Proteins FABP6, Human
- Known as:
- Proteins FABP6, Human
- Catalog number:
- C221
- Product Quantity:
- 10μg
- Category:
- -
- Supplier:
- Novoprotein
- Gene target:
- Proteins FABP6 Human
Related genes to: Proteins FABP6, Human
- Gene:
- FABP6 NIH gene
- Name:
- fatty acid binding protein 6
- Previous symbol:
- -
- Synonyms:
- I-15P, ILLBP, I-BAP, ILBP3, I-BABP, ILBP, I-BALB
- Chromosome:
- 5q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-09-12
- Date modifiied:
- 2016-10-05
Related products to: Proteins FABP6, Human
Related articles to: Proteins FABP6, Human
- Bladder cancer (BC) is a highly prevalent malignant tumor. The traditional Chinese medicine formula Guo Lou Qu Mai Wan (GLQMW), when used in conjunction with chemotherapy, has been shown to reduce adverse reactions and prolong survival time, although its specific mechanisms remain unclear. This study aims to investigate whether GLQMW exerts its therapeutic effects on bladder cancer by modulating the tumor immune microenvironment. - Source: PubMed
Publication date: 2026/04/15
Teng QiliangCheng ShuminChen JiaZhu HongyaHu KaiSun LinglingZhao JinYuan ZhenboWang WenjingZhang LiLiu TaoliFeng Jiahao - To investigate the expression of the fatty acid binding protein 6 () long transcript in clear cell renal cell carcinoma (ccRCC), its correlation with tumor biological behavior, and further analyze its potential as a biomarker and therapeutic target. - Source: PubMed
Yin HaomingWang ZijieShu FanZhang ZhanyiLiang HuiZhang Shudong - Fatty acid binding proteins (FABPs) are key regulators of lipid metabolism and are expressed in the stroma of breast cancer. However, their roles in different breast cancer subtypes remain unclear. This study explored the expression patterns of FABPs across breast cancer subtypes and examined their associations with immune cell infiltration and clinical features using large datasets, with validation performed through testing in breast cancer cell lines and human tissue samples. - Source: PubMed
Publication date: 2026/02/25
Ali Eman Taha OsmanMin Eun-JiCho WonkyoungPark Young Mi - Residual feed intake (RFI) is a key indicator of feed efficiency in poultry. Although regulatory links such as the hypothalamus-gut and gut-liver axes have been implicated, most studies remain restricted to single axes or fragmented analyses, and systematic multi-organ integration is lacking. Here, we measured feed efficiency in 1,000 Nonghua ducks and selected 12 individuals with divergent RFI for transcriptomic profiling of the hypothalamus, pituitary, liver, duodenum, jejunum, ileum, and cecum, combined with serum metabolomics. We identified 769 differentially expressed genes (DEGs), with the hypothalamus, liver, and cecum as major contributors, and 28 differential serum metabolites enriched in lipid and amino acid metabolism. Beyond tissue-specific functions, enrichment analysis highlighted several pathways that were repeatedly shared across central and peripheral tissues, including neuroactive ligand-receptor interaction, hormone signaling, steroid hormone biosynthesis, and insulin signaling, suggesting a coordinated regulation of feed efficiency between the brain, gut, and liver. To clarify their relevance, we integrated gene modules with metabolites and identified two candidate cross-organ association frameworks: the MEblack-6-Oxopiperidine-2-carboxylic acid (gut-liver) networks, enriched for liver genes CNTNAP1, SHC3, and RAB36, and cecal genes DCC and CCDC60. The MEblue-LysoPE(18:2(9Z,12Z)/0:0) (gut-brain) networks, enriched for cecal genes FABP6, KCNJ11, and the pituitary gene TRPA1, in which these genes and metabolites may contribute to RFI regulation. Together, these findings provide new insights into cross-organ molecular networks underlying feed efficiency in ducks and establish a valuable resource for future functional studies and breeding strategies. - Source: PubMed
Publication date: 2026/01/27
Guo ShihaoXi YangQi JingjingYang ZhaoHan XuLing WeikangBai LiliHuang AnqiHu ShenqiangHu JiweiHan ChunchunWang JiwenLi LiangLiu Hehe - Salmonella Pullorum (S. Pullorum) incurs high mortality in chicks and disrupts intestinal health, and poses a severe threat to poultry industry and human health. However, in Chinese Taihe Black-Bone Silky Fowls (TBSF), the jejunum biomarker and molecular mechanism responding to S. Pullorum inoculation remain elusive. This study aims to characterize the jejunum proteome changes of TBSF affected by S. Pullorum. Using a data-independent acquisition (DIA) proteomics method, jejunum samples were collected from chicks and analyzed. These samples corresponded to the following treatment groups: the blank control group (TBSF with PBS treatment), and groups challenged with Salmonella Pullorum at doses of 1.39 × 10⁸ CFU/mL (L), 2.78 × 10⁸ CFU/mL (M), and 5.56 × 10⁸ CFU/mL (H). Meanwhile, the LD group (challenged with 1.39 × 10 CFU/mL S. Pullorum and administered 0.1g/kg bw 20% florfenicol powder) was used as experimental validation. A total of 8977 proteins were identified. Compared with the blank group, the numbers of differentially abundant proteins were 976 in the L group, 536 in the LD group, 635 in the M group, 673 in the H group, respectively. KEGG analysis showed that proteins affected by S. Pullorum were mainly associated with the signal transduction and infectious disease. EggNOG annotation of proteins showed that regulated proteins were significantly involved in intracellular trafficking, secretion, and vesicular transport, as well as post-translational modification, protein turnover, and chaperones. The results indicate that the alterations in jejunal protein profiles following S. Pullorum challenge are primarily driven by the host's active defense mechanisms against infection. Notably, the protein abundance of FABP6 and ACE2 was significantly higher in the Blank control group compared to all infected groups. This differential expression was further corroborated by RT-PCR analysis, which showed a corresponding increase in FABP6 mRNA levels in the Blank group, confirming FABP6 as a host gene responsive to S. Pullorum. Collectively, this study proposes potential protein biomarkers for the diagnosis of S. Pullorum infection, identifies promising targets for therapeutic development, and provides enhanced mechanistic insight into host-pathogen interactions. that changes of jejunum proteins in response to S. Pullorum are driven by the host's intensified efforts to counteract the infection. The protein abundance of FABP6 and ACE2 was significantly higher in the blank group than in the S. Pullorum-challenged groups. This observation was further validated at the transcriptional level, as RT-PCR analysis confirmed that FABP6 mRNA expression was also elevated in the blank group. These consistent results establish FABP6 as a host gene responsive to S. Pullorum infection. Consequently, this study not only identifies potential protein biomarkers for diagnosing S. Pullorum infection but also proposes novel targets for therapeutic development, thereby enhancing our understanding of the underlying host-pathogen interactions. - Source: PubMed
Publication date: 2026/02/02
Ye MengjunZhang LiYuan LijuanXiang JianjunLiao QiegenLong WeiDong YifanYu XirenAi QiushuangQiu SuyanZhang Dawen