APOLIPOPROTEIN CIII, Human Ultra Pure
- Known as:
- APOLIPOPROTEIN CIII, Human Ultra Pure
- Catalog number:
- 125-21
- Product Quantity:
- 500 ug
- Category:
- -
- Supplier:
- LeeBio
- Gene target:
- APOLIPOPROTEIN CIII Human Ultra Pure
Ask about this productRelated genes to: APOLIPOPROTEIN CIII, Human Ultra Pure
- Gene:
- ADAM18 NIH gene
- Name:
- ADAM metallopeptidase domain 18
- Previous symbol:
- -
- Synonyms:
- tMDCIII, ADAM27
- Chromosome:
- 8p11.22
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-01
- Date modifiied:
- 2018-05-03
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Related articles to: APOLIPOPROTEIN CIII, Human Ultra Pure
- Hepatocellular carcinoma (HCC) is the most common primary liver cancer worldwide. Cancer cells' local infiltration, proliferation, and spread are mainly influenced by the protein hydrolyzing function of different matrix metalloproteinases (MMPs). However, no study has determined the relationship between MMPs and prognostic prediction in HCC. - Source: PubMed
Publication date: 2024/05/16
Yuan XingxingYang LiuxinGao JiaweiMao XuZhang YaliYuan Wei - The current study aims to determine the molecular mechanisms of diabetic retinopathy (DR) using the protein-protein interactome and metabolome map. We examined the protein network of novel biomarkers of DR for direct (physical) and indirect (functional) interactions using clinical target proteins in different models. - Source: PubMed
Publication date: 2020/06/18
Patrick Ambrose TeruHe WeilueMadu JoshuaSripathi Srinivas RChoi SeulggieLee KookSamson Faith PwaniyiboPowell Folami LBartoli ManuelaJee DonghyunGutsaeva Diana RJahng Wan Jin - Cancer-associated fibroblasts (CAFs) are important factors in the progression of hepatocellular carcinoma (HCC). But the characterization of these cells remains incomplete. This study aims to identify a panel of markers for CAFs that are associated with HCC progression. - Source: PubMed
Publication date: 2018/11/05
Zou BaojiaLiu XialeiGong YihangCai ChaonongLi PeipingXing ShanPokhrel BibeshZhang BaimengLi Jian - To determine the genomic signatures of human uterine leiomyomas and prevalence of MED12 mutations in human uterine leiomyosarcomas. - Source: PubMed
Publication date: 2016/11/23
Yatsenko Svetlana AMittal PriyaWood-Trageser Michelle AJones Mirka WSurti UrvashiEdwards Robert PSood Anil KRajkovic Aleksandar - Mass spectrometry based proteomics has facilitated sperm composition studies in several mammalian species but no studies have been undertaken in non-human primate species. Here we report the analysis of the 1247 proteins that comprise the Rhesus macaque (Macaca mulatta) sperm proteome (termed the MacSP). Comparative analysis with previously characterized mouse and human sperm proteomes reveals substantial levels of orthology (47% and 40% respectively) and widespread overlap of functional categories based on Gene Ontology analyses. Approximately 10% of macaque sperm genes (113/1247) are significantly under-expressed in the testis as compared with other tissues, which may reflect proteins specifically acquired during epididymal maturation. Phylogenetic and genomic analyses of three MacSP ADAMs (A-Disintegrin and Metalloprotease proteins), ADAM18-, 20- and 21-like, provides empirical support for sperm genes functioning in non-human primate taxa which have been subsequently lost in the lineages leading to humans. The MacSP contains proteasome proteins of the 20S core subunit, the 19S proteasome activator complex and an alternate proteasome activator PA200, raising the possibility that proteasome activity is present in mature sperm. Robust empirical characterization of the Rhesus sperm proteome should greatly expand the possibility for targeted molecular studies of spermatogenesis and fertilization in a commonly used model species for human infertility. - Source: PubMed
Publication date: 2013/07/01
Skerget SheriRosenow MatthewPolpitiya AshokaPetritis KonstantinosDorus SteveKarr Timothy L