Recombinant Human Glutaminyl cyclase protein is a Human Full Length protein, in the 1 to 361 aa range, expressed in Wheat germ and suitable for ELISA, WB.
M A G G R H R R V V G T L H L L L L V A A L P W A S R G V S P S A S A W P E E K N Y H Q P A I L N S S A L R Q I A E G T S I S E M W Q N D L Q P L L I E R Y P G S P G S Y A A R Q H I M Q R I Q R L Q A D W V L E I D T F L S Q T P Y G Y R S F S N I I S T L N P T A K R H L V L A C H Y D S K Y F S H W N N R V F V G A T D S A V P C A M M L E L A R A L D K K L L S L K T V S D S K P D L S L Q L I F F D G E E A F L H W S P Q D S L Y G S R H L A A K M A S T P H P P G A R G T S Q L H G M D L L V L L D L I G A P N P T F P N F F P N S A R W F E R L Q A I E H E L H E L G L L K D H S L E G R Y F Q N Y S Y G G V I Q D D H I P F L R R G V P V L H L I P S P F P E V W H T M D D N E E N L D E S T I D N L N K I L Q V F V L E Y L H L
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Glutaminyl-peptide cyclotransferase, Glutaminyl cyclase, Glutaminyl-tRNA cyclotransferase, Glutamyl cyclase, QC, sQC, EC, QPCT
Recombinant Human Glutaminyl cyclase protein is a Human Full Length protein, in the 1 to 361 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Belongs to the glutaminyl-peptide cyclotransferase family.
This product was previously labelled as QPCT.
Glutaminyl cyclase also known by the alternate name 'QC' catalyzes the conversion of glutaminyl residues towards pyroglutamyl formation in proteins. This enzyme weighs around 39 kDa and is distributed across various tissues with significant expression in the brain and secretory tissues. The active site of this enzyme facilitates the cyclization of N-terminal glutaminyl and glutamyl residues influencing protein stability and function.
This enzyme modifies peptide hormones and neuropeptides by enhancing their activity or stability. Glutaminyl cyclase does not usually operate within large protein complexes. However its activity is critical for processing secretory proteins into their mature forms. Modifications by the enzyme often regulate peptide function making it an important player in cellular communication processes.
Glutaminyl cyclase plays an important role in the neuroendocrine cascade and protein maturation pathways. This enzyme's activity connects with other proteins like hormone receptors affecting their downstream signaling processes. It also shares connections with proteins involved in the proteolytic processing pathway ensuring maturation and activation of peptide substrates.
Malfunction of glutaminyl cyclase associates with Alzheimer's disease and amyloidosis. The enzyme's activity influences accumulation of pyroglutamyl-modified proteins which have links to amyloid plaque formation in Alzheimer's disease. This connection involves amyloid-beta peptides where glutaminyl cyclase enhances the aggregation potential through N-terminal cyclization. Effective modulation of this enzyme’s activity might represent a therapeutic approach for related disorders.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
ab161786 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com