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164599 Aminopeptidase N, Rat

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164599
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Overview

Replacement Information

Products

Catalog NumberPackaging Qty/Pack
164599-10U Plastic ampoule 10 u
Description
OverviewNative aminopeptidase N purified from rat renal brush-border membranes and cleaved with papain to produce soluble enzyme. A single-chain, integral membrane protease that, functions with broad specificity to remove N-terminal amino acids from peptides. It has been reported that levels of aminopeptidase N are elevated in cancer subjects and correlate with tumor load, and thus, the enzyme is believed to play a role in angiogenesis.
Catalogue Number164599
Brand Family Calbiochem®
SynonymsAPN/CD13, aminopeptidase N
References
ReferencesBhagwat, S.V., et al. 2003. Blood 101, 1818.
van Hensbergen, Y., et al. 2002. Clin. Cancer Res. 8, 3747.
Ishii, K., et al. 2001. Biol. Pharm. Bull. 24, 226.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Leu-<i>p</i>NA per min at 37°C, pH 7.2
EC number3.4.11.2
FormLiquid
FormulationIn 200 mM NaCl, 50 mM Tris-HCl, pH 8.0.
Quality LevelMQ100
Applications
Biological Information
Purity≥90% by SDS-PAGE
Specific Activity≥100 units/mg protein
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
164599-10U 04055977207583

Documentation

Aminopeptidase N, Rat SDS

Title

Safety Data Sheet (SDS) 

Aminopeptidase N, Rat Certificates of Analysis

TitleLot Number
164599

References

Reference overview
Bhagwat, S.V., et al. 2003. Blood 101, 1818.
van Hensbergen, Y., et al. 2002. Clin. Cancer Res. 8, 3747.
Ishii, K., et al. 2001. Biol. Pharm. Bull. 24, 226.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision10-April-2008 RFH
SynonymsAPN/CD13, aminopeptidase N
DescriptionNative aminopeptidase N purified from rat renal brush-border membranes and cleaved with papain to produce soluble enzyme. A single-chain, integral membrane protease that functions to remove N-terminal amino acids from peptides with broad specificity. Aminopeptidase N is believed to play a role in angiogenesis and elevated levels of aminopeptidase N have been reported in patients with various types of cancer and have been correlated with tumor load. Also involved in the final stages of digestion of small peptides in the intestinal brush border.
FormLiquid
FormulationIn 200 mM NaCl, 50 mM Tris-HCl, pH 8.0.
Concentration Label Please refer to vial label for lot-specific concentration
Recommended reaction conditions200 mM Tris-HCl, pH 7.2, 100 µl substrate (L-leu-pNA; final concentration 1 mM) in 200 mM Tris-HCl, pH 7.2, enzyme sample, final volume 200 µl; incubate at 37°C for 10 min.*; cleavage is monitored at 405 nm. *Note: Incubation time of 10 min. is provided as a guideline. The incubation time depends on the activity of the enzyme and the sensitivity of the instrument and should be determined for individual assays.
EC number3.4.11.2
Purity≥90% by SDS-PAGE
Specific activity≥100 units/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Leu-pNA per min at 37°C, pH 7.2
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesBhagwat, S.V., et al. 2003. Blood 101, 1818.
van Hensbergen, Y., et al. 2002. Clin. Cancer Res. 8, 3747.
Ishii, K., et al. 2001. Biol. Pharm. Bull. 24, 226.