ND PROTEIN PRECIPITATION Kit
- Known as:
- ND PROTEIN PRECIPITATION Kit
- Catalog number:
- ec-888-kit(50ml)
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- AGTC National Diagnostics
- Gene target:
- PROTEIN PRECIPITATION Kit
Related genes to: ND PROTEIN PRECIPITATION Kit
- Gene:
- TYRP1 NIH gene
- Name:
- tyrosinase related protein 1
- Previous symbol:
- TYRP, CAS2
- Synonyms:
- GP75, CATB, TRP, b-PROTEIN, OCA3
- Chromosome:
- 9p23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-09-04
- Date modifiied:
- 2016-04-19
Related products to: ND PROTEIN PRECIPITATION Kit
Related articles to: ND PROTEIN PRECIPITATION Kit
- Tyrosinase-related protein 1 (Tyrp1) is a melanosomal glycoprotein required for eumelanin biosynthesis through the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA). Pathogenic variants in Tyrp1 cause oculocutaneous albinism type 3 (OCA3), but the molecular basis by which individual substitutions impair Tyrp1 stability and activity remains incompletely understood. Here, we examined wild-type Tyrp1 and three missense variants associated with OCA3: R356Q and R326H as OCA3-related variants, and D308N as a benign control; these were under conditions relevant to melanosome maturation. To assess stability, we developed a urea-induced unfolding assay in which His-tagged Tyrp1 variants were immobilized to Ni-NTA magnetic beads before chemical denaturation. R356Q was the most destabilized variant, with a ΔΔG of 0.695 kcal/mol at pH 5.0 (acidic conditions) and 1.998 kcal/mol at pH 7.4 (near-neutral conditions) relative to wild-type. R326H showed intermediate destabilization, whereas D308N behaved similarly to wild-type. DHICA oxidation assays in the presence of MBTH showed about 20% reduced catalytic activity for R356Q, particularly under acidic conditions. Molecular dynamics simulations and ligand docking were consistent with these findings and indicated that R356Q increases conformational flexibility and perturbs structural integrity. In contrast, glycosylation reduced conformational fluctuations and enhanced stability across Tyrp1 and mutant variants examined. Together, these results show that pH, glycosylation, and disease-associated substitutions collectively modulate Tyrp1 folding energetics and catalytic competence and identify R356Q as a strongly destabilizing OCA3 variant. By defining how disease-associated Tyrp1 substitutions affect protein stability and function, this study may provide a framework for interpreting genotype-phenotype relationships and improving molecular diagnosis of OCA3. - Source: PubMed
Publication date: 2026/05/30
Sabir WaleedOsuna IsabellaDolinska Monika BSergeev Yuri V - The bioprospecting of Onosma species for multifunctional phenolics is gaining momentum, yet the impact of extraction methods on bioactivity is underexplored. This study compared methanolic extracts of O. rechingeri obtained via ultrasound-assisted extraction (UAE-ME), maceration (MAC-ME), and Soxhlet (SOE-ME). Total phenolic and flavonoid content was highest in SOE-ME. Luteolin-7-glucoside and hesperidin were abundant in MAC-ME, while SOE-ME was richest in rosmarinic acid. SOE-ME showed superior electron-transfer antioxidant activity, while metal chelation favored UAE-ME and MAC-ME. Enzyme inhibition varied by extraction: MAC-ME was most effective against AChE and α-amylase, SOE-ME against tyrosinase. Correlation analysis revealed distinct compound-activity associations: tyrosinase aligned with electron transfer, AChE and α-amylase with chelation. Docking suggested luteolin-7-glucoside as a strong α-amylase binder (-9.09 kcal/mol) and rosmarinic acid as a promising in silico binder of AChE and TYRP1. Overall, extraction strategy significantly alters chemical profiles and bioactivity, but these findings should be interpreted as preliminary because they are based on crude extracts, in vitro assays, correlation analysis with a limited sample set, and docking predictions; therefore, they highlight the need for targeted fractionation and further biological validation. - Source: PubMed
