[Lys(Ac)382]-p53 (361-393), human, biotin-labeled, amide

Product Name: [Lys(Ac)382]-p53 (361-393), human, biotin-labeled, amide

Sequence One Letter Code: Biotin-LC-GSRAHSSHLKSKKGQSTSRHK-K(Ac)-LMFKTEGPDSD-NH2

Sequence Three Letter Code: Biotin-LC-Gly-Ser-Arg-Ala-His-Ser-Ser-His-Leu-Lys-Ser-Lys-Lys-Gly-Gln-Ser-Thr-Ser-Arg-His-Lys-Lys(Ac)-Leu-Met-Phe-Lys-Thr-Glu-Gly-Pro-Asp-Ser-Asp-NH2

Molecular Weight: 4034.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: This peptide is derived from residues 361–393 of the human tumor suppressor protein p53 and contains acetylation at lysine 382, a critical regulatory post-translational modification. Acetylation at this site enhances p53 stability and transcriptional activity by reducing ubiquitination mediated by the MDM2 E3 ligase. The peptide includes an N-terminal biotin label that enables immobilization on streptavidin surfaces for affinity-based assays. This configuration facilitates studies of protein–protein interactions and recognition of acetylated p53 by regulatory proteins. The peptide is widely used to investigate mechanisms controlling p53 activation, DNA damage responses, and tumor suppressor regulation. It supports cancer research focused on post-translational modification–dependent control of p53 function.

Current Research: The tumor suppressor protein p53 is one of the most important regulators of cellular responses to stress, DNA damage, and oncogenic transformation. Acting primarily as a transcription factor, p53 controls the expression of genes involved in cell cycle arrest, apoptosis, senescence, and DNA repair. Because of its central role in preventing malignant transformation, p53 activity is tightly regulated by multiple mechanisms, including post-translational modifications (PTMs) such as phosphorylation, ubiquitination, methylation, and acetylation. Synthetic peptides derived from key regulatory regions of p53 are widely used to investigate these molecular mechanisms. One such reagent is the biotinylated p53 (361–393) peptide containing acetylation at lysine 382 (K382ac). The Role of p53 in Cellular Stress Responses Under normal physiological conditions, p53 levels remain low due to continuous degradation mediated by MDM2, an E3 ubiquitin ligase that targets p53 for proteasomal destruction. This interaction keeps p53 activity suppressed in unstressed cells. However, when cells experience DNA damage, oxidative stress, or oncogenic signaling, a network of signaling pathways activates p53. These signals lead to stabilization and activation of the protein, enabling it to function as a transcription factor that orchestrates protective cellular responses. Once activated, p53 can halt cell cycle progression to allow DNA repair or trigger programmed cell death if damage is irreparable. The regulation of p53 stability and activity depends heavily on post-translational modifications within its C-terminal regulatory domain, where lysine residues serve as key modification sites. Acetylation at Lysine 382 One of the most extensively studied modifications in the p53 C-terminal region is acetylation at lysine 382 (K382). This modification is catalyzed by histone acetyltransferases such as p300/CBP and PCAF, which are recruited in response to cellular stress signals. Acetylation at K382 has several important functional consequences: Enhanced transcriptional activity of p53 Increased protein stability Reduced ubiquitination by MDM2 Improved recruitment of transcriptional coactivators Normally, MDM2 binds to p53 and promotes ubiquitination of lysine residues within the C-terminal region, leading to p53 degradation. When lysine 382 becomes acetylated, this modification interferes with MDM2-mediated ubiquitination, helping stabilize the p53 protein and sustain its transcriptional activity. Because of these regulatory effects, K382 acetylation plays a critical role in controlling how cells respond to DNA damage and stress signals. Peptide Design and Biotin Tagging The p53 (361–393) peptide corresponds to a segment of the C-terminal regulatory region of human p53 that includes lysine 382. In this synthetic version, the lysine residue is specifically modified with an acetyl group, reproducing the regulatory modification found in activated p53. To support experimental applications, the peptide also contains an N-terminal biotin label. Biotin binds with extremely high affinity to streptavidin, allowing the peptide to be easily immobilized on streptavidin-coated beads, plates, or biosensor surfaces. This configuration creates a stable platform for affinity-based assays and biochemical experiments focused on interactions involving acetylated p53. Studying Protein–Protein Interactions One of the primary applications of the biotinylated p53 (361–393) K382ac peptide is the study of protein–protein interactions involving the p53 regulatory domain. Many cellular proteins recognize or bind to acetylated p53, influencing its stability and transcriptional activity. Using immobilized peptide assays, researchers can examine how regulatory proteins interact with acetylated p53. These studies help identify proteins that act as: Transcriptional coactivators Chromatin regulators Acetylation “reader” proteins p53 modulators involved in stress responses By isolating and characterizing these interactions, scientists gain insight into how p53 signaling networks function at the molecular level. Applications in Cancer Research Mutations or dysregulation of the p53 pathway occur in more than half of human cancers, making it one of the most important targets in cancer biology. Understanding how post-translational modifications regulate p53 activity is therefore critical for developing therapeutic strategies aimed at restoring tumor suppressor function. The biotinylated p53 (361–393) Ac-Lys382 peptide supports a range of experimental applications relevant to cancer research, including: Affinity pull-down assays identifying proteins that bind acetylated p53 Enzyme activity studies examining acetyltransferases or deacetylases Screening assays for compounds that influence p53 regulatory pathways Mechanistic studies of DNA damage signaling and transcriptional activation These experiments help clarify how modification-dependent regulation of p53 contributes to tumor suppression and cellular stress responses. Advancing Understanding of p53 Regulation The activity of p53 is controlled by a complex network of signaling pathways and molecular interactions. Synthetic peptides that replicate specific regulatory modifications provide researchers with a powerful way to isolate and study individual components of this system. The biotinylated p53 (361–393) peptide containing acetylated lysine 382 offers a well-defined experimental model of a key regulatory modification in the p53 pathway. By enabling detailed investigation of acetylation-dependent protein interactions and signaling mechanisms, this peptide continues to support advances in cancer biology, DNA damage research, and tumor suppressor regulation.