Acetyl-p53 (Lys120) Antibody [P22N5]

Application: Reactivity: Human

Lane 1: 293, Lane 2: HT29, Lane 3: COS

Usage Information

Dilution
WB1:2000 IF1:1000 FCM1:100

Application
WB, IF, FCM

Reactivity
Human

Source
Mouse 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
43 kDa

Datasheet & SDS

Biological Description

Specificity
Acetyl-p53 (Lys120) detects endogenous levels of p53 protein only when acetylated at Lys 120.

Clone
[P22N5]

Synonym(s)
P53; TP53; Cellular tumor antigen p53; Antigen NY-CO-13; Phosphoprotein p53; Tumor suppressor p53

Background
Acetyl-p53 at lysine 120 (AcK120-p53) is a post-translationally modified form of the tumor suppressor protein p53, a key transcription factor that mediates cellular responses to stress, including DNA damage repair, apoptosis, and cell cycle arrest. Lys120 is located within the DNA-binding domain (DBD) of p53 and is acetylated by MYST family acetyltransferases such as TIP60 and hMOF in response to genotoxic stress. This acetylation does not substantially alter the DBD fold but increases the flexibility and conformational dynamics of loop L1, thereby enhancing p53’s ability to selectively recognize specific DNA response elements, with a preference for pro-apoptotic gene promoters like BAX and PUMA. Acetylation at Lys120 is essential for efficient p53-mediated apoptosis. It promotes the transcription of pro-apoptotic genes and supports p53’s transcription-independent roles at mitochondria, such as displacing anti-apoptotic proteins like MCL-1. This modification also influences the quaternary structure of p53, favoring tetrameric forms that bind DNA with higher affinity and specificity. Loss or mutation of Lys120 impairs p53-driven apoptosis, shifting cell fate toward cell cycle arrest rather than cell death, with significant implications for tumorigenesis and cancer progression.

Background

Acetyl-p53 at lysine 120 (AcK120-p53) is a post-translationally modified form of the tumor suppressor protein p53, a key transcription factor that mediates cellular responses to stress, including DNA damage repair, apoptosis, and cell cycle arrest. Lys120 is located within the DNA-binding domain (DBD) of p53 and is acetylated by MYST family acetyltransferases such as TIP60 and hMOF in response to genotoxic stress. This acetylation does not substantially alter the DBD fold but increases the flexibility and conformational dynamics of loop L1, thereby enhancing p53’s ability to selectively recognize specific DNA response elements, with a preference for pro-apoptotic gene promoters like BAX and PUMA. Acetylation at Lys120 is essential for efficient p53-mediated apoptosis. It promotes the transcription of pro-apoptotic genes and supports p53’s transcription-independent roles at mitochondria, such as displacing anti-apoptotic proteins like MCL-1. This modification also influences the quaternary structure of p53, favoring tetrameric forms that bind DNA with higher affinity and specificity. Loss or mutation of Lys120 impairs p53-driven apoptosis, shifting cell fate toward cell cycle arrest rather than cell death, with significant implications for tumorigenesis and cancer progression.

References
https://pubmed.ncbi.nlm.nih.gov/27338200/ https://pubmed.ncbi.nlm.nih.gov/21525412/

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%