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MABE342

Sigma-Aldrich

Anti-Puromycin Antibody, clone 4G11

clone 4G11, from mouse

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100 μL
$498.00

$498.00


Estimated to ship onMarch 29, 2025

A recombinant, preservative-free antibody is available for your target. Try ZMS1016

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100 μL
$498.00

About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
clone:
4G11, monoclonal
application:
FACS
ICC
IF
WB
species reactivity:
human
technique(s):
flow cytometry: suitable
immunocytochemistry: suitable
immunofluorescence: suitable
western blot: suitable
citations:
21

$498.00


Estimated to ship onMarch 29, 2025

A recombinant, preservative-free antibody is available for your target. Try ZMS1016

Request a Bulk Order

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

4G11, monoclonal

species reactivity

human

species reactivity (predicted by homology)

all

technique(s)

flow cytometry: suitable
immunocytochemistry: suitable
immunofluorescence: suitable
western blot: suitable

isotype

IgG1κ

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... NPEPPS(9520)

Related Categories

General description

Puromycin is an aminonucleoside antibiotic, derived from the Streptomyces alboniger bacterium, that functions as a protein synthesis inhibitor that blocks translation through premature chain termination in the ribosome. Monoclonal antibodies to puromycin may be used with standard immunochemical methods to directly monitor translation, a method known as surface sensing of translation (SUnSET). Part of the molecule resembles the 3′ end of the aminoacylated tRNA, making it useful for protein translation analysis. Puromycin induces DNA fragmentation in thymocytes and in human HL-60 leukemia cells.

Specificity

Demonstrated to react with Human test sample, preincubated with Puromycin. Predicted to react with all species when test sample is incubated with Puromycin.

application

Anti-Puromycin antibody, clone 4G11 detects puromycin incorporated into protein. Monoclonal antibodies to puromycin may also be used with standard immunochemical methods.
Immunocytochemistry Analysis: A 1:2,000 dilution from a representative lot detected Puromycin-incorporated neosynthesized proteins in HeLa cells treated with Puromycin. However, a decrease in signal is observed with the addition of Cycloheximide, an inhibitor of protein biosynthesis in eukaryotic organisms.

Western Blotting Analysis: A representative lot from an independent laboratory detected Puromycin-incorporated neosynthesized proteins in WB (David, A., et al. (2012). J Cell Biol. 197(1):45-57.; Schmidt, E., K., et al. (2009). Nat Methods. 6(4):275-277.).

Immunofluorescence Analysis: A representative lot from an independent laboratory detected Puromycin-incorporated neosynthesized proteins in IF (David, A., et al. (2012). J Cell Biol. 197(1):45-57.; Schmidt, E., K., et al. (2009). Nat Methods. 6(4):275-277.).

Fluorescence Activated Cell Sorting Analysis: A representative lot from an independent laboratory detected Puromycin-incorporated neosynthesized proteins in FACS (David, A., et al. (2012). J Cell Biol. 197(1):45-57.; Schmidt, E., K., et al. (2009). Nat Methods. 6(4):275-277.).

Alexa Fluor is a registered trademark of Life Technologies.

Quality

Evaluated by Western Blotting in HEK293 cell lysates treated with Puromycin and Cyclohexamide, or with Puromycin only.

Western Blotting Analysis: A 1:12,500 dilution of this antibody detected Puromycin-incorporated neosynthesized proteins in HEK293 cell lysates treated with Puromycin only. This antibody also detected small mounts of puromycin in HEK293 cells treated with Puromycin and Cyclohexamide.

Target description

Puromycin is incorporated in neosynthesized proteins. In the presense of Puromycin only, this antibody detects Puromycin-incorporated neosynthesized proteins at multiple molecular weights. However, a decrease in signal is observed in the co-presense of Cycloheximide, an inhibitor of protein biosynthesis in eukaryotic organisms.

Physical form

Format: Purified

Legal Information

ALEXA FLUOR is a trademark of Life Technologies

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Paul A Roberson et al.
Frontiers in nutrition, 7, 628405-628405 (2021-02-02)
Introduction: Amino acid transporters are essential for cellular amino acid transport and promoting protein synthesis. While previous literature has demonstrated the association of amino acid transporters and protein synthesis following acute resistance exercise and amino acid supplementation, the chronic effect
Yong-Jie Zhang et al.
Nature medicine, 24(8), 1136-1142 (2018-06-27)
The major genetic cause of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) is a C9orf72 G4C2 repeat expansion1,2. Proposed mechanisms by which the expansion causes c9FTD/ALS include toxicity from repeat-containing RNA and from dipeptide repeat proteins translated from these
Joni Vanneste et al.
Scientific reports, 9(1), 15728-15728 (2019-11-02)
Repeat expansions in the C9orf72 gene cause amyotrophic lateral sclerosis and frontotemporal dementia characterized by dipeptide-repeat protein (DPR) inclusions. The toxicity associated with two of these DPRs, poly-GR and poly-PR, has been associated with nucleocytoplasmic transport. To investigate the causal
Joshua M Dewe et al.
Molecular and cellular biology, 37(21) (2017-08-09)
Mutations in the tRNA methyltransferase 1 (TRMT1) gene have been identified as the cause of certain forms of autosomal-recessive intellectual disability (ID). However, the molecular pathology underlying ID-associated TRMT1 mutations is unknown, since the biological role of the encoded TRMT1
J Max Michel et al.
Experimental physiology, 108(10), 1268-1281 (2023-08-17)
We recently reported that vastus lateralis (VL) cross-sectional area (CSA) increases after 7 weeks of resistance training (RT, 2 days/week), with declines occurring following 7 weeks of subsequent treadmill high-intensity interval training (HIIT) (3 days/week). Herein, we examined the effects of this training paradigm

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