Skip to Content
Merck
All Photos(1)

Documents

A5598

Sigma-Aldrich

Anti-c-Myc−Peroxidase antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-c-Myc antibody produced in rabbit

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

MDL number:
MFCD00239651
UNSPSC Code:
12352203
NACRES:
NA.56

biological source

rabbit

conjugate

peroxidase conjugate

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

concentration

1.8-4 mg/mL

technique(s)

western blot: 1:5,000

UniProt accession no.

P01106

storage temp.

−20°C

Gene Information

human ... MYC(4609)

Looking for similar products? Visit Product Comparison Guide

General description

The Anti-c-Myc peroxidase conjugate rabbit antibody reacts with c-Myc tagged fusion proteins. It recognizes the c-Myc tag sequence expressed at either the amino- or the carboxyl-terminus.

Specificity

N-terminal or C-terminal c-Myc (Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu) tagged fusion proteins.

Immunogen

peptide corresponding amino acids 408-425 of the human c-myc proto-oncogene, conjugated to maleimide-activated KLH through a C-terminal added cysteine residue.

Application

Antibody is suitable for immunoblotting.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Physical form

Solution in 0.01 M sodium phosphate buffer saline, pH 7.4, containing 0.05% MIT

Preparation Note

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

Not finding the right product?  

Try our Product Selector Tool.

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H317

Hazard Classifications

Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Yang Lu et al.
Molecular biology of the cell, 19(10), 4260-4272 (2008-08-08)
Efg1 is essential for hyphal development and virulence in the human pathogenic fungus Candida albicans. How Efg1 regulates gene expression is unknown. Here, we show that Efg1 interacts with components of the nucleosome acetyltransferase of H4 (NuA4) histone acetyltransferase (HAT)
Rodolfo Zentella et al.
Nature chemical biology, 13(5), 479-485 (2017-03-01)
Plant development requires coordination among complex signaling networks to enhance the plant's adaptation to changing environments. DELLAs, transcription regulators originally identified as repressors of phytohormone gibberellin signaling, play a central role in integrating multiple signaling activities via direct protein interactions
Gang Li et al.
Nature cell biology, 13(5), 616-622 (2011-04-19)
The circadian clock controls many metabolic, developmental and physiological processes in a time-of-day-specific manner in both plants and animals. The photoreceptors involved in the perception of light and entrainment of the circadian clock have been well characterized in plants. However
Zirui Zheng et al.
Journal of immunology (Baltimore, Md. : 1950), 196(3), 1199-1208 (2015-12-25)
IFN regulatory factors play a pivotal role in many cellular processes, including inflammatory and immune responses. Their activation is tightly regulated by TANK-binding kinase 1 (TBK1). In response to microbial components, TBK1 activates IFN regulatory factor 3 (IRF3) and cytokine
Du-Hwa Lee et al.
The Plant cell, 29(11), 2895-2920 (2017-11-01)
Dynamic control of protein translation in response to the environment is essential for the survival of plant cells. Target of rapamycin (TOR) coordinates protein synthesis with cellular energy/nutrient availability through transcriptional modulation and phosphorylation of the translation machinery. However, mechanisms
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service