Microsomal aminopeptidase

Modify Date: 2024-01-11 18:29:09

Microsomal aminopeptidase Structure
Microsomal aminopeptidase structure
Common Name Microsomal aminopeptidase
CAS Number 9054-63-1 Molecular Weight 200.31776
Density N/A Boiling Point N/A
Molecular Formula C12H24O2 Melting Point N/A
MSDS USA Flash Point N/A

 Use of Microsomal aminopeptidase


Microsomal aminopeptidase (microsomal aminoptidase) was first reported from C. elegans. The Microsomal aminopeptidase is beneficial for the development of molecular vaccines against parasitic nematodes[1].

 Names

Name Aminopeptidase
Synonym More Synonyms

 Microsomal aminopeptidase Biological Activity

Description Microsomal aminopeptidase (microsomal aminoptidase) was first reported from C. elegans. The Microsomal aminopeptidase is beneficial for the development of molecular vaccines against parasitic nematodes[1].
Related Catalog
References

[1]. Smith TS, et al. Cloning and characterization of a microsomal aminopeptidase from the intestine of the nematode Haemonchus contortus. Biochim Biophys Acta. 1997 Apr 4;1338(2):295-306.  

 Chemical & Physical Properties

Molecular Formula C12H24O2
Molecular Weight 200.31776
Appearance of Characters powder | white
Storage condition 2-8°C

 Safety Information

Personal Protective Equipment Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter
Safety Phrases 22-24/25
RIDADR NONH for all modes of transport
WGK Germany 3

 Articles57

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Sodium solute symporter and cadherin proteins act as Bacillus thuringiensis Cry3Ba toxin functional receptors in Tribolium castaneum.

J. Biol. Chem. 288(25) , 18013-21, (2013)

Understanding how Bacillus thuringiensis (Bt) toxins interact with proteins in the midgut of susceptible coleopteran insects is crucial to fully explain the molecular bases of Bt specificity and insec...

Novel leucine ureido derivatives as inhibitors of aminopeptidase N (APN).

Bioorg. Med. Chem. 21(7) , 1621-7, (2013)

Aminopeptidase N (APN/CD13) over expressed on tumor cells, plays a critical role in tumor invasion, metastasis, and tumor angiogenesis. Here we described the design, synthesis and preliminary activity...

Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from Plasmodium falciparum.

J. Med. Chem. 56(12) , 5213-7, (2013)

The malaria parasite Plasmodium falciparum employs two metallo-aminopeptidases, PfA-M1 and PfA-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme repr...

 Synonyms

MFCD00131501