Publication date: 2026/06/06
Alshammari MamdouhSarikurkcu CengizBardakci FevziAlreshidi MousaAdnan MohdSiddiqui Arif JamalTepe Bektas - Melanin synthesis is regulated by a complex genetic network, and its dysregulation can promote malignant transformation. Pheomelanin, a lighter and more photoreactive form of melanin, contributes to oxidative stress and may facilitate melanoma development. Its abundance varies with skin phototype, but its role in melanoma cell biology remains poorly characterized, highlighting the need to study pheomelanogenic gene expression in cells with distinct pigmentary. - Source: PubMed
Publication date: 2026/02/11
Tam IrenaKurkiewicz SławomirMarek ŁukaszStojko Jerzy - Skin coloration is a distinctive phenotype and an economically important trait in ornamental fish. Understanding its regulatory mechanisms is crucial for both aquaculture and selective breeding. In this study, we cloned and analysed the full-length complementary DNA (cDNA) sequences of four key pigmentation-related genes-mitf, mc1r, tyr and sox10-in the black-tailed angelfish (Centropyge vrolikii). We established the fin-derived tissue cell line of C. vrolikii (CVFTCL) and confirmed its transfection efficiency using EGFP, achieving 40%-50% expression 24 h post-transfection, providing an in vitro platform for subsequent gene function verification. Using the primary fin cell culture system, we conducted overexpression and RNA interference (RNAi) experiments to investigate the regulatory relationships among these genes. Overexpression of mitf upregulated mc1r but downregulated sox10 and tyr; overexpression of mc1r enhanced mitf expression while inhibiting sox10 and tyr; overexpression of tyr only increased tyrp1 expression and overexpression of sox10 upregulated both mc1r and mitf, without affecting tyr. RNAi-mediated knockdown confirmed the efficiency of gene silencing and supported the regulatory relationships inferred from overexpression experiments. Collectively, these findings indicate that mitf, mc1r, tyr and sox10 may interact to coregulate melanocyte development and melanin synthesis, thereby influencing skin coloration in C. vrolikii. This study provides a mechanistic framework for pigmentation regulation and a foundation for colour improvement and selective breeding in this species. - Source: PubMed
Publication date: 2026/05/28
Luo DingyuanXi NingShi ShengkaiLu YizhenChen ZebinLiu HongweiChen JincanHuang HaiZhong ZhaoweiJiang Yonghua - Coat colour is among the most distinctive phenotypic traits for pig breed identification. Zhaotong pigs (ZTs), indigenous pigs in China, present two coat colour types: black and brown. However, the key genes and regulatory mechanisms responsible for coat colour variation remain unknown. In this study, we analysed the whole-genome resequencing data of 1110 individuals, including 43 pig breeds, Eurasian wild boars, and an outgroup. Population genetic structure analysis, including principal component analysis (PCA), phylogenetic tree construction, and admixture analysis, revealed that ZTs present unique genetic characteristics. Using selective sweep analysis of the black population vs brown population of ZTs and a genome-wide association study (GWAS) targeting coat colour, we identified tyrosinase-related protein 1 (TYRP1) and nuclear factor I B (NFIB) as two important functional genes that influence coat colour in ZTs. A mutation at the g.209726926_209726931del locus in exon 8 of the TYRP1 gene results in decreased eumelanin synthesis, leading to the brown coat colour of ZTs. Our study is the first to systematically elucidate the molecular genetic mechanisms underlying coat colour formation in ZTs, providing essential theoretical foundations for the conservation of indigenous pig genetic resources and the development of new specialized breeds. - Source: PubMed
Publication date: 2026/05/25
Zhou ChunluLi XinpengDong WenjunWang LixingChu JinyuChong YuqingMa YunlongDong XinxingYan Dawei