Human calumenin,CALU ELISA Kit
- Known as:
- Human calumenin,CALU Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- 201-12-1428
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Sunredbio SunBT Sun red bio
- Gene target:
- Human calumenin CALU ELISA Kit
Related genes to: Human calumenin,CALU ELISA Kit
- Gene:
- CALU NIH gene
- Name:
- calumenin
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 7q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-25
- Date modifiied:
- 2016-10-05
Related products to: Human calumenin,CALU ELISA Kit
Related articles to: Human calumenin,CALU ELISA Kit
- Local pulmonary delivery offers a non-invasive application route for mRNA therapeutics with the potential for high bioavailability at the target-site of applications such as mucosal vaccination or the treatment of lung diseases. However, efficient delivery remains challenging due to major lung-specific barriers, particularly mucus. Herein, pH-responsive, amphiphilic xenopeptides comprising lipoamino fatty acids and oligoamino acids (OAAs) connected in distinct branched U-shape or bundle topologies were evaluated as mRNA polyplexes for delivery to A549 and Calu-3 lung cells under standard submerged or air-liquid interface (ALI) transfection conditions, and upon intratracheal application in BALB/c mice. Optionally, polyplexes were coated with negatively charged hyaluronic acid (HA) or colloidally stabilized with poly(ethylene glycol) (PEG). For U-shapes, hydrophobic modification of the OAA domain boosted their efficiency. Interestingly, best-performing formulations varied across transfection conditions. While the bundle topology showed the highest potential in submerged cell culture, U-shaped carriers were more efficient under ALI conditions. Polyplex surface modification with HA or PEG did not strongly alter in vitro transfections, whereas hydrophobized U-shape core polyplexes combined with surface modification enhanced their efficiency in vivo. Thus, the cationizable core and surface properties of mRNA nanoparticles require specific balancing in various lung cell models and lung. - Source: PubMed
Publication date: 2026/05/31
Thalmayr SophieMüller JoschkaPolewka VivienGialdini IreneNguyen AnnyDohmen ChristianLamb Don CMerkel Olivia MWagner Ernst - Influenza viruses continue to pose a global health threat, and available antiviral therapies are limited by resistance and reduced efficacy. Host-directed drugs such as MEK inhibitors have emerged as promising alternatives. Zapnometinib, a clinical-stage MEK inhibitor, has shown both antiviral and immunomodulatory activity. However, its impact on antigen presentation at the level of the HLA-I ligandome has not been investigated. - Source: PubMed
Publication date: 2026/05/26
Hamza HazemGhosh MichaelRammensee Hans-GeorgPlanz Oliver - Since the publication of the previous consensus document on point-of-care lung ultrasound (PoCLUS) in 2012, new evidence has emerged. This consensus aims to update current recommendations by focusing on the clinical applications of PoCLUS as a standalone tool, while acknowledging that this focused approach represents a necessary preliminary step toward its effective integration with other organ-specific ultrasound examinations and complementary diagnostic modalities. - Source: PubMed
Publication date: 2026/06/08
Volpicelli GiovanniGargani LunaZieleskiewicz LaurentTuinman Pieter RKimura Bruce JZisis GeorgiosVaona AlbertoCoiro StefanoAraujo Gustavo NNoble VickiLaursen Christian BBouhemad BelaidSilva SteinNogué RamonZanobetti MaurizioChiumello Davide AMathis GebhardNazerian PeimanPivetta EmanueleXirouchaki NektariaZoccali CarmineCarreras-Mora JoséOveland Nils P - Coronaviruses (CoVs) rely on host surface factors to mediate viral attachment and entry, yet conserved host cofactors shared across different CoVs remain poorly defined. Here, we established a host-factor capture platform based on metabolic glycoengineering and photo-crosslinking to identify host factors associated with CoV Spike proteins under near-physiological conditions. Using this approach, we identified prohibitin (PHB) as a candidate Spike-associated host factor shared by SARS-CoV, MERS-CoV, and SARS-CoV-2. Functional analyses showed that depletion of membrane-associated PHB decreased pseudovirus infection, whereas PHB reconstitution or overexpression enhanced susceptibility across multiple cell systems, including Huh7, BEAS-2B, Calu-3, and primary human airway epithelial cells (hAECs). In addition, antibody-mediated blockade of cell-surface PHB suppressed pseudovirus entry in both hAECs and human lung organoids. Immunohistochemical analyses further demonstrated PHB expression in normal human lung tissues. Mechanistically, recombinant PHB interacted with the Spike proteins of all three CoVs, and this association was supported by surface plasmon resonance and co-immunoprecipitation assays. Structural prediction combined with fragment-based alanine scanning identified residues 139-154 within the extracellular PHB domain as a critical region for efficient Spike association. Furthermore, PHB-associated pseudovirus entry was sensitive to lipid raft disruption, supporting a role for cholesterol-dependent membrane microdomains in this process. Together, these findings identify membrane-associated PHB as a conserved Spike-associated host factor linked to CoV entry. - Source: PubMed
Publication date: 2026/06/08
Zhu XingxingWang XiaoyangWang YimingWang XinchenLi YuanhaoHua LiwenDuan HonggaoYan RongdingYuan TaoLi JingYuan YeshuangZhang BoZhou DeminXiao Sulong - Bone marrow stromal antigen 2 (BST-2, or tetherin) is an interferon-inducible host restriction factor that inhibits the release of enveloped viruses by tethering nascent virions to cellular membranes. While its antiviral function is well established in retroviral systems, its role in SARS-CoV-2 egress remains unclear. Here, we used a virus-like particle (VLP) system composed of SARS-CoV-2 structural proteins M, E, and N to investigate the impact of BST-2 on viral particle release. BST-2 significantly inhibited VLP release in HEK293T and Calu-3 lung epithelial cells. Confocal microscopy revealed that BST-2 colocalizes with viral structural proteins at the endoplasmic reticulum-Golgi intermediate compartment (ERGIC), the main site of coronavirus assembly. We next evaluated the roles of the SARS-CoV-2 accessory proteins ORF3a and ORF7a in overcoming this restriction. ORF3a localized to endolysosomal compartments and promoted VLP release through a BST-2-independent mechanism, without altering BST-2 expression or localization. In contrast, ORF7a colocalized with both BST-2 and ERGIC markers and restored VLP release by promoting BST-2 degradation. Notably, ORF7a also relieved BST-2-mediated restriction of HIV-1 VLP release, suggesting a conserved antagonistic function. These findings demonstrate BST-2 as an intracellular inhibitor of SARS-CoV-2 particle release and establish ORF7a as viral accessory antagonist that neutralizes this host defense. - Source: PubMed
Publication date: 2026/06/02
Smith AdamDong Xinhong