100 units/mg protein

composition

Protein, ≥70% biuret

UniProt accession no.

Q58DL1

shipped in

dry ice

storage temp.

−20°C

Gene Information

cow ... ARG2(518752)

General description

L-arginase is also called as L-arginine amidinohydrolase. It exists in two forms, such as arginase-1 and arginase-2. Arginase-1 is present in liver cells and arginase-2 is seen usually in extrahepatic tissues like, kidney, brain, skeletal muscle, small intestine and the lactating mammary gland. Arginase -2 is mapped to human chromosome 14q24.1−24.3.

Biochem/physiol Actions

L-arginase hydrolyze L-arginine into L-ornithine and urea, which is the last step of the urea cycle in the liver of ureotelic species. Arginase plays a major role in the mammalian immune system and the enzyme participates in several aspects of inflammation.
L-Arginase is the major degradative enzyme for arginine; converts arginine to ornithine.
L-Arginase is the major degradative enzyme for arginine; converts arginine to ornithine; deficiency is associated with spasticity and motor dysfunction.

Other Notes

One unit will cause the hydrolysis of 1.0 μmole of L-arginine per minute at pH 9.5 and 37 °C.

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Cet article
G2626G7882SAB5701218
L-Arginase from bovine liver Protein ≥70 % by biuret, powder

Sigma-Aldrich

A3233

L-Arginase from bovine liver

L-Glutamic Dehydrogenase from bovine liver Type II, 50% glycerol solution, ≥35 units/mg protein

Sigma-Aldrich

G2626

L-Glutamic Dehydrogenase from bovine liver

L-Glutamic Dehydrogenase from bovine liver Type III, lyophilized powder, ≥20 units/mg protein

Sigma-Aldrich

G7882

L-Glutamic Dehydrogenase from bovine liver

Anti-Arginase 2 (ARG2) antibody produced in rabbit

Sigma-Aldrich

SAB5701218

Anti-Arginase 2 (ARG2) antibody produced in rabbit

specific activity

≥100 units/mg protein

specific activity

≥35 units/mg protein

specific activity

≥20 units/mg protein

specific activity

-

biological source

bovine liver

biological source

bovine liver

biological source

bovine liver

biological source

rabbit

Gene Information

cow ... ARG2(518752)

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

human ... Arg2(384)

form

powder

form

glycerol solution (50%)

form

lyophilized powder

form

liquid

UniProt accession no.

Q58DL1

UniProt accession no.

P00366

UniProt accession no.

P00366

UniProt accession no.

P78540

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000471786
0000471786
0000451602
0000451602
0000368691

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Numéro d'article de commerce international

RéférenceGTIN
A3233-25KU04061833228302
A3233-12.5KU04061833228296
A3233-2.5KU04061833360514

Questions

  1. I want to use this enzyme at a neutal pH, could you please comment on the activity and how much reduction in enzyme activity and specificity would be happening due to the change in the pH?

    1 answer

    1. L-Arginase typically exhibits optimal activity at pH 9.5 and 37 °C. While the product is likely to retain some degree of potency, the enzymatic activity of this material at neutral pH has not been determined. The enzyme is known to be rapidly inactivated at pH values below 6, according to "The Reversible Inactivation of Rat-Liver Arginase at Low pH". Please see the link below, Figure 1, which shows the Inactivation of arginase at different pH values:
      https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1972.tb01809.x

      Please see the link below to review an additional article highlighting the relationship between pH and mouse liver arginase.
      https://www.jstage.jst.go.jp/article/biochemistry1922/45/12/45_12_1011/_pdf

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