Antibodies: POLDIP2 HOST: Goat Clonality: pAb
- Known as:
- Antibodies: POLDIP2 HOST: Goat Clonality: pAb
- Catalog number:
- CA21702-100
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biomatic
- Gene target:
- Antibodies: POLDIP2 HOST: Goat Clonality: pAb
Related genes to: Antibodies: POLDIP2 HOST: Goat Clonality: pAb
- Gene:
- CERNA2 NIH gene
- Name:
- competing endogenous lncRNA 2 for microRNA let-7b
- Previous symbol:
- -
- Synonyms:
- HOST2
- Chromosome:
- 10q23.1
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2017-04-27
- Date modifiied:
- 2017-07-14
- Gene:
- POLDIP2 NIH gene
- Name:
- DNA polymerase delta interacting protein 2
- Previous symbol:
- -
- Synonyms:
- PDIP38, DKFZP586F1524
- Chromosome:
- 17q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-27
- Date modifiied:
- 2016-07-11
Related products to: Antibodies: POLDIP2 HOST: Goat Clonality: pAb
Alkaline Phosphatase Conjugated Affinity Purified anti-Swine IgG (H&L) [Goat] Secondary_Antibodies Alkaline Phosphatase Conjugated Affinity Purified anti_Swine IgG (H&L) [Goat] guanine nucleotide binding protein alpha inhibiting activity polypeptide 1 (GNAI1) polyclonal antibody kinase suppressor of ras (KSR) polyclonal antibody'F 4_80 Antigen (mouse) Host Rat'F 4_80 Antigen (mouse) Host Rat(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host Guinea Pig(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host Rabbit(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Guinea Pig(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Guinea Pig(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Rabbit(Arg8)-Vasopressin - Diluted Antiserum for RIA, Host: Rabbit(Arg8)-Vasopressin - EIA Kit (H - sr, pl), Host Rabbit, Extraction-free, CE-marked(Arg8)-Vasopressin - EIA Kit (H - sr, pl), Host RabbitExtraction-freeCE-marked(Arg8)-Vasopressin - EIA Kit (H - sr, pl), Host: Rabbit, Extraction-free, CE-marked Related articles to: Antibodies: POLDIP2 HOST: Goat Clonality: pAb
- Heme biosynthesis is tightly coordinated to support essential functions without accumulating toxic porphyrins and depleting cellular iron. Heme induces degradation of the heme biosynthetic enzyme, 5-aminolevulinate synthase (ALAS), by the mitochondrial caseinolytic protease complex CLPX-CLPP (CLPXP), but the mechanism for heme-triggered degradation had not been elucidated. We found that polymerase delta-interacting protein 2 (POLDIP2) is a heme-sensing adaptor protein sufficient to reconstitute negative feedback degradation of ALAS by CLPXP. POLDIP2 was necessary to support ALAS turnover in cells and regulate heme production during erythropoiesis. POLDIP2 directly recognized and recruited heme-bound ALAS to CLPXP. Degradation initiation required a carboxyl-terminal element of ALAS, truncations of which cause an erythropoietic protoporphyria. Our findings establish a mechanism for conditional degradation by CLPXP that underlies erythropoietic protoporphyrias linked to CLPX and ALAS. - Source: PubMed
Publication date: 2026/07/30
Cottle ThomasJoh LydiaPosner CoriDeCosta AdamCampagna Dean RFleming Mark DDucamp SarahKardon Julia R - The lungs are the primary target of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), with the infection resulting in lung inflammation, pulmonary vascular leakage and diffuse alveolar damage. Polymerase delta-interacting protein-2 (Poldip2) mediates lung inflammation and vascular permeability after lipopolysaccharide-induced acute respiratory distress syndrome; however, whether it also affects the pathological consequences of SARS-CoV-2 infection is completely unknown. Here, we assessed the role of Poldip2 in inflammation, immune cell infiltration and lung tissue damage in response to SARS-CoV-2. Our data show that Poldip2 expression was elevated in human lung vascular endothelium after infection. In a Poldip2-deficient heterozygous mouse model, acute clinical symptoms were not affected. However, seven days after infection, Poldip2 knockdown reduced viral load, decreased infiltration of myeloperoxidase (MPO)-positive neutrophils into inflamed lungs, and reduced tissue damage. Poldip2 also modulated the inflammatory response to viral infection in a heterogeneous manner, reflecting its diverse regulatory roles. These data support the concept that targeting Poldip2 could potentially attenuate severe lung injury following SARS-CoV-2 infection. - Source: PubMed
