HPA_1
- Known as:
- HPA_1
- Catalog number:
- ANT-155
- Product Quantity:
- 240µg
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- HPA_1
Related products to: HPA_1
ABO Genotyping, Human Blood group detection , HLA, HPA & BLOOD GROUP DETECTION, conventional PCRAnserine Heparanase Elisa Kit (HPA)Anserine anti - Heparanase Elisa Kit (HPA)Antibody to Heparanase (HPA) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntibody to Heparanase (HPA) Organism: Homo sapiens (Human) Type: Polyclonal Source: RabbitAntibody to Heparanase (HPA) Organism: Mus musculus (Mouse) Type: Polyclonal Source: RabbitAntibody to Heparanase (HPA) Organism: Mus musculus (Mouse) Type: Polyclonal Source: RabbitAntibody to Heparanase (HPA) Organism: Rattus norvegicus (Rat) Type: Polyclonal Source: RabbitAntibody to Heparanase (HPA) Organism: Rattus norvegicus (Rat) Type: Polyclonal Source: RabbitAntibody: Helix pomatia agglutinin (HPA), Serum (0.1 ml) , Immunogen: Helix pomatia agglutinin (HPA) , Host: rabbit , polyclonal, Confirmed reactivity: Helix pomatiaAntibody: Helix pomatia agglutinin (HPA), Serum (1 ml), Immunogen: Helix pomatia agglutinin (HPA) , Host: rabbit , polyclonal, Confirmed reactivity: Helix pomatiaAntibody: Helix pomatia agglutinin (HPA), Total IgG (0.2 mg), Immunogen: Helix pomatia agglutinin (HPA) , Host: rabbit , polyclonal, Confirmed reactivity: Helix pomatiaAntibody: Helix pomatia agglutinin (HPA), Total IgG (1mg), Immunogen: Helix pomatia agglutinin (HPA) , Host: rabbit , polyclonal, Confirmed reactivity: Helix pomatiaAnti_bovine NGF IgG fraction (monoclonal)Anti_human basic FGF IgG fraction (monoclonal) Related articles to: HPA_1
- Arginine iminohydrolases are a family of enzymes involved in the conversion of arginine to citrulline. There are five isoforms in humans (PADI1, 2, 3, 4, and 6). Some of them are observed experimentally in the cytoplasm and in the nucleus of the cell; for moving to the latter location, they must pass through the cell nuclear membrane by using the translocation machinery, mainly formed by the proteins named importins. We have previously described and characterized the isolated PADI4 nuclear localization sequences (NLSs) and their binding to importin α3 (Impα3). By using theoretical predictors, here we foretold the existence of several NLSs in isoforms PADI1, PADI2, and PADI3. These predicted polypeptide regions were chemically synthesized, and the soluble ones were conformationally characterized in isolation. We studied their ability to bind Impα3 and its truncated species (ΔImpα3) without the importin binding domain, by using several biophysical techniques and molecular simulations. The isolated peptides were disordered and monomeric in solution. Moreover, all of them were capable of binding to both importin species with affinities in the low micromolar range, and targeting the canonical NLS binding site for cargo proteins. These findings suggest that the predicted NLS regions could be the sites for the binding of the corresponding intact PADI protein to importin, and therefore, any of the PADI enzymes could be translocated into the nucleus. - Source: PubMed
Neira José LAbian OlgaVelazquez-Campoy AdriánRizzuti Bruno - Fibro-adipogenic progenitor cells (FAPs) support muscle tissue homeostasis, regulate muscle growth, injury repair, and fibrosis, and activate muscle progenitor cell differentiation to promote regeneration. We aimed to investigate the effects of co-culturing FAPs with muscle satellite cells (MuSCs) on myogenic differentiation. Proteomic profiling of co-culture supernatants identified significant DCX, IMP2A, NUDT16L1, SLC38A2, and IL-6 upregulation. Comparative transcriptomics of mono-cultured versus co-cultured MuSCs revealed differential expression of oxidative stress-related genes (, , , , , and ). Pathway enrichment analyses highlighted cell cycle regulation, TNF signaling, and ferroptosis. Gene ontology analysis of MuSCs indicated significant gene enrichment in myosin-related components. Combined transcriptomic and proteomic analyses demonstrated HO-1 downregulation at the transcriptional and translational levels, with altered pathways being predominantly related to myosin filament, muscle