Phospho-c-Myc (Ser62) Antibody [M18C23]

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
62 kDa

Positive Control	KARPAS-299 cells (MG-132, 10 μM, overnight); HCT 116 cells (MG-132, 10 μM, overnight)
Negative Control	KARPAS-299 cells; HCT 116 cells

Datasheet & SDS

Biological Description

Specificity
Phospho-c-Myc (Ser62) Antibody [M18C23] detects endogenous levels of total Myc protein only when it is phosphorylated at Ser62.

Clone
M18C23

Synonym(s)
Myc proto-oncogene protein; Class E basic helix-loop-helix protein 39 (bHLHe39); Proto-oncogene c-Myc; Transcription factor p64; MYC; BHLHE39

Background
Phospho-c-Myc Ser62 refers to the mitogen-induced phosphorylation of serine 62 within the N-terminal transactivation domain of c-Myc, a basic helix-loop-helix leucine zipper transcription factor in the Myc/Max/Mad network that forms heterodimers with Max to bind E-box DNA sequences, regulating a large portion of the genome involved in cell proliferation, metabolism, ribosome biogenesis, and biomass accumulation. Ser62 is located in the conserved Myc box I motif near Thr58, within a proline-rich sequence that enables orderly phosphorylation and interaction with coactivators such as TRRAP, TIP60, and p107. Phosphorylation at Ser62 by kinases like ERK, CDK1/2, or JNK in response to growth factor and Ras signaling stabilizes c-Myc by preventing its ubiquitin-mediated proteasomal degradation through inhibition of Fbw7, and primes it for subsequent phosphorylation at Thr58 by GSK3β, thus regulating Myc turnover and activity. This modification increases c-Myc/Max transcriptional activation of target genes involved in cell cycle progression and regenerative proliferation, supports DNA damage repair by recruiting repair factors, and facilitates oncogenic transformation and metastasis in various cancers, including colorectal, squamous cell, and RAS-mutant lung and pancreatic cancers. Elevated phospho-Ser62 c-Myc levels are linked to therapy resistance, cancer stemness, and poor prognosis.

Background

Phospho-c-Myc Ser62 refers to the mitogen-induced phosphorylation of serine 62 within the N-terminal transactivation domain of c-Myc, a basic helix-loop-helix leucine zipper transcription factor in the Myc/Max/Mad network that forms heterodimers with Max to bind E-box DNA sequences, regulating a large portion of the genome involved in cell proliferation, metabolism, ribosome biogenesis, and biomass accumulation. Ser62 is located in the conserved Myc box I motif near Thr58, within a proline-rich sequence that enables orderly phosphorylation and interaction with coactivators such as TRRAP, TIP60, and p107. Phosphorylation at Ser62 by kinases like ERK, CDK1/2, or JNK in response to growth factor and Ras signaling stabilizes c-Myc by preventing its ubiquitin-mediated proteasomal degradation through inhibition of Fbw7, and primes it for subsequent phosphorylation at Thr58 by GSK3β, thus regulating Myc turnover and activity. This modification increases c-Myc/Max transcriptional activation of target genes involved in cell cycle progression and regenerative proliferation, supports DNA damage repair by recruiting repair factors, and facilitates oncogenic transformation and metastasis in various cancers, including colorectal, squamous cell, and RAS-mutant lung and pancreatic cancers. Elevated phospho-Ser62 c-Myc levels are linked to therapy resistance, cancer stemness, and poor prognosis.

References
https://pubmed.ncbi.nlm.nih.gov/18408012/ https://pubmed.ncbi.nlm.nih.gov/10551811/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%