BAK1
- Known as:
- BAK1
- Catalog number:
- 002402A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- BAK1
Related genes to: BAK1
- Gene:
- BAK1 NIH gene
- Name:
- BCL2 antagonist/killer 1
- Previous symbol:
- CDN1
- Synonyms:
- BCL2L7, BAK
- Chromosome:
- 6p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-09
- Date modifiied:
- 2016-02-24
Related products to: BAK1
Anserine BCL2 Antagonist_Killer 1 Elisa Kit (BAK1)Anserine anti - BCL2 Antagonist_Killer 1 Elisa Kit (BAK1)anti-BAK1 / BAKanti-BAK1 / BAK (N-Terminus)Anti-BAK1, Rabbit Polyclonal to BAK1, Isotype , Host RabbitAnti-BAK1, Rabbit Polyclonal to BAK1, Isotype , Host RabbitAntibodies: BAK1 HOST: Goat Clonality: pAbAntibody: BAK1 | BRI1-ASSOCIATED RECEPTOR KINASE 1, Host: rabbit, polyclonal, Confirmed reactivity: Arabidopsis thalianaBAIAP2L2 Gene BAI1-associated protein 2-like 2Bak Polyclonal Antibody, Reactivity: H M R, Gene ID: 578, Synonyms: BAK1Bak Polyclonal Antibody, Reactivity: H M R, Gene ID: 578, Synonyms: BAK1Bak Polyclonal Antibody, Reactivity: H, Gene ID: 578, Synonyms: BAK1Bak Polyclonal Antibody, Reactivity: H, Gene ID: 578, Synonyms: BAK1BAK1 AntibodyBAK1 Over-expression Lysate Related articles to: BAK1
- Systemic lupus erythematosus (SLE) is a prototypical autoimmune disease with complex pathogenesis. Mitochondrial dysfunction and aberrant cell death are key drivers, but the mitoxyperiosis pathway has not been explored in SLE. This study aimed to evaluate mitoxyperiosis-associated gene expression in SLE, construct a diagnostic model, identify molecular subtypes, and characterize immune-inflammatory correlations. - Source: PubMed
Publication date: 2026/09/24
Gu BingjieYang LeileiWang XiaoqinSu Dinglei - This study investigated how inflammatory cell death-associated regulators influence the prognosis of lung adenocarcinoma (LUAD) and elucidated their underlying mechanisms. - Source: PubMed
Yang YalunLiu DiMa Shengwei - Tomato (Solanum lycopersicum), a cornerstone of global agriculture and nutrition, has undergone decades of breeding focused on yield and stress resilience. Yet, consumer-driven traits such as fruit uniformity, flavor complexity, and nutritional value remain suboptimal. The emerging convergence of hormonal biology and precision genome editing presents a transformative approach to addressing this gap. Brassinosteroids (BRs), a class of steroidal phytohormones, act as central regulators of cell expansion, tissue patterning, and developmental plasticity. Their signaling cascade, initiated by perception at the BRI1-BAK1 receptor complex and transduced via BES1/BZR1 transcriptional modules, intersects with networks controlling fruit set, morphology, ripening, and stress adaptation. Gene editing through CRISPR/Cas9 technology now enables targeted dissection and manipulation of these BR-regulated nodes with unprecedented accuracy. CRISPR/Cas9 studies have directly characterized BR signaling regulators such as SlBZR1, SlBIN2, and SlBES1, while complementary genetic and transgenic studies have provided functional evidence for other BR-related components, including SlBRI1 and the BR-biosynthetic gene SlDWF4, further supporting the roles of BR signaling in tomato fruit development, ripening, and carotenoid accumulation. Beyond improvement of traits, CRISPR/Cas9 offers the potential to tune BR pathways and their crosstalk with auxin and ethylene, providing a systems-level framework for engineering climate-resilient and nutritionally superior cultivars. This review integrates mechanistic insights into BR signaling with cutting-edge CRISPR/Cas9 applications, positioning tomato as a model for reprogramming fruit development and as a paradigm for next-generation crop improvement. - Source: PubMed
Publication date: 2026/09/09
Tahira MaryamSu WenranMaqsood Faizan KhurramIkram MuhammadJavaid Muhammad HaseebRao Muhammad JunaidZhang Junhong - Plants balance gas exchange with pathogen defense through dynamic stomatal regulation. Stomata close temporarily during pathogen attack to limit invasion, then reopen to restore photosynthesis and transpiration while lowering apoplast water saturation to inhibit pathogen proliferation. The secreted peptides, SCREW/CTNIP promote stomatal reopening through the receptor NUT/HSL3 and co-receptor BAK1/SERK3, thereby counteracting ABA and MAMP-triggered stomatal closure. Here we present the cryo-EM structures of AtNUTECD and the AtNUTECD-SCREW2/CTNIP4-AtBAK1ECD complex, uncovering a distinctive peptide-receptor interaction mechanism. SCREW2 adopts a unique cross-ribbon conformation that distinguishes it from other known conformations of LRR-RK-binding peptides, enabling its specific recognition by AtNUT and subsequent recruitment of AtBAK1. An N-linked glycan at N449 within the SCREW2-AtNUT binding interface is required for efficient SCREW2 recognition. Mutations in SCREW2 recognition sites significantly attenuated downstream MAPK activation and PTI marker gene expression. - Source: PubMed
Publication date: 2026/09/17
Wei XiaobinYao MengyiZhao PingpingZhang XinZhang KaiHu WenShi JiaqingGuo ShuangyuLi RuxinWang WeiXu YouweiGuo SiyiXu H EricSong Chun-Peng - Secreted cysteine-rich peptides (CRPs) are vital plant signalling molecules, yet how their essential intramolecular disulfide bonds structurally mediate receptor complex activation is poorly understood. Here we present the crystal structure of an Arabidopsis immune complex comprising the CRP SMALL PHYTOCYTOKINES REGULATING DEFENSE AND WATER LOSS (SCREW), the receptor PLANT SCREW UNRESPONSIVE RECEPTOR (NUT) and the coreceptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR KINASE 1 (BAK1). Unlike typical multi-disulfide CRPs with compact folds, SCREW maintains a flexible loop constrained into a neck-ring-like conformation through stabilization by a single disulfide bond and a critical proline residue. In the complex, SCREW's carboxy-terminal cyclic region inserts between NUT and BAK1, burying a large surface area on BAK1. Disrupting this neck-ring-like conformation or its key interfaces abolishes complex assembly and downstream signalling. This assembly mechanism is conserved in rapeseed and probably among other dicots. Our work reveals a distinct disulfide-dependent conformation, critical for receptor activation and potentially common among two-cysteine CRPs. - Source: PubMed
Publication date: 2026/09/17
Wang ZhiyunWan LihaoTang SiqiWang XiaochenYang YueWu HuiminZhang ShaoranYu XiaoXu Shutong