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A3233

L-Arginase from bovine liver

Protein ≥70 % by biuret, powder

Synonym(s):

L-Arginine amidinase, L-Arginine amidino-hydrolase

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2500 units
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CLP 589,000
12500 units
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CLP 2,450,000
25000 units
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CLP 4,240,000

About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-570-3
MDL number:
EC Number:
Specific activity:
≥100 units/mg protein
Biological source:
bovine liver

CLP 589,000


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biological source

bovine liver

Quality Level

form

powder

specific activity

≥100 units/mg protein

composition

Protein, ≥70% biuret

UniProt accession no.

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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This Item
G2626G7882SAB5701218
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)

specific activity

≥100 units/mg protein

specific activity

≥35 units/mg protein

specific activity

≥20 units/mg protein

specific activity

-

form

powder

form

glycerol solution (50%)

form

lyophilized powder

form

liquid

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

shipped in

dry ice

shipped in

wet ice

shipped in

-

shipped in

wet ice


pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

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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Arginase: an emerging key player in the mammalian immune system
Munder M
British Journal of Pharmacology, 158(3), 638-651 (2009)
L-Arginase: a Medically Important Enzyme
Kumar K and Verma N
Research Journal of Pharmacy and Technology, 6(12), 1430-1430 (2013)
Yoshinori Narita et al.
Journal of immunology (Baltimore, Md. : 1950), 190(2), 812-820 (2012-12-19)
Evaluation of immune dysfunction during the tumor-bearing state is a critical issue in combating cancer. In this study, we initially found that IL-6, one of the cachectic factors, suppressed CD4(+) T cell-mediated immunity through downregulation of MHC class II by



Global Trade Item Number

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

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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