AMY1B Antibody (OASA09126)
- Known as:
- AMY1B Antibody (OASA09126)
- Catalog number:
- oasa09126
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- AMY1B Antibody (OASA09126)
Related genes to: AMY1B Antibody (OASA09126)
- Gene:
- AMY1B NIH gene
- Name:
- amylase alpha 1B (salivary)
- Previous symbol:
- AMY1
- Synonyms:
- -
- Chromosome:
- 1p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2019-01-18
Related products to: AMY1B Antibody (OASA09126)
Related articles to: AMY1B Antibody (OASA09126)
- Proteomic profiling offers thorough insights into protein structure and function, as well as it acts as an essential approach for analyzing molecular changes at the tissue level. However, because of the proteome's diversity and dynamic nature, biomarker discovery remains challenging. By combining proteomics with bioinformatics, the level of understanding in relation to molecular interactions and disease processes can be improved. Through an integrative approach, few limitations can be addressed, thereby promoting proteomic profiling for the discovery of new therapeutic targets and novel biomarkers for a variety of disorders. - Source: PubMed
Publication date: 2026/06/18
Rao Bounika EsvanthNair Anju MRamesh PreethiRamshankar VijayalakshmiGopinath SAbhinand P ANdkoraj ArtnoraMazur MartaWarnakulasuriya SamanCatakapatri Venugopal Divyambika - The RAGs, comprising RAG1 and RAG2, catalyze V(D)J recombination by recognizing recombination-signal sequences (RSS). Glioblastoma, the aggressive brain cancer, has many oncogenic chromosomal alterations; however, the mechanism of their generation is largely unknown. Here, we report that RAGs are expressed in human glioblastoma cells at transcript and protein levels. RNA-seq data analysis confirmed the expression of RAGs in the majority of patients with glioma. Analysis of patient breakpoint sequences reveals cryptic RSS in regions undergoing rearrangements. Biochemical studies demonstrate that RAGs can bind and cleave cryptic RSS in fragile regions (AMY1B, CAMK2D, RN7SKP123-MTF2, DIPK1A, IRX5-IRX6), albeit at lower efficiency. Recombination assay using episomes harboring the fragile regions showed aberrant recombination in these regions, and the efficiency was significantly reduced in RAG1 ablated cells. Finally, we recapitulate the glioblastoma associated AMY1B and RN7SKP123-MTF2 chromosomal rearrangement using an extrachromosomal assay. Thus, the present study provides mechanistic insights into the generation of chromosomal aberrations associated with glioblastoma. - Source: PubMed
Publication date: 2025/10/21
Paranjape AmitaKumari SusmitaSahu Lipsa RaniMondal AmritaKunhiraman SwapnaSharma M ArunNilavar Namrata MChoudhary BibhaRaghavan Sathees C - Xerostomia is a salivary gland dysfunction that negatively impacts the life quality of patients; however, there is no effective treatment for xerostomia. Bioengineered organs, generated using stem cells obtained from newborn salivary glands and ligated injury models, are a new organ transplantation strategy that could be feasible for xerostomia treatment. Reconstruction of salivary gland organoids by seed cells obtained from human minor salivary glands will offer theoretical fundaments and technology support for clinical application and organ regeneration research. Herein, we aimed to propose a new method for culturing and enriching adult human minor salivary gland stem cells in vitro in a three-dimensional (3D) environment via Wnt signaling activation. - Source: PubMed
Publication date: 2023/08/25
Kang Bo KyoungZhu ZhuWang JianZhou JiaYu ShunZhou XianyuZhao ZhenminXie AiguoLu LinYang Jun - The rising incidence of obesity and type 2 diabetes is contributing to the escalating burden of disease globally. These metabolic disorders are closely linked with diet and in particular with carbohydrate consumption; hence, it is important to understand the underlying mechanisms that influence carbohydrate metabolism. Amylase, the enzyme responsible for the digestion of starch, is coded by the genes AMY1A, AMY1B, and AMY1C (salivary amylase) and AMY2A and AMY2B (pancreatic amylase). Previous studies demonstrate wide variations in AMY1A copy numbers, which can be attributed to several genetic, nutritional, and geographical diversities seen in populations globally. Current literature suggests that AMY1A copy number variations are important in obesity and other cardiometabolic disorders through their effects on glucose and lipid homeostasis, inflammatory markers, and the gut microbiome. This review synthesizes the available evidence to improve understanding of the role of AMY1A in obesity and related cardiometabolic risk factors and disorders including insulin resistance and type 2 diabetes, cardiovascular risk and inflammation, and the gut microbiome. - Source: PubMed
Publication date: 2021/01/11
Hariharan RohitMousa Ayade Courten Barbora - The human amylase gene (AMY1) has a broad copy number (CN) variation that may associate with body mass index. - Source: PubMed
Barber Thomas MBhatti Ahsan AElder Patrick J DBall Sarah PCalvez RonanRamsden David BCuthbertson Dan JPfeiffer Andreas FBurnett DavidWeickert Martin O