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The protein encoded by EIF2AK3 phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Additionally we are shipping PERK Kits (20) and PERK Proteins (10) and many more products for this protein.
Showing 10 out of 163 products:
Mouse (Murine) Polyclonal PERK Primary Antibody for IF, IHC (p) - ABIN400976
Harding, Zhang, Ron: Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. in Nature 1999
Show all 8 references for ABIN400976
Human Polyclonal PERK Primary Antibody for IF (cc), IF (p) - ABIN744713
He, Long, Zhong, Fu, Li, Lin: Sustained endoplasmic reticulum stress inhibits hepatocyte proliferation via downregulation of c-Met expression. in Molecular and cellular biochemistry 2014
Show all 4 references for ABIN744713
Human Polyclonal PERK Primary Antibody for EIA, IHC (p) - ABIN360502
Delépine, Nicolino, Barrett, Golamaully, Lathrop, Julier: EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome. in Nature genetics 2000
Show all 3 references for ABIN360502
Human Monoclonal PERK Primary Antibody for ELISA, WB - ABIN969093
Yamaguchi, Larkin, Lara-Lemus, Ramos-Castañeda, Liu, Arvan: Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK. in The Journal of biological chemistry 2008
Show all 2 references for ABIN969093
Human Polyclonal PERK Primary Antibody for IHC (p), WB - ABIN658472
Kim, Moretti, Mitchell, Jung, Lu: Endoplasmic reticulum stress mediates radiation-induced autophagy by perk-eIF2alpha in caspase-3/7-deficient cells. in Oncogene 2010
Show all 2 references for ABIN658472
Mouse (Murine) Polyclonal PERK Primary Antibody for IP, IHC - ABIN233768
Huang, Wu, Chen, Hong: Aquatic birnavirus-induced ER stress-mediated death signaling contribute to downregulation of Bcl-2 family proteins in salmon embryo cells. in PLoS ONE 2011
Human Polyclonal PERK Primary Antibody for IHC (p), WB - ABIN392617
Nakayama, Endo, Tsukano, Mori, Oike, Gotoh: Molecular mechanisms of the LPS-induced non-apoptotic ER stress-CHOP pathway. in Journal of biochemistry 2010
PlGF (show PGF Antibodies) inhibition attenuates PERK activation, likely by tempering hypoxia in HCC (show FAM126A Antibodies) via vessel normalisation. The UPR is able to regulate PlGF (show PGF Antibodies) expression, suggesting the existence of a feedback mechanism for hypoxia-mediated UPR
this study demonstrates novel roles for the endoplasmic reticulum stress-response transducer PERK and a downstream effector of its activation, CHOP (show DDIT3 Antibodies), in tubule cell production of fibronectin (show FN1 Antibodies)
Nck1 silencing in pancreatic beta cells promotes PERK activation and signaling to protect beta cells against pathological stresses.
Nitric oxide can S-nitrosylate the endoplasmic reticulum stress sensors IRE1alapha and PERK.
Results show that PERK-eIF2alpha (show EIF2A Antibodies)-mediated translational failure is a key process leading to neuronal loss in a mouse model of frontotemporal dementia, where the misfolded protein is a form of mutant tau
whole-body or pancreas-specific Perk ablation in mice leads to an increase in IFNAR1 (show IFNAR1 Antibodies) protein levels and signaling in pancreatic tissues.
PGRN (show GRN Antibodies) is a key regulator of insulin (show INS Antibodies) resistance and PGRN (show GRN Antibodies) may mediate its effects, at least in part, by inducing ER stress via the PERK-eIF2alpha (show EIF2A Antibodies) dependent pathway
findings suggest that palmitate increases musclin gene expression via the activation of the PERK signaling pathway in C2C12 myotubes
ER stress-PERK-GSK3alpha/beta signaling promotes proatherogenic macrophage lipid accumulation
interface mutations that disrupt tetramer formation in vitro reduce phosphorylation of PERK and its target eIF2alpha (show EIF2A Antibodies) in cells.
Using drugs that specifically inhibit or activate the PERK or IRE1alpha sensors, we demonstrate that signalling through the PERK axis activates this expression, through a transcriptional mechanism
Data show CGK733 induced microtubule associated protein LC3B (show MAP1LC3B Antibodies) formation upstream of AMP-activated protein kinase (show PRKAA2 Antibodies) and protein kinase (show CDK7 Antibodies) RNA-like endoplasmic reticulum kinase/CCAAT-enhancer-binding protein homologous protein (show DDIT3 Antibodies) pathways and p21 Cip1 (show CDKN1A Antibodies) expression.
Data from 2 consanguineous families suggest EIF2AK3 mutations (c.1337_1338insT/p.K346*; c.3009C>T/p.R903*) account for Wolcott-Rallison syndrome; ultrastructural features of autopsy materials suggest endoplasmic reticulum dysfunction. [CASE STUDIES]
CGK733-induced intracellular calcium sequestration in pancreatic tumor cells is correlated with the PERK/CHOP (show DDIT3 Antibodies) signaling pathway and may also be involved in the dysregulations of calcium-binding proteins.
Data indicated that the relative timing of IRE1 and PERK signalling determines the shift from cell survival to apoptosis.
In human alveolar epithelial A549 cells, Lipopolysaccharide induces autophagic cell death that depends on the activation of the PERK branch of the unfolded protein response upon endoplasmic reticulum (ER) stress .
In this review, we particularly focused on the novel, intriguing and complicated role of PERK in ER stress-decided cell fate, and also discussed more roles of PERK in restoring cellular homeostasis
This study demonstrates a new role for CREB (show CREB1 Antibodies) as a regulator of ER stress, which is required to properly respond to stressful conditions, such as hypoxia.
PERK-activated osteosarcomatous autophagy via inhibition of the mTORC1 pathway prevents cell apoptosis.
The protein encoded by this gene phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. It is a type I membrane protein located in the endoplasmic reticulum (ER), where it is induced by ER stress caused by malfolded proteins. Mutations in this gene are associated with Wolcott-Rallison syndrome.
eukaryotic translation initiation factor 2-alpha kinase 3
, eukaryotic translation initiation factor 2-alpha kinase 3-like
, PRKR-like endoplasmic reticulum kinase
, pancreatic eIF2-alpha kinase
, eukaryotic translation initiation factor 2 alpha kinase 3
, pancreatic EIF2-alpha kinase