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GERPN1236

Anti-GST HRP Conjugate

Cytiva RPN1236, pack of 75 μL

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

conjugate

peroxidase conjugate

antibody product type

primary antibodies

packaging

pack of 75 μL

manufacturer/tradename

Cytiva RPN1236

color

Colorless

shipped in

dry ice

storage temp.

−20°C

General description

Anti-GST HRP Conjugate.

Application

GST is a commonly used expression marker in cloning that is also used for purification and detection of fusion Proteins. This highly specific antibody to GST is conjugated to horseradish peroxidase and optimized for use in Western blotting with ECL Detection Reagents.
GST is a commonly used expression marker in cloning that is also used for purification and detection of fusion Proteins. This highly specific antibody to GST is conjugated to horseradish peroxidase and optimized for use in Western blotting with ECL Detection Reagents.

Features and Benefits

  • Offers the advantages of speed, sensitivity, increased safety, and convenience when used with ECL detection systems. Application tested with ECL and ECL Plus reagents in western blotting for sensitive hard copy results
  • Detection of GST is simplified because no secondary antibody is required
  • The conjugate recognizes multiple epitopes of GST and therefore is not reliant on functional GST for fusion Protein detection. It has also been cross-absorbed to E. coli Proteins so that GST-fusion Proteins can be easily and specifically identified against an E. coli background.
  • Binds with high affinity to GST fusion Proteins.
  • Also suitable for colorimetric detection with diaminobenzidine (DAB) and tetramethylbenzidine (TMB).
  • ECL optimized protocols included.

Storage and Stability

Please be aware this product may be shipped 90 days before the expiration date. For more information on the batch specific expiration date, please contact technical service.
Store at 4 to 30 °C ()

Analysis Note

To view the Certificate of Analysis for this product, please visit www.cytiva.com.

Legal Information

GST Gene Fusion Vectors
A license for commercial use of GST Gene Fusion Vectors under US patent 5,654,176 and equivalent patents and patent applications in other countries must be obtained from Millipore Corp (formerly Chemicon International Inc).
ECL is a trademark of Cytiva

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Storage Class Code

12 - Non Combustible Liquids


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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Asparagine endopeptidase cleaves α-synuclein and mediates pathologic activities in Parkinson's disease.
Zhang Z, et al.
Nature Structural and Molecular Biology, 24(8), 632-632 (2017)
Hannes Vanhaeren et al.
eLife, 9 (2020-03-27)
Protein ubiquitination is a very diverse post-translational modification leading to protein degradation or delocalization, or altering protein activity. In Arabidopsis thaliana, two E3 ligases, BIG BROTHER (BB) and DA2, activate the latent peptidases DA1, DAR1 and DAR2 by mono-ubiquitination at
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The repair of double-stranded DNA breaks (DSBs) by homologous recombination involves the formation of branched intermediates that can lead to crossovers following nucleolytic resolution. The nucleases Mus81-Mms4 and Yen1 are tightly controlled during the cell cycle to limit the extent
Ying Chen et al.
Science advances, 10(11), eadj2570-eadj2570 (2024-03-13)
Ubiquitination plays a crucial role throughout plant growth and development. The E3 ligase DA2 has been reported to activate the peptidase DA1 by ubiquitination, hereby limiting cell proliferation. However, the molecular mechanisms that regulate DA2 remain elusive. Here, we demonstrate
Zhentao Zhang et al.
Nature structural & molecular biology, 24(8), 632-642 (2017-07-04)
Aggregated forms of α-synuclein play a crucial role in the pathogenesis of synucleinopathies such as Parkinson's disease (PD). However, the molecular mechanisms underlying the pathogenic effects of α-synuclein are not completely understood. Here we show that asparagine endopeptidase (AEP) cleaves

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