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Human CPNE1 / Copine I / CPN1 Protein (SUMO Tag)

COPN1,CPN1

Catalog Number P14283-H21B
Organism Species Human
Host Baculovirus-Insect Cells
Synonyms COPN1,CPN1
Molecular Weight The secreted recombinant human CPNE1 consists of 656 amino acids and predicts a molecular mass of 72.7 KDa. The apparent molecular mass of the protein is approximately 73 KDa in SDS-PAGE under reducing conditions due to glycosylation.
predicted N Met
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human CPNE1 (Q99829) (Met1-Ala537) was fused with the SUMO tag at the N-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Signaling Pathway |Calcium Signaling |Others in Calcium Signaling
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.0, 10% gly
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Copine I, also known as CPN1, is a member of the copine family. Copine I is a calcium-dependent membrane-binding protein which has a wide tissue distribution. Calcium-dependent membrane-binding proteins may regulate molecular events at the interface of the cell membrane and cytoplasm. Copine I contains two N-terminal type II C2 domains and an integrin A domain-like sequence in the C-terminus, while it does not contain a predicted signal sequence or transmembrane domains. Copine I may function in membrane trafficking.
Reference
  • Cowland JB, et al. (2003) Tissue expression of copines and isolation of copines I and III from the cytosol of human neutrophils. J Leukoc Biol. 74(3):379-88.
  • Tomsig JL, et al. (2003) Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif. J Biol Chem. 278 (12):10048-54.
  • Strausberg RL, et al. (2003) Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci. 99(26):16899-903.