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A3233

L-Arginase from bovine liver

Protein ≥70 % by biuret, powder

Sinónimos:

L-Arginine amidinase, L-Arginine amidino-hydrolase

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Talla/SKUDisponibilidadPrecio
2500 units

Fecha estimada de envío16 de octubre de 2026desdeCarlos Spegazzini

US$ 959,00
12500 units

Fecha estimada de envío23 de octubre de 2026desdeCarlos Spegazzini

US$ 3.990,00
25000 units

Fecha estimada de envío23 de octubre de 2026desdeCarlos Spegazzini

US$ 6.930,00

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

US$ 959,00

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Fecha estimada de envío16 de octubre de 2026Detalles


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biological source

bovine liver

Quality Segment

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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Este artículo
G7882SAB5701218SAB5701574
description

Protein ≥70 % by biuret, powder

description

Type III, lyophilized powder, ≥20 units/mg protein

description

-

description

-

specific activity

≥100 units/mg protein

specific activity

≥20 units/mg protein

specific activity

-

specific activity

-

Gene Information

cow ... ARG2(518752)

Gene Information

cow ... GLUD1(281785)

Gene Information

human ... Arg2(384)

Gene Information

human ... ARG1(383)

biological source

bovine liver

biological source

bovine liver

biological source

rabbit

biological source

rabbit

form

powder

form

lyophilized powder

form

liquid

form

liquid

shipped in

dry ice

shipped in

-

shipped in

wet ice

shipped in

wet ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C


Pictogramas

Health hazard

Palabra de advertencia

Danger

Códigos de peligro

Indicaciones de precaución

Hazard Classifications

Resp. Sens. 1

Clase de almacenamiento

11 - Combustible Solids

¿Qué está pasando?

WGK 1

Punto de inflamación (°F)

Not applicable

Punto de inflamación (°C)

Not applicable

EPI (equipos de protección individual)

Eyeshields, Gloves, type N95 (US)



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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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