HPA023314
Anti-SHMT1 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sinonimo/i:
Shmt1 Antibody, Shmt1 Antibody - Anti-SHMT1 antibody produced in rabbit, Anti-Glycine hydroxymethyltransferase, Anti-SHMT, Anti-Serine hydroxymethyltransferase, cytosolic, Anti-Serine methylase
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About This Item
Coniugato:
unconjugated
application:
IF
IHC
IHC
Clone:
polyclonal
Reattività contro le specie:
human
citations:
10
tecniche:
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000
Prodotti consigliati
Origine biologica
rabbit
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
affinity isolated antibody
Tipo di anticorpo
primary antibodies
Clone
polyclonal
Nome Commerciale
Prestige Antibodies® Powered by Atlas Antibodies
Stato
buffered aqueous glycerol solution
Reattività contro le specie
human
tecniche
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:500-1:1000
Sequenza immunogenica
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCL
N° accesso UniProt
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
modifica post-traduzionali bersaglio
unmodified
Informazioni sul gene
human ... SHMT1(6470)
Descrizione generale
Cytoplasmic serine hydroxymethyltransferase or SHMT1 regulates the biosynthesis of thymidylate in mammals. SHMT1 catalyzes the conversion of serine to glycine, which also results in the formation of 5,10-methylene-tetrahydrofolate. Rises in SHMT1 activity have been linked to increased DNA synthesis in tumors and hence SHMT1 can have cancer therapeutic implications . Anti-SHMT1 antibody is specific for SHMT1 in humans.
Immunogeno
Serine hydroxymethyltransferase, cytosolic recombinant protein epitope signature tag (PrEST)
Applicazioni
Anti-SHMT1 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 protein array and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige. Anti-SHMT1 antibody is also suitable for use in indirect immunofluorescence.
Caratteristiche e vantaggi
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:
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 APREST75854
Stato fisico
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Note legali
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Esclusione di responsabilità
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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Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
S B Renwick et al.
Structure (London, England : 1993), 6(9), 1105-1116 (1998-10-01)
Serine hydroxymethyltransferase (SHMT) is a ubiquitous enzyme found in all prokaryotes and eukaryotes. As an enzyme of the thymidylate synthase metabolic cycle, SHMT catalyses the retro-aldol cleavage of serine to glycine, with the resulting hydroxymethyl group being transferred to tetrahydrofolate
Lisa M Nilsson et al.
PLoS genetics, 8(3), e1002573-e1002573 (2012-03-23)
c-Myc (hereafter called Myc) belongs to a family of transcription factors that regulates cell growth, cell proliferation, and differentiation. Myc initiates the transcription of a large cast of genes involved in cell growth by stimulating metabolism and protein synthesis. Some
Stephanie Lucas et al.
Life science alliance, 1(2), e201800036-e201800036 (2018-11-21)
Breakdown of serine by the enzyme serine hydroxymethyltransferase (SHMT) produces glycine and one-carbon (1C) units. These serine catabolites provide important metabolic intermediates for the synthesis of nucleotides, as well as methyl groups for biosynthetic and regulatory methylation reactions. Recently, it
Johannes Meiser et al.
Nature communications, 9(1), 1368-1368 (2018-04-11)
Formate overflow coupled to mitochondrial oxidative metabolism\ has been observed in cancer cell lines, but whether that takes place in the tumor microenvironment is not known. Here we report the observation of serine catabolism to formate in normal murine tissues
Christiaan F Labuschagne et al.
Cell reports, 7(4), 1248-1258 (2014-05-13)
Previous work has shown that some cancer cells are highly dependent on serine/glycine uptake for proliferation. Although serine and glycine can be interconverted and either might be used for nucleotide synthesis and one-carbon metabolism, we show that exogenous glycine cannot
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