Datasheet

Biological Description

Specificity	Anti-PERK Rabbit Antibody [A22L11] detects endogenous levels of total PERK protein.
Background	PERK is a key ER-resident transmembrane kinase that acts as a major sensor and transducer of endoplasmic reticulum (ER) stress, playing a vital role in cellular homeostasis and fate determination. PERK contains an ER luminal domain that detects accumulation of misfolded proteins, and a cytoplasmic kinase domain that gets activated by homodimerization and autophosphorylation upon ER stress. Activated PERK phosphorylates the eukaryotic initiation factor 2 alpha (eIF2α) at Ser51, attenuating global protein synthesis to reduce the load of new proteins entering the ER while selectively upregulating stress response genes via transcription factors such as ATF4. This regulatory mechanism balances cell survival through autophagy or triggers apoptosis under prolonged stress. PERK activity is intricately regulated by its association with ER chaperones such as GRP78 (BiP), as well as by phosphorylation of critical residues within its kinase domain. PERK is present at mitochondria-associated membranes (MAMs), where it mediates ER-mitochondrial crosstalk that is crucial for oxidative stress sensing and apoptotic signaling. Pharmacological inhibition of PERK reduces pathology in neurodegenerative disease models but can cause side effects, indicating the importance of precise regulation. Among ER stress sensors, PERK modulates cell fate decisions, acting as a potential therapeutic target for diseases characterized by ER stress and protein misfolding.

Specificity

Anti-PERK Rabbit Antibody [A22L11] detects endogenous levels of total PERK protein.

Background

PERK is a key ER-resident transmembrane kinase that acts as a major sensor and transducer of endoplasmic reticulum (ER) stress, playing a vital role in cellular homeostasis and fate determination. PERK contains an ER luminal domain that detects accumulation of misfolded proteins, and a cytoplasmic kinase domain that gets activated by homodimerization and autophosphorylation upon ER stress. Activated PERK phosphorylates the eukaryotic initiation factor 2 alpha (eIF2α) at Ser51, attenuating global protein synthesis to reduce the load of new proteins entering the ER while selectively upregulating stress response genes via transcription factors such as ATF4. This regulatory mechanism balances cell survival through autophagy or triggers apoptosis under prolonged stress. PERK activity is intricately regulated by its association with ER chaperones such as GRP78 (BiP), as well as by phosphorylation of critical residues within its kinase domain. PERK is present at mitochondria-associated membranes (MAMs), where it mediates ER-mitochondrial crosstalk that is crucial for oxidative stress sensing and apoptotic signaling. Pharmacological inhibition of PERK reduces pathology in neurodegenerative disease models but can cause side effects, indicating the importance of precise regulation. Among ER stress sensors, PERK modulates cell fate decisions, acting as a potential therapeutic target for diseases characterized by ER stress and protein misfolding.

Usage Information

Application

WB, IP, IHC

Dilution

WB	IP	IHC
1:1000	1:50	1:1000 - 1:4000

Reactivity

Human

Source

Rabbit

MW

140 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/24180212/
https://pubmed.ncbi.nlm.nih.gov/26225772/

Anti-PERK Rabbit Antibody [A22L11]

Biological Description

Usage Information

References

Application Data