LAPTM4B antibody Polyclonal Antibodies Primary antibodies
- Known as:
- LAPTM4B (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100545
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- LAPTM4B antibody Polyclonal Antibodies Primary antibodies
Related genes to: LAPTM4B antibody Polyclonal Antibodies Primary antibodies
- Gene:
- LAPTM4B NIH gene
- Name:
- lysosomal protein transmembrane 4 beta
- Previous symbol:
- -
- Synonyms:
- LC27
- Chromosome:
- 8q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-12-16
- Date modifiied:
- 2008-08-11
Related products to: LAPTM4B antibody Polyclonal Antibodies Primary antibodies
Related articles to: LAPTM4B antibody Polyclonal Antibodies Primary antibodies
- This study aims to reveal the potential mechanism and potential prognostic markers of programmed cell death (PCD) genes associated with 6-acetoxy-anopterine (6-AA) resistance in prostate adenocarcinoma (PRAD). - Source: PubMed
Publication date: 2026/01/31
Cheng JieMao Dongdong - Lysosomal-associated protein transmembrane (LAPTM) family members-LAPTM4A, LAPTM4B, and LAPTM5-regulate lysosomal integrity, autophagy-lysosome flux, lipid homeostasis, and immune signaling, pathways increasingly implicated in neurological disease. This review synthesizes structure-function evidence for LAPTM proteins and examines how their dysregulation contributes to Alzheimer's and Parkinson's disease, ischemia-reperfusion injury, and gliomas. Based on a targeted narrative analysis of primary and translational studies, we highlight that LAPTM proteins influence lysosomal acidification and membrane stability, endolysosomal trafficking, and ceramide/ion handling, thereby shaping protein aggregate clearance, oxidative stress responses, and microglia/macrophage polarization. Preclinical data link LAPTM5 to stroke outcomes via stress-kinase and lysosomal pathways, while LAPTM4A and LAPTM4B associate with glioma progression, immune evasion, and therapy resistance. Overall, LAPTM proteins represent promising biomarkers and therapeutic targets, warranting cell-type-resolved validation and central nervous system (CNS)-optimized delivery strategies, including gene therapy, small-molecule/degrader approaches, and multi-omics-guided patient stratification. - Source: PubMed
Publication date: 2026/02/10
Wu BowenNiu ZhenyanSui Yanfang - Acute myeloid leukemia (AML) remains a high-risk hematologic malignancy due to frequent relapse and therapeutic resistance. Although induction therapy can achieve cytological remission, a fraction of leukemic cells (minimal residual disease, MRD) persists within the protective bone marrow (BM) microenvironment. MRD is heterogeneous and may include subclones with intrinsic survival features present before therapy. Among these, rare BM-resident leukemic cells (BMresLC) may represent pre-adapted precursors of MRD, maintained in a low-proliferative (Ki67) or quiescent state. We previously showed that calcium signaling through ORAI1-dependent store-operated calcium entry (SOCE) contributes not only to AML stemness and drug resistance but also to the regulation of the G0-G1 cell-cycle transition and the emergence of slow-cycling leukemic cells. With this study, we have characterized the stemness and calcium signature of BMresLC before any therapeutic intervention. Our results, beyond further characterizing a population of cells rarely studied, could thus pave the way to new therapeutic opportunities combining current treatments with the targeting of relevant pathways highlighted by our work. - Source: PubMed
Publication date: 2026/01/09
Titah SofiaGuillemette AurélieLewuillon ClaraShaik Faruk AzamBerthon CélineGoursaud LaureTardivel MeryemBongiovanni AntoninoChauvet PaulJouy NathaliePeyrouze PaulineCheok MeylingBrinster CarineManier SalomonTarhan Mehmet ÇagatayLemonnier LoïcQuesnel BrunoTouil Yasmine - Tyrosine kinase inhibitors (TKIs) have transformed the treatment of EGFR-mutant non-small cell lung cancer (NSCLC); however, acquired resistance remains a major clinical challenge. While lysosomes have been implicated in drug resistance, their precise role in EGFR-TKI resistance remains unclear. In this study, we found that EGFR-TKI, including gefitinib and osimertinib, impaired WWP2-mediated proteasomal degradation of LAPTM4B. Through analysis of clinical tumor samples, genetic manipulation, and functional assays, we identify the lysosomal protein LAPTM4B as a key driver of EGFR-TKI resistance by enhancing EGFR phosphorylation and downstream signaling. Mechanistically, LAPTM4B interacts with ATP1A1 and facilitates its endocytosis, while simultaneously preventing its degradation by suppressing TRIM8-mediated K63-linked ubiquitination and proteasomal turnover. This stabilization of ATP1A1 enhances lysosomal acidification, ultimately promoting EGFR-TKI resistance. To identify potential therapeutic strategies, we conducted an unbiased high-content drug screen and identified compounds that suppress LAPTM4B expression. These compounds synergistically enhance the efficacy of EGFR-TKIs in NSCLC models and , with minimal toxicity. Integrative analyses of patient tissue samples, cellular models, an animal model, and cancer databases highlight the critical role of the LAPTM4B-ATP1A1-lysosomal acidification axis in EGFR-TKI resistance, providing a promising therapeutic avenue for overcoming resistance in EGFR-mutant NSCLC. - Source: PubMed
Publication date: 2026/01/01
Liu DanLiu MinxiaLv DongjinLi YuxiangGuo HongjuanLu BingxiaoLeng HaoYan RuyuYu HongtaoBlom TomasZhou Kecheng - - Source: PubMed
Li YangZou LihuaLi QiyuanHaibe-Kains BenjaminTian RuiyangLi YanDesmedt ChristineSotiriou ChristosSzallasi ZoltanIglehart J DirkRichardson Andrea LWang Zhigang Charles