Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer composed of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.In melanocytic cells CPN1 gene expression may be regulated by MITF.
Background References
1. Keil C. et. al. Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. J. Mol. Biol. 366:504-516(2007).
ICC staining of CPN1 in LOVO cells (green). Formalin fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 10 minutes at room temperature and blocked with 1% Blocker BSA for 15 minutes at room temperature. Cells were probed with the primary antibody (HA500462, 1/100) for 1 hour at room temperature, washed with PBS. Alexa Fluor®488 Goat anti-Rabbit IgG was used as the secondary antibody at 1/1,000 dilution. The nuclear counter stain is DAPI (blue).
Western blot analysis of CPN1 on MCF7 cell lysate with Rabbit anti-CPN1 antibody (HA500462) at 1/1,000 dilution.
Lysates/proteins at 20 µg/Lane.
Exposure time: 120 seconds; ECL: K1802
Blocking: 5% NFDM/TBST, 1 hour at room temperature Primary antibody: HA500462, 1/1,000 in 5% NFDM/TBST, overnight at 4 ℃ Secondary antibody: Goat anti-Rabbit IgG-HRP (HA1001), 1/50,000 in 5% NFDM/TBST, 1 hour at room temperature
Predicted band size: 52 kDa Observed band size: 60 kDa
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