Publication date: 2026/04/29
Hu RuinanValdivia AlejandraWhite TaylorJu WillyBrockman Maegan LZhang ZhanQu HongyanGafford GeorgetteJoseph GijiBurton SamanthaBassit LedaCharles Tysheena PSchinazi Raymond FLevit Rebecca DDerdeyn Cynthia AGriendling Kathy KLassègue BernardHernandes Marina S - At least 70% of the human protein-coding genes contain multiple polyadenylation sites (PAS) and undergo alternative polyadenylation (APA), generating distinct transcripts from a single gene. While APA has been implicated in various physiological and pathological processes, its regulatory factors and cellular mechanisms remain incompletely understood. A previous study demonstrated that APA influences the localization of the cell surface marker CD47. Here, we present the results of a genome-wide CRISPR screen aimed at identifying APA regulators using CD47 as a reporter. Given that isoform-specific knockdown of CD47, as well as knockdown of core 3' end processing factors, alters CD47 localization, we developed an immunofluorescence-based method that simultaneously detects cell surface and intracellular CD47 protein, enabling the visualization of APA-dependent changes at the single-cell level. Leveraging this approach, we conducted a CRISPR screen and identified multiple genes affecting CD47 cell-surface expression. In addition to known membrane trafficking factors, we uncovered several nuclear factors, among which POLDIP2 emerged as a potential novel APA regulator with a global impact on APA. This study provides a foundation for further investigations into the molecular mechanisms governing APA. - Source: PubMed
Publication date: 2025/08/10
Wuttinontananchai ChayaninYamamoto JunichiSakamoto SatoshiYamaguchi Yuki - Renal angiomyolipoma (AML) encompasses benign variants (lipomatous [L-AML], myomatous [M-AML]) and epithelioid AML (eAML), a potentially malignant subtype associated with aggressive behavior. While TSC1/TSC2 mutations are frequent, the molecular drivers underlying eAML pathogenesis remain unclear. Whole-exome sequencing (WES) was performed on 35 AML samples (15 eAML, 10 L-AML, 10 M-AML) with matched germline controls. Driver genes were identified using OncodriveCLUST and MutSigCV. Validation was conducted on 71 FFPE samples integrating expression profiling and survival analysis. The finding suggested that TSC2 emerged as the most frequently mutated pathogenic gene in AML, exhibiting a mutation rate of 69 %. TSC2, POLDIP2, NEFH, and MUC2 emerged as potential driver genes across AML subtypes, whereas RHPN2, ASXL1, TOP3B, and USP35 showed subtype-specific mutations. Notably, distinct cytogenetic aberrations were observed among AML variants, including deletions at 3p26.3, 5p13.1, 6p22.1, and 11p11.11. Clonal evolution analysis suggested that l-AML and eAML, as well as M-AML and eAML, may originate from a common ancestral clone, retaining early mutations and acquiring additional alterations post-divergence. Low TSC2/POLDIP2 and high NEFH/MUC2 expression correlated with favorable survival in eAML patients. Importantly, lower TSC2/POLDIP2 expression also predicted superior response rates to Everolimus therapy. In conclusion, our study comprehensively delineates genomic distinctions and evolutionary trajectories among renal AML subtypes, establishing TSC2, POLDIP2, NEFH, and MUC2 as prognostic biomarkers and therapeutic predictors, facilitating precision medicine in eAML management. - Source: PubMed
Publication date: 2025/07/23
Anwaier AihetaimujiangQu YuanyuanYe ShiqiTian XiZhu ShuxuanZhou SiqiShi GuohaiZhu YuZhang HailiangYe DingweiXu Wenhao - Inflammation is a crucial aspect of the pathophysiology of diabetic retinopathy (DR). Polymerase delta-interacting protein 2 (Poldip2) has been linked to inflammation in various disorders, but its role in DR remains unclear. This study aims to elucidate the underlying mechanisms of Poldip2 in DR. - Source: PubMed
Publication date: 2025/05/02
Lin SiyuJi ZhiyuGao JieFan JiaweiHou JingjingLiu ShaWang ChuanxiChen KeyangTao LimingJiang Zhengxuan