Human/Mouse/Rat Neurolysin Antibody Summary
aa 38-704
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of Human, Mouse, and Rat Neurolysin by Western Blot. Western blot shows lysates of SH-SY5Y human neuroblastoma cell line, bEnd.3 mouse endothelioma cell line, rat cortical neuron tissue, and human brain (cortex) tissue. PVDF Membrane was probed with 1 µg/mL of Sheep Anti-Human/Mouse/Rat Neurolysin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3814) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Neurolysin at approximately 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Neurolysin
Neurolysin, also known as Oligopeptidase M (mitochondrial peptidase), soluble angiotensin II-binding protein and endopeptidase EC 3.4.24.16 (1, 2), is a homologue of Thimet Ologopeptidase (THOP1), a zinc peptidase of the M3 family that also includes mitochondrial intermediate peptidase. Neurolysin expresses in two forms with the difference of an N-terminal transit peptide that targets the localization to mitochondria (1). The shorter form exists in cytosol. The recombinant human Neurolysin is expressed without the transit peptide and is isolated from the cytosol. Like THOP1, Neurolysin is capable of cleaving a number of vasoactive peptides such as bradykinin and neurotensin (3). All known substrates of THOP1 and Neurolysin contain 17 or fewer amino acids.
- Serizawa, A. et al. (1995) J. Biol. Chem. 270:2092.
- Barett, A.J. and J.M. Chen (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, A.J. et al.) pp. 356, Elsevier Academic Press, San Diego.
- Norman, M.U. et al. (2003) Am. J. Physiol. Heart Circ. Physiol. 284:H1978.
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