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Human CANX / Calnexin Protein (Fc Tag)

CNX,IP90,P90

Catalog Number P13929-H02H
Organism Species Human
Host Human Cells
Synonyms CNX,IP90,P90
Molecular Weight The recombinant human CANX/Fc is a disulfide-linked homodimer. The reduced monomer comprises 702 amino acids and has a predicted molecular mass of 79.4 kDa. The apparent molecular mass of the protein is approximately 110 kDa in SDS-PAGE under reducing conditions.
predicted N His 21
SDS-PAGE
Purity > 85 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human CANX (P27824) (Met1-Pro481) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Bio-activity
Research Area Signaling |Signal Transduction |Signaling Pathway |Calcium Signaling |Calcium Binding Protein |Calreticulin Family |
Formulation Lyophilized from sterile PBS, pH 7.4
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 Calnexin is a calcium-binding protein that belongs to the calreticulin family. It interacts with newly synthesized glycoproteins in the endoplasmic reticulum. Calnexin seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.
Reference
  • Rajagopalan S, et al. (1994) Retention of unassembled components of integral membrane proteins by Calnexin(CANX). Science. 263(5145):387-90.
  • Lenter M, et al. (1994) The integrin chains beta 1 and alpha 6 associate with the chaperone Calnexin(CANX) prior to integrin assembly. J Biol Chem. 269(16):12263-8.
  • Pind S, et al. (1994) Retention of unassembled components of integral membrane proteins by Calnexin(CANX). Science. 263(5145):387-90.