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Human BAK1 Protein expressed in Wheat germ - ABIN1346390
Lindner, Concannon, Boukes, Cannon, Llambi, Ryan, Boland, Kehoe, McNamara, Murray, Kay, Hector, Green, Huber, Prehn: Systems analysis of BCL2 protein family interactions establishes a model to predict responses to chemotherapy. in Cancer research 2013
These results suggest that pleiotropic phenotypic alterations shown in the BAK1- overexpressing transgenic plants result from the constitutive activation of SA-mediated defense responses.
The study reveals the signaling activation mechanism in floral organ abscission by IDA-induced HAE/HSL2-SERK complex formation accompanied by transphosphorylation.
Receptor like kinases (RLP)-mediated resistance and endocytosis require ligand-induced recruitment of BAK1/SERK3, reminiscent of BAK1/SERK3 interaction and subcellular fate of the FLAGELLIN (show FliC Proteins) SENSING 2 (FLS2) RLK (show TXK Proteins).
G protein signaling is directly activated by the pathogen-associated molecular pattern flagellin (show FliC Proteins) peptide 22 through its LRR RLK (show TXK Proteins), FLS2, and co-receptor BAK1.
BAK1 disruption stimulates the release of PROPEP3, produced in response to Pep application and during pathogen challenge, and renders PEPRs necessary for basal resistance.
mutation of suppressor of BIR1 (show KCNJ6 Proteins)-1, which encodes an emerging positive regulator of transmembrane receptors in plants, suppressed the effects of BAK1 overexpression.
SERK1 or SERK2 extracellular domains are essential for SERK function in male sporogenesis, while the SERK3 extracellular and cytoplasmic domains are essential for SERK3 activity in brassinosteroid and flagellin (show FliC Proteins) signaling.
Data indicate protein kinases FLS2 and BAK1 contribute to autoimmune signaling in ACCELERATED CELL DEATH6 (ACD6 (show EHMT2 Proteins)) L591F amino acid substitution.
Arabidopsis plants expressing FLS2 with the Q530A+Q627A double mutation were impaired both in detectable interaction with BAK1 and in FLS2-mediated responses, lending overall support to current models of FLS2 structure and function.
Using MALDI-TOF (show FEZF2 Proteins) MS, we identified Cys353, Cys374 and Cys408 as potential sites of glutathionylation on the BAK1 cytoplasmic domain and directed mutagenesis suggests that Cys353 and Cys408 are major sites of GRXC2-mediated glutathionylation.
interleukin-6 (show IL6 Proteins), endothelin ET-1 (show EDN1 Proteins), and apoptotic Bak and Bcl-XL (show BCL2L1 Proteins) genes have roles in small bowel transplantation, in a swine model of ischemia and reperfusion injury
Bak mRNA was significantly increased in haploid parthenotes compared with the diploid parthenotes. These results suggest that the haploid state affects apoptosis-related gene expression which results in increased apoptosis
The low-level constitutive production of platelets caused by the G allele of rs5745568 in BAK1 protein seems to increase the risk of bleeding in dengue infection
the expression of Bak1 was downregulated in CRC (show CALR Proteins) tumor tissues and was reversely correlated with the expression of miR410, which provided further support that Bak1 was regulated by miR410.
Low expression of BAX (show BAX Proteins) is associated with docetaxel resistance in gastric cancer.
Polymorphisms of KITLG (show KITLG Proteins), SPRY4 (show SPRY4 Proteins), and BAK1 genes in patients with testicular germ cell tumors and individuals with infertility associated with AZFc deletion of the Y chromosome
Different selenium concentrations had varying effects on BAK1 and APAF1 (show APAF1 Proteins) levels. APAF1 (show APAF1 Proteins) may play an important role in the pathogenesis of KBD
Findings argue for auto-activation of Bak in the absence of anti-apoptotic Bcl-2 (show BCL2 Proteins) proteins and provide evidence of profound differences in the activation of Bax (show BAX Proteins) and Bak.
LTX-315 kills cancer cells through Bax (show BAX Proteins)/Bak-regulated mitochondrial membrane permeabilization
E6 proteins of human papillomavirus types 6 and 11 are able to protect keratinocytes from apoptosis via Bak degradation.
A Novel Naphthalimide Compound Restores p53 (show TP53 Proteins) Function in Non-small Cell Lung Cancer by Reorganizing the Bak.Bcl-xl Complex and Triggering Transcriptional Regulation.
Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains.
The authors show that Bak is activated and that activated Bak is bound to p53 (show TP53 Proteins) during reovirus encephalitis.
Pancreatic beta-Cell Death due to Pdx-1 (show PDX1 Proteins) Deficiency Requires Multi-BH Domain Protein Bax (show BAX Proteins) but Not Bak.
lipid profile in the absence of the proapoptotic proteins BAX (show BAX Proteins) and BAK in mouse embryonic fibroblasts
alpha1 dissociation is a key step in unfolding Bak into three major components, the N terminus, the core (alpha2-alpha5) and the latch (alpha6-alpha8) that is required for apoptosis.
BAX (show BAX Proteins) and BAK have a nonapoptotic role in eicosanoid metabolism in inflammation.
Puma (show BBC3 Proteins) is the major mediator of virus-induced Bax (show BAX Proteins)/Bak activation and mitochondrial membrane permeabilization induction.
Motifs of VDAC2 (show VDAC2 Proteins) required for mitochondrial Bak import and tBid-induced apoptosis.
dual ablation of Bax (show BAX Proteins) and Bak suppressed ureteral obstruction induced inflammation and kidney fibrosis with decreased tubular cell cycle arrest
bak therefore regulates gastric epithelial cell apoptosis, proliferation, differentiation, mucosal thickness, and susceptibility to gastric atrophy and dysplasia following H. felis infection
Benzo(a)pyrene-7,8-diol-9,10-epoxide induced p53 (show TP53 Proteins)-independent necrosis via the mitochondria-associated pathway involving Bax (show BAX Proteins) and Bak activation
regulation of A1 and Bak contribute to mitochondrial membrane stability, reduced caspase-9 (show CASP9 Proteins) activity, and delayed apoptosis in bovine neutrophils exposed to glucocorticoids
The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.
BCL2-like 7 protein
, apoptosis regulator BAK
, bcl-2 homologous antagonist/killer
, bcl-2-like protein 7
, pro-apoptotic protein BAK
, Bcl2 homologous antagonist/killer
, Bcl-2-like 7