SAP97 (RPI 197.4) Mouse mAb
- Known as:
- SAP97 (RPI 197.4) Mouse mAb
- Catalog number:
- ASAVAM-PS005F
- Product Quantity:
- 200 µg
- Category:
- -
- Supplier:
- Other suppliers
- Gene target:
- SAP97 (RPI 197.4) Mouse mAb
Related genes to: SAP97 (RPI 197.4) Mouse mAb
- Gene:
- AGT NIH gene
- Name:
- angiotensinogen
- Previous symbol:
- SERPINA8
- Synonyms:
- -
- Chromosome:
- 1q42.2
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2016-01-12
- Gene:
- DLG1 NIH gene
- Name:
- discs large MAGUK scaffold protein 1
- Previous symbol:
- -
- Synonyms:
- SAP97, SAP-97, hdlg, DLGH1, dJ1061C18.1.1
- Chromosome:
- 3q29
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-04
- Date modifiied:
- 2016-05-24
- Gene:
- PGLYRP3 NIH gene
- Name:
- peptidoglycan recognition protein 3
- Previous symbol:
- -
- Synonyms:
- PGRPIA, PGLYRPIalpha, PGRP-Ialpha
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-17
- Date modifiied:
- 2016-10-05
- Gene:
- PGLYRP4 NIH gene
- Name:
- peptidoglycan recognition protein 4
- Previous symbol:
- -
- Synonyms:
- SBBI67, PGRPIB, PGLYRPIbeta, PGRP-Ibeta
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-17
- Date modifiied:
- 2016-10-05
- Gene:
- PTBP1 NIH gene
- Name:
- polypyrimidine tract binding protein 1
- Previous symbol:
- PTB
- Synonyms:
- HNRPI, HNRNP-I, PTB2, PTB3, PTB-1, PTB4, pPTB
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1992-06-29
- Date modifiied:
- 2015-03-26
Related products to: SAP97 (RPI 197.4) Mouse mAb
Related articles to: SAP97 (RPI 197.4) Mouse mAb
- Primary cilia are critical sensory organelles whose structure and composition are tightly regulated. The Scribble polarity complex protein DLG1 has recently been implicated in controlling both ciliary protein composition and length in mouse kidney epithelial cells. In addition, the palmitoyl transferase ZDHHC5 localizes to primary cilia and negatively regulates their length. However, the molecular mechanisms underlying DLG1-mediated ciliary regulation and its interaction network remain poorly defined. - Source: PubMed
Publication date: 2026/06/10
Rezi Csenge KataDoganli CananAslanyan Mariam GChamlali MohamedMary BenjaminCallesen Nina LykkeAbu-Khesha Rokeah Rafat KamelDiwan Gaurav DRussell Robert BLorentzen EsbenBoldt KarstenRoepman RonaldLarsen Lars AllanPedersen Lotte B - The widespread use of next-generation sequencing has allowed refinement of the classification and diagnosis of salivary gland neoplasms, leading to identification of recurrent gene fusions in a majority of salivary gland carcinoma types, and characterization of several novel entities. A small proportion of salivary gland carcinomas do not meet the diagnostic criteria for any known tumor type and are therefore classified as "salivary gland carcinoma, not otherwise specified". Given the ever-growing arsenal of tools to classify these lesions, the number of cases diagnosed as such is expected to continue decreasing. - Source: PubMed
Publication date: 2026/06/09
Mantilla Jose GSnuderl MatijaLiu Cheng ZZhou Fang - Cell adhesion molecules of the immunoglobulin superfamily (IgCAMs) coordinate adhesive interactions with intracellular organization during tissue morphogenesis. In the follicular epithelium, epithelial maintenance depends on reintegration, a process in which mitotically displaced cells reincorporate into the epithelial monolayer. Previous work identified the IgCAMs Fasciclin 2 (Fas2) and Neuroglian (Nrg) as parallel, partially redundant regulators of reintegration, but the intracellular mechanisms linking adhesion to reintegration remained unclear. Here, we show that Fas2 supports reintegration through two mechanistically distinct modes: a transmembrane mode and a GPI-linked mode. Although both contribute to reintegration, the transmembrane mechanism is more effective and depends on stabilization of a cortical Fas2 pool through intracellular coupling. Using yeast two-hybrid screening, genetics, and fluorescence recovery after photobleaching (FRAP), we identify the scaffold protein Discs large (Dlg1) as a functional intracellular partner of transmembrane Fas2. Partial disruption of Dlg1 preferentially sensitizes epithelia in which the parallel Nrg-dependent reintegration mechanism is compromised, consistent with Dlg1 functioning primarily within the Fas2-dependent reintegration arm. While Dlg1 is not required for Fas2 membrane localization, Dlg1 disruption increases the mobile fraction of transmembrane Fas2, indicating that Dlg1 promotes retention of a stabilized cortical Fas2 pool. Together, these findings support a model in which epithelial reintegration depends on coordinated adhesion-scaffold coupling and reveal mechanistic parallels between epithelial reintegration and IgCAM-dependent processes in the developing nervous system. - Source: PubMed
Publication date: 2026/05/27
Finegan Tara MLinhoff Michael WRice HannahGhasemzadeh SahelWright ZachNeville Kathryn EWilson Tyler JOst Evan WLowe NicholasDunivan AdrianMendoza Oscar AndradeCammarota Christian MBergstralh Dan T - The synergistic cardioprotective effects of monoester alkaloids and ginsenosides constitute the pharmacological basis of Shenfu decoction (SFD) for chronic heart failure. However, the underlying molecular interactions remain unclear. - Source: PubMed
Publication date: 2026/04/23
Li HaoChen QingshanZhang QiqiangWang LiangDi XuemeiNie YonghongZhang Hai - 3q29 deletion (3q29Del) syndrome is caused by a 1.6 Mb copy number variant (CNV) located near the telomeric end of the long arm of the third human chromosome. Hemizygosity of this set of 22 protein-coding genes significantly increases risk for schizophrenia and autism spectrum disorders among other neurodevelopmental conditions, but it is not known which genes in this CNV interval are responsible for these phenotypes. We have evaluated existing literature and public genomic resources for this set of genes, categorizing them based on known cellular functions and assessed their potential as phenotypic drivers. We provide a comprehensive, synthetic review of the essential known functions of 3q29 deleted genes, and how multiple 3q29-encoded proteins may functionally interact. Our analysis reveals that ubiquitination/SUMOylation stands out among processes potentially compromised due to compound haploinsufficiency of four 3q29Del genes (UBXN7, FBXO45, RNF168, SENP5). The available genomic evidence indicates that no single gene in the 3q29 locus is solely responsible for the neurodevelopmental phenotypes of 3q29Del syndrome. Overall, we propose that functional, expression, and gene constraint evidence supports six genes (TFRC, UBXN7, FBXO45, PAK2, NCBP2, DLG1) as the most likely phenotypic drivers in 3q29Del syndrome. Haploinsufficiency of these proteins would likely disrupt metabolic, synaptic, and signaling mechanisms in developing and mature neurons, which collectively may impair neural circuit differentiation and function. - Source: PubMed
Publication date: 2026/04/21
Herriges Allyson RPurcell Ryan H