Polyclonal Rabbit APLP2 (Ab-755) Antibody
- Known as:
- Polyclonal Rabbit APLP2 (Antibody-755) Antibody
- Catalog number:
- KA0243
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit APLP2 (Ab-755) Antibody
Related genes to: Polyclonal Rabbit APLP2 (Ab-755) Antibody
- Gene:
- APLP2 NIH gene
- Name:
- amyloid beta precursor like protein 2
- Previous symbol:
- APPL2
- Synonyms:
- APPH
- Chromosome:
- 11q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1993-06-23
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal Rabbit APLP2 (Ab-755) Antibody
Related articles to: Polyclonal Rabbit APLP2 (Ab-755) Antibody
- Keel length is a key body size indicator, which has an important impact on the overall growth performance, bone health, and production performance of poultry. In the process of selecting crossed strains for yellow feathered broiler chickens, it is generally necessary to select keel length, but there is little research on keel length development. Therefore, resequencing and GWAS was employed to obtain SNP molecular markers associated with keel length in a specialized Yellow-feathered broiler line. We identified 10 SNPs that were potentially significantly correlated with keel length for the first time located at 9 genes, including ATP7B, CST3, OTOP1, CRMP1, SLC12A1, COPS2, FAM227B, IFT140, APLP2. SNP2 and SNP3 loci were in a strongly linked state (D ' value=1), the other 8 SNP loci were not in a strongly linked state (D 'value<1). The association analysis between single SNP marker and keel length traits showed that TT and CT at SNP1 (rs315701680), GG at SNP2 (rs738740137), AA at SNP3 (rs317223723), AA at SNP4 (rs732443622), GG at SNP5(rs315667756), CC at SNP6 (rs314381113), GG at SNP7 (rs732811384), TT at SNP8 (rs314197610), CC and TC at SNP9 (rs13782000), TT and GT at SNP10 (rs737401141) genotypes were all the dominant genotypes for keel length. The strong linkage between SNP2 and SNP3 resulted in two haplotypes H1 (AG) and H2 (GA), respectively. The H1H1 haplotype (GGAA) produced by SNP2 and SNP3 linkage was the dominant genotype for keel length. The SNP molecular markers and dominant genotypes at SNP1-SNP10 loci identified in this study may be used to improve the accuracy and genetic progress of keel length selection. Meanwhile, candidate genes potentially significantly related to keel length will lay the foundation for genetic selection of keel length and cultivation of high-quality yellow feathered broilers in the future. - Source: PubMed
Publication date: 2026/03/27
Tu Y JLiu Y FZhang MJu X JShan Y JJi G GShu J T - Amyloid precursor protein (APP) is associated with both familial and sporadic forms of Alzheimer's disease. We previously reported that APP and its family members, amyloid precursor-like proteins 1 and 2 (APLP1 and APLP2), regulate intrinsic neuronal excitability and synaptic plasticity in excitatory principal neurons, though APP family is dispensable for neuronal survival. However, the physiological role of APP family in inhibitory interneurons remains poorly understood. Here, we use our previously characterized floxed APP, APLP1, APLP2 and GAD2-Cre alleles to generate inhibitory neuron-specific conditional triple knockout (IN-APP/APLP1/APLP2 cTKO) mice. Our electrophysiological analysis of acute hippocampal slices revealed that IN-APP/APLP1/APLP2 cTKO CA1 pyramidal neurons exhibit increased amplitudes of evoked GABA receptor-mediated inhibitory postsynaptic currents (IPSCs), while basal spontaneous IPSC frequency and amplitude remain unchanged. At Schaffer collateral (SC)-CA1 synapses, short-train frequency facilitation is enhanced in slices from IN-APP/APLP1/APLP2 cTKO mice, whereas paired-pulse facilitation (PPF) and long-term potentiation (LTP) are normal. Consistent with a cell-autonomous interneuron defect, basal excitatory transmission, measured by spontaneous and miniature excitatory postsynaptic currents (EPSCs) in CA1 pyramidal neurons, is unaltered. These data show that APP family in inhibitory interneurons regulates activity-dependent inhibitory output without overtly perturbing baseline glutamatergic transmission and thus, indirectly shapes short-term facilitation at SC-CA1 synapses. Together with our earlier findings in excitatory neuron-specific APP/APLP1/APLP2 cTKO mice showing intrinsic hyperexcitability, enhanced short-term facilitation, and impaired LTP, these results suggest that the APP family modulates inhibitory and excitatory functions at SC-CA1 synapses through complementary mechanisms in principal neurons and interneurons. - Source: PubMed
Publication date: 2026/03/29
Lee Sang HunKang JongkyunZhang ChenBolshakov Vadim YShen Jie - Triple-negative breast cancer (TNBC) exhibits pronounced intratumoral heterogeneity, and cancer stem cells (CSCs) are thought to play a pivotal role in this process. However, the molecular regulatory mechanisms linking CSC-associated stemness features to tumor progression remain insufficiently elucidated. - Source: PubMed
Publication date: 2026/03/23
Huo ZhenzhongSun WeiboLou ChunYang Tiansong - Organophosphate pesticides such as diazinon (DZN) are involved in developing psychological symptoms and memory deficits, but their effects on the amyloid precursor proteins (APP) gene expression remain unclear. - Source: PubMed
Sarailoo MehdiAfshari SalvaAsghariazar VahidNiri Mehdi VosoughiSafarzadeh ElhamDadkhah Masoomeh - Few regulators of K-Ras plasma membrane organization are known. We combined TurboID-based proximity proteomics with a BRET screen to identify eight potential K-Ras G-domain interactors. We focused on APLP2, which indirectly engages with C-Raf in immediate proximity to K-Ras, and SPRY2, which exhibits properties of an effector. Co-immunoprecipitation and BRET assays revealed that the SPRY2 C-terminal half binds oncogenic RasG12V more than full-length SPRY2. Both forms localize to the plasma membrane, but this localization and binding to K-Ras are disrupted by inhibitors of K-Ras membrane anchorage or activity. Mutations at the predicted interface of K-Ras and SPRY2's C-terminal region affect the interaction. Both full-length SPRY2 and its C-terminal fragment promote the differentiation of C2C12 muscle cells, a process requiring MAPK pathway inhibition. Finally, SPRY2 homo- and hetero-oligomerizes with SPRY4. We propose that active K-Ras recruits SPRY2 dimers to the membrane, where they block Ras effector access. - Source: PubMed
Publication date: 2025/11/07
Pavic KarolinaHood Fiona ElizabethDuval Carla JaneManoharan Ganesh BabuLaurini ChristinaSiddiqui Farid AhmadMo Stephanie Puy LamPrior Ian AndrewAbankwa Daniel Kwaku