Datasheet

Biological Description

Specificity	Acetyl-p53 (Lys382) Antibody [K2J24] detects endogenous levels of p53 only when acetylated at lysine 382.
Background	Acetyl-p53 (Lys382) refers to the tumor suppressor protein p53 that has undergone acetylation at its conserved carboxyl-terminal lysine 382, a key post-translational modification regulating its stability and activity. Structurally, p53 is a 393-amino acid transcription factor composed of an N-terminal transactivation domain, a central DNA-binding domain, an oligomerization domain, and a C-terminal regulatory domain where Lys382 resides. Acetylation at Lys382, mediated mainly by histone acetyltransferases such as p300/CBP and PCAF, enhances p53’s DNA-binding affinity, prevents MDM2-mediated degradation, and promotes its accumulation in the nucleus. Acetyl-p53 (Lys382) is widely expressed in mammalian cells but its levels are tightly controlled and increase under stress conditions such as DNA damage, oxidative stress, or treatment with histone deacetylase inhibitors (HDACi). Functionally, acetylation at Lys382 not only augments the transcriptional activity of p53 in driving the expression of cell cycle regulators (e.g., p21) and proapoptotic genes (e.g., BAX, PUMA, DR5), but also facilitates its transcription-independent roles at mitochondria. Specifically, Lys382 acetylation enables p53 to disrupt the inhibitory Ku70-BAX complex, thereby freeing BAX to translocate to mitochondria, generate reactive oxygen species, and promote apoptosis. Thus, Acetyl-p53 (Lys382) represents a critical molecular switch integrating stress responses, tumor suppression, and apoptosis.

Specificity

Acetyl-p53 (Lys382) Antibody [K2J24] detects endogenous levels of p53 only when acetylated at lysine 382.

Background

Acetyl-p53 (Lys382) refers to the tumor suppressor protein p53 that has undergone acetylation at its conserved carboxyl-terminal lysine 382, a key post-translational modification regulating its stability and activity. Structurally, p53 is a 393-amino acid transcription factor composed of an N-terminal transactivation domain, a central DNA-binding domain, an oligomerization domain, and a C-terminal regulatory domain where Lys382 resides. Acetylation at Lys382, mediated mainly by histone acetyltransferases such as p300/CBP and PCAF, enhances p53’s DNA-binding affinity, prevents MDM2-mediated degradation, and promotes its accumulation in the nucleus. Acetyl-p53 (Lys382) is widely expressed in mammalian cells but its levels are tightly controlled and increase under stress conditions such as DNA damage, oxidative stress, or treatment with histone deacetylase inhibitors (HDACi). Functionally, acetylation at Lys382 not only augments the transcriptional activity of p53 in driving the expression of cell cycle regulators (e.g., p21) and proapoptotic genes (e.g., BAX, PUMA, DR5), but also facilitates its transcription-independent roles at mitochondria. Specifically, Lys382 acetylation enables p53 to disrupt the inhibitory Ku70-BAX complex, thereby freeing BAX to translocate to mitochondria, generate reactive oxygen species, and promote apoptosis. Thus, Acetyl-p53 (Lys382) represents a critical molecular switch integrating stress responses, tumor suppression, and apoptosis.

Usage Information

Application

WB, IF, FCM

Dilution

WB	IF	FCM
1:250 - 1:5000	1:100 - 1:250	1:20

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

53 kDa

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

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/19265193/

Acetyl-p53 (Lys382) Antibody [K2J24]

Biological Description

Usage Information

References

Application Data