Aperçu rapide pour Dipeptidyl-Peptidase 6 (DPP6) (Middle Region) Peptide (ABIN975974)
Antigène
DPP6
(Dipeptidyl-Peptidase 6 (DPP6))
Origine
Humain
Source
Synthetic
Application
Blocking Peptide (BP), Western Blotting (WB)
Protein Region
Middle Region
Attributs du produit
This is a synthetic peptide designed for use in combination with anti-DPP6 antibody (Catalog #: ARP44867_P050). It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
Each Investigator should determine their own optimal working dilution for specific applications.
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
Concentration
1 mg/mL
Buffer
Final peptide concentration is 1 mg/mL in PBS.
Conseil sur la manipulation
Avoid repeated freeze-thaw cycles.
Stock
-20 °C
Stockage commentaire
For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
Antigène
DPP6
(Dipeptidyl-Peptidase 6 (DPP6))
Sujet
DPP6 is a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties.This gene encodes a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.