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HPA022963

Sigma-Aldrich

Anti-NMT1 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab2

Synonym(s):

Anti-Glycylpeptide N-tetradecanoyltransferase 1, Anti-Myristoyl-CoA:protein N-myristoyltransferase 1, Anti-NMT 1, Anti-Peptide N-myristoyltransferase 1, Anti-Type I N-myristoyltransferase

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About This Item

MDL number:
UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

Pricing and availability is not currently available.

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

mouse, rat, human

enhanced validation

orthogonal RNAseq
Learn more about Antibody Enhanced Validation

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This Item
HPA022949D4692SAB5700753
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

-

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

product line

Prestige Antibodies® Powered by Atlas Antibodies

product line

Prestige Antibodies® Powered by Atlas Antibodies

product line

-

product line

-

UniProt accession no.

P30419

UniProt accession no.

P30419

UniProt accession no.

P26358

UniProt accession no.

P26358

shipped in

wet ice

shipped in

wet ice

shipped in

dry ice

shipped in

wet ice

Immunogen

Glycylpeptide N-tetradecanoyltransferase 1 recombinant protein epitope signature tag (PrEST)

Application

Anti-NMT1 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

Biochem/physiol Actions

NMT1 (N-myristoyltransferase 1) is responsible for myristoylation of proteins. It is needed for the transfer of myristate from myristoyl coenzyme A to the amino-terminal glycine in the target protein. NMT1 also promotes the replication of HIV (human immunodeficiency virus)-1 by controlling viral RNA expression.[1] Additionally, it also participates in tumor cell proliferation.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST75702

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Charles E Ducker et al.
Molecular cancer research : MCR, 3(8), 463-476 (2005-08-27)
N-myristoyltransferases (NMT) add myristate to the NH(2) termini of certain proteins, thereby regulating their localization and/or biological function. Using RNA interference, this study functionally characterizes the two NMT isozymes in human cells. Unique small interfering RNAs (siRNA) for each isozyme
Wouter W Kallemeijn et al.
Cell chemical biology, 26(6), 892-900 (2019-04-23)
On-target, cell-active chemical probes are of fundamental importance in chemical and cell biology, whereas poorly characterized probes often lead to invalid conclusions. Human N-myristoyltransferase (NMT) has attracted increasing interest as target in cancer and infectious diseases. Here we report an
Hikaru Ohta et al.
Biochemical and biophysical research communications, 463(4), 988-993 (2015-06-16)
N-myristoyltransferase (NMT) catalyzes protein N-myristoylation. It has been suggested that the isozyme NMT1 enhances the replication of human immunodeficiency virus type-1 (HIV-1). However, the details of the mechanism by which NMT1 does so remain unclear. In this study, we investigated
Anuraag Shrivastav et al.
Journal of translational medicine, 5, 58-58 (2007-11-21)
Colon cancer is the second leading cause of cancer deaths in the western world. If detected early, colorectal cancer is one of the most treatable forms of cancer. Unfortunately, very few people are screened. N-myristoyltransferase (NMT) catalyzes myristoylation of various
Emmanuelle Thinon et al.
Nature communications, 5, 4919-4919 (2014-09-27)
Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. Here, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined

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