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Bovine Endothelin Converting Enzyme 2 (ECE2) ELISA Kit-Sandwich

Cat. No.EK2F479

Product TypeAnimal Immunoassay Kits

Size

Product Overview

BioVenic Bovine Endothelin Converting Enzyme 2 (ECE2) ELISA Kit-Sandwich is designed for the quantitative determination of Bovine Endothelin Converting Enzyme 2(ECE2) in serum, plasma, tissue homogenate, cell culture supernatant, cell extract, and other biological fluids using a Sandwich ELISA method. For research use only.

Specifications

Assay Type ELISA-Sandwich
Specificity The assay kit is specific for Bovine ECE2.
Target Species Bovine
Species Reactivity Bovine
Reproducibility Intra-Assay: CV < 10%; Inter-Assay: CV < 10%
Assay Time Around 210 min
Sample Requirement Serum, plasma, tissue homogenate, cell culture supernatant, cell extract, and other biological fluids.

Target Information

Endothelin Converting Enzyme 2 is an enzyme that converts endothelin-1, a potent vasoconstrictor peptide, into its inactive form. This helps regulate blood vessel tone and blood pressure. It is encoded by the bovine gene ECE2. It is found on the cell surface of various cell types, including endothelial cells lining blood vessels. It is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum.

Target/Biomarker Bovine ECE2
Target Synonym EEF1AKMT4-ECE2 readthrough transcript protein; EC 3.4.24.71 [Includes: Methyltransferase-like region; EC 2.1.1.-; Endothelin-converting enzyme 2 region
Gene ID 281134
UniProt ID P0DPE2

Shipping and Storage

This product is shipped with gel ice packs. It is recommended to store at 2-8 °C (Up to 6 months).

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

References

  1. Emoto, N. & Yanagisawa, M. Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum. The Journal of biological chemistry. 1995, 270: 15262-15268.
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