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100 U (DMC)

Ref. SER-3030601
SERVA / NORDMARK
N0003553
9001-12-1

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Détails Produit

 

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World's first animal free GMP Grade Neutral Protease

Neutral Protease AF GMP Grade is derived from C. histolyticum using a production process completely free of any animal based components. Thus, any risk of transmission of potential animal-derived pathogens is excluded. This purified metalloprotease is suitable for the dissociation of tissue in clinical applications. For especially gentle cell isolation it is recommended to use Neutral Protease AF GMP Grade in combination with highly purified Collagenase AF-1 GMP Grade (Cat. No. N0003554).

 

 

Specifications:

Plant-based fermentation process. Contains chromatographically purified neutral protease.
Vial contains not less than 100 DMC U of neutral protease.

Neutral protease activity (DMC) ≥ 0.50 U/mg.

Endotoxin: ≤ 100 EU/mg (Ph. Eur.)

Largely free of collagenolytic activity.

Microbiological examination: Total aerobic microbial count (TAMC), total combined yeast/moulds count (TYMC), absence of Clostridia
Endproduct is 0.22 µm filtered.

Manufactured according to EU GMP guidelines.

Mr Mr approx. 34 000 • CAS [9001-92-7]

Order Information

Productname Cat.No Size EUR
Neutral Protease AF GMP Grade

Nordmark: N0003553

Serva : 3030601

≥ 100DMC-U Inquire

 

Storage Temperature: +2 °C to +8 °C
This article will be delivered cooled on blue ice.

 

Related Products

Neutral Protease AF GMP Grade is often used in combination with Collagenase AF-1 GMP Grade (Cat. No N0003554). For customer convenience, these both products are also sold together in the GMP Cell Isolation Kit AF-1 (Cat. No. N0003716).

 

References and Definitions

Unit definition:
Neutral Protease: 1 DMC Unit catalyzes the cleavage of 1 µmol peptide bond from dimethylcasein per minute at 25 °C, pH 7.0, expressed in terms of newly formed terminal amino groups, determined with TNBS (1).
Endotoxin: Ph. Eur. [1 Endotoxin Unit is equal to 1 International Unit of a WHO approved reference standard endotoxin (RSE)]. 

References:

  1. Lin, Y.-C. et al. (1969) J. Biol. Chem. 244, 789-93