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SAB4200633

Sigma-Aldrich

Monoclonal Anti-QPCT antibody produced in mouse

clone QP-2, purified from hybridoma cell culture

Synonym(s):

Glutaminyl-tRNA cyclotransferase (GCT), Glutamyl cyclase, QC, glutaminyl-peptide cyclotransferase, sQC

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

QP-2, monoclonal

mol wt

~40 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

flow cytometry: 5-10 μg/test using using HeLa cells.
immunoblotting: 2-4 μg/mL using using whole extracts of SK-Mel-28 cells.
immunofluorescence: 4-8 μg/mL using using SK-Mel-28 cells.

isotype

IgG2a

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... QPCT(25797)

General description

Monoclonal Anti-QPCT (mouse IgG2a isotype) is derived from the hybridoma QP-2 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice. Glutaminyl-peptide cyclotransferase (QPCT) is an enzyme present in the mammalian brain, porcine pituitary and human B lymphocytes. It is located on the human chromosome at 2p22.2.

Specificity

Monoclonal Anti-QPCT recognizes human QPCT.

Immunogen

synthetic peptide corresponding to a sequence at the C-terminal region of human QPCT.

Application

Monoclonal Anti-QPCT antibody produced in mouse may be used in:
  • immunoblotting
  • flow cytometry
  • immunofluorescence

Biochem/physiol Actions

Glutaminyl-peptide cyclotransferase (QPCT) catalyzes the post-translation modification of both glutaminyl precursors into N-terminal pyroglutamate (pGlu) and N-terminal glutamate cyclization. It is found to be involved in Alzheimer′s Disease (AD) pathogenesis and cognitive decline by QPCT-catalyzed pGlu- amyloid-β (Aβ) formation. Inhibition of QPCT prevents thyroid cancer metastasis. QPCT is also involved in other amyloidotic disorders such as familial British dementia (FBD) or familial Danish dementia (FDD).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For extended storage, freeze at -20 °Cin working aliquots. Repeated freezing and thawing,or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation. Working dilution samples should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Abstract LB-23: Meta-analysis of genome-wide association studies identifies multiple loci associated with chronic lymphocytic leukemia.
Berndt S I, et al.
Cancer research, 20(1), 79-90 (2013)
Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells
Cynis H, et al.
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1764(10), 1618-1625 (2006)
Stephan Schilling et al.
FEBS letters, 563(1-3), 191-196 (2004-04-06)
N-terminal pyroglutamate (pGlu) formation from glutaminyl precursors is a posttranslational event in the processing of bioactive neuropeptides such as thyrotropin-releasing hormone and neurotensin during their maturation in the secretory pathway. The reaction is facilitated by glutaminyl cyclase (QC), an enzyme
Astrid Kehlen et al.
Endocrine-related cancer, 20(1), 79-90 (2012-11-28)
CCL2 is a chemokine known to recruit monocytes/macrophages to sites of inflammation. CCL2 is also associated with tumor progression in several cancer types. Recently, we showed that the N-terminus of CCL2 is modified to a pyroglutamate (pE)-residue by both glutaminyl

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