ODZ3 _ Teneurin_3
- Known as:
- ODZ3 _ Teneurin_3
- Catalog number:
- Y214162
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ODZ3 _ Teneurin_3
Related genes to: ODZ3 _ Teneurin_3
- Gene:
- TENM1 NIH gene
- Name:
- teneurin transmembrane protein 1
- Previous symbol:
- ODZ3, TNM, ODZ1
- Synonyms:
- TEN-M1
- Chromosome:
- Xq25
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-21
- Date modifiied:
- 2015-09-08
- Gene:
- TENM3 NIH gene
- Name:
- teneurin transmembrane protein 3
- Previous symbol:
- ODZ3
- Synonyms:
- Ten-M3, KIAA1455
- Chromosome:
- 4q34.3-q35.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-24
- Date modifiied:
- 2018-02-13
Related products to: ODZ3 _ Teneurin_3
Antibodies: ODZ3 _ Teneurin-3 HOST: Goat Clonality: pAbBovine Teneurin-1(ODZ1) ELISA kitBovine Teneurin-2(ODZ2) ELISA kitCanine Teneurin-1(ODZ1) ELISA kitCanine Teneurin-1(ODZ1) ELISA kitCanine Teneurin-2(ODZ2) ELISA kitCanine Teneurin-2(ODZ2) ELISA kitChicken Teneurin-1(ODZ1) ELISA kitChicken Teneurin-1(ODZ1) ELISA kitChicken Teneurin-1(ODZ1) ELISA kit SpeciesChickenChicken Teneurin-2(ODZ2) ELISA kitChicken Teneurin-2(ODZ2) ELISA kitChicken Teneurin-2(ODZ2) ELISA kit SpeciesChickenChicken,Gallus gallus,Neurestin,ODZ2,Protein Odd Oz_ten-m homolog 2,Ten-2,Tenascin-M2,Teneurin-2,Ten-m2,TNM2Chicken,Gallus gallus,ODZ1,Protein Odd Oz_ten-m homolog 1,Ten-1,Tenascin-M1,Teneurin-1,Ten-m1,TNM1 Related articles to: ODZ3 _ Teneurin_3
- Synaptic adhesion molecules (SAMs) are evolutionarily conserved proteins that play an important role in the form and function of neuronal synapses. Teneurins (Tenms) and latrophilins (Lphns) are well-known cell adhesion molecules that form a transsynaptic complex. Recent studies suggest that Tenm3 and Lphn2 (gene symbol Adgrl2) are involved in hippocampal circuit assembly via their topographical expression. However, it is not known whether other teneurins and latrophilins display similar topographically restricted expression patterns during embryonic and postnatal development. Here, we reveal the cartography of all teneurin (Tenm1-4) and latrophilin (Lphn1-3 [Adgrl1-3]) paralog expression in the mouse hippocampus across prenatal and postnatal development as monitored by large-scale single-molecule RNA in situ hybridization mapping. Our results identify a striking heterogeneity in teneurin and latrophilin expression along the spatiotemporal axis of the hippocampus. Tenm2 and Tenm4 expression levels peak at the neonatal stage when compared to Tenm1 and Tenm3, while Tenm1 expression is restricted to the postnatal pyramidal cell layer. Tenm4 expression in the dentate gyrus (DG) exhibits an opposing topographical expression pattern in the embryonic and neonatal hippocampus. Our findings were validated by analyses of multiple RNA-seq datasets at bulk, single-cell, and spatial levels. Thus, our study presents a comprehensive spatiotemporal map of Tenm and Lphn expression in the hippocampus, showcasing their diverse expression patterns across developmental stages in distinct spatial axes. - Source: PubMed
Publication date: 2024/05/07
Liakath-Ali KifRefaee RebeccaSüdhof Thomas C - Ten-m/Odz/teneurins are a new family of four distinct type II transmembrane molecules. Their extracellular domains are composed of an array of eight consecutive EGF modules followed by a large globular domain. Two of the eight modules contain only 5 instead of the typical 6 cysteine residues and have the capability to dimerize in a covalent, disulfide-linked fashion. The structural properties of the extracellular domains of all four mouse Ten-m proteins have been analyzed using secreted, recombinant molecules produced by mammalian HEK-293 cells. Electron microscopic analysis supported by analytical ultracentrifugation data revealed that the recombinant extracellular domains of all Ten-m proteins formed homodimers. SDS-PAGE analysis under nonreducing conditions as well as negative staining after partial denaturation of the molecules indicated that the globular COOH-terminal domains of Ten-m1 and -m4 contained subdomains with a pronounced stability against denaturing agents, especially when compared with the homologous domains of Ten-m2 and -m3. Cotransfection experiments of mammalian cells with two different extracellular domains revealed that Ten-m molecules have also the ability to form heterodimers, a property that, combined with alternative splicing events, allows the formation of a multitude of molecules with different characteristics from a limited set of genes. - Source: PubMed
Publication date: 2002/05/08
Feng KangZhou Xiao-HongOohashi ToshitakaMörgelin MatthiasLustig ArielHirakawa SatoshiNinomiya YoshifumiEngel JürgenRauch UweFässler Reinhard