system process, and muscle contraction cellular components. HO-1 knockdown reduced intracellular iron accumulation in MuSCs, suppressing iron-dependent autophagy. This alleviated oxidative stress and promoted myogenic differentiation. Exogenous IL-6 (0.1 ng/mL) downregulated HO-1 expression, initiating an identical regulatory cascade, while HO-1 overexpression reversed the IL-6-mediated reduction in the expression of the autophagy markers LC3 and ATG5, suppressing myogenic enhancement. This establishes the co-culture-induced IL-6/HO-1 axis as a core regulator of iron-dependent oxidative stress and autophagy during myogenic differentiation. - Source: PubMed
Publication date: 2025/08/10
Zhang MengyuanLiu SiyuWang YonghengShan ShanCang Ming - In the United States, African Americans (AA) have higher Pancreatic ductal adenocarcinoma (PDAC) incidence and mortality rates than Caucasian Americans (CA). This study aimed to identify distinct gene expression signatures and differentially regulated pathways in AA and CA PDACs. - Source: PubMed
Publication date: 2025/07/04
Bajpai PrachiPaluri RaviDiffalha Sameer AlChandrashekar Darshan SAfaq FarrukhOtali DennisElkholy AmrMiller C RyanPeter ShajanManne AshishNagaraju Ganji PurnachandraSaddala Madhu SudhanaKhushman Moh'dVarambally SooryanarayanaManne Upender - Preeclampsia (PE) is a multisystemic syndrome of pregnancy that seriously affects maternal and infant healthcare. Here, we identified PADI1 as an abnormally highly expressed gene in PE and investigated its effect on trophoblast cells. According to the analysis results from GEO datasets GSE186257 and GSE143953, PADI1 is highly expressed in the placental samples of PE patients. PADI1 knockdown promoted the growth and migration of trophoblast cells. HTR-8 and Swan-71 cells were treated with 200 nmol/L TG to simulate ERS in vitro. PADI1 knockdown inhibited TG-induced ERS and apoptosis. Mechanistically, PADI1 knockdown downregulated ERS-related factors including IRE1α, XBP1, CHOP, ATF6 and GRP78. The FAK/ERK1/2 signaling pathway has been identified as a downstream target of PADI1 in trophoblast cells. Inhibition of FAK/ERK1/2 effectively hindered the enhancement of cell activity by PADI1 knockdown in TG-treated trophoblast cells. In conclusion, PADI1 was highly expressed in the placental tissues of PE patients. PADI1 knockdown inhibited the ERS-induced apoptosis in trophoblast cells through FAK/ERK1/2 signaling pathway, suggesting the potential role of PADI1 in PE prevention and treatment. - Source: PubMed
Publication date: 2025/05/13
Ning JianhuaYang SongbinGao FengchunWang LongbinLin ZeyuCheng DiFan Kefeng - Protein citrullination is accomplished by a broad enzyme family named Peptidyl Arginine Deiminases (PADs), which makes this post-translational modification in many proteins that perform physiological and pathologic mechanisms in the body. Due to these modifications, citrullination has become a significant topic in the study of pathological processes. It has been related to some chronic and autoimmune diseases, including rheumatoid arthritis (RA), interstitial lung diseases (ILD), multiple sclerosis (MS), and certain types of cancer, among others. Antibody production against different targets, including filaggrin, vimentin, and collagen, results in an immune response if they are citrullinated, which triggers a continuous inflammatory process characteristic of autoimmune and certain chronic diseases. PAD coding genes ( to and ) harbor variations that can be important in these enzymes' folding, activity, function, and half-life. However, few studies have considered these genetic factors in the context of chronic diseases. Exploring PAD pathways and their role in autoimmune and chronic diseases is a major topic in developing new pharmacological targets and valuable biomarkers to improve diagnosis and prevention. The present review addresses and highlights genetic, molecular, biochemical, and physiopathological factors where PAD enzymes perform a major role in autoimmune and chronic diseases. - Source: PubMed
Publication date: 2023/12/13
Nava-Quiroz Karol JLópez-Flores Luis APérez-Rubio GloriaRojas-Serrano JorgeFalfán-Valencia Ramcés