IMPI _ Immunization grade porcine type I collagen, 10 mg lyophilized
- Known as:
- IMPI _ Immunization grade pig classification I collagen, 10 mg lyophilized
- Catalog number:
- 1063
- Category:
- -
- Supplier:
- Chondr
- Gene target:
- IMPI _ Immunization grade porcine type collagen 10 lyophilized
Related genes to: IMPI _ Immunization grade porcine type I collagen, 10 mg lyophilized
- Gene:
- SCARB2 NIH gene
- Name:
- scavenger receptor class B member 2
- Previous symbol:
- CD36L2
- Synonyms:
- HLGP85, LIMPII, SR-BII, LIMP-2
- Chromosome:
- 4q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-09-07
- Date modifiied:
- 2018-03-02
Related products to: IMPI _ Immunization grade porcine type I collagen, 10 mg lyophilized
α1(I) Collagen (614 - 639), Type I Collagen α1(I) C - Telopeptide, human(+/-)-Iso Myosmine , Technical Grade CAS: 53844-46-5 Formula: C9H10N2 (+_-)-Iso Myosmine , Technical Grade C9H10N2 CAS: 53844-46-5 (1,2_Dichloroethyl)benzene Practical Grade(1,2_Dichloroethyl)benzene Practical Grade(2-Hydroxypropyl)-Beta-Cyclodextrin grade: Cosmetic(2-Hydroxypropyl)-Beta-Cyclodextrin grade: Food(2-Hydroxypropyl)-Beta-Cyclodextrin grade: Pharmaceutical(2-Hydroxypropyl)-Beta-Cyclodextrin , Grade: Cosmetic(2-Hydroxypropyl)-Beta-Cyclodextrin , Grade: Food(2-Hydroxypropyl)-Beta-Cyclodextrin , Grade: Pharmaceutical(Ala11·22·28)_VIP (human, bovine, porcine, rat) Salt Trifluoroacetate Binding _ Synonym (Ala11·22·28)_Aviptadil SumFormula C139H231N43O39S(Ala11·22·28)_VIP (human, bovine, porcine, rat) Salt Trifluoroacetate Binding _ Synonym (Ala11·22·28)_Aviptadil SumFormula C139H231N43O39S(Ala31,Aib32)-Neuropeptide Y (porcine)
(Ala31,Aib32)-NPY (porcine) 98% C187H281N55O56 CAS: 313988-59-9(Ala31,Aib32)_Neuropeptide Y (porcine) Salt Trifluoroacetate Binding _ Synonym (Ala31,Aib32)_NPY (porcine) SumFormula C187H281N55O56 Related articles to: IMPI _ Immunization grade porcine type I collagen, 10 mg lyophilized
- Scavenger receptor class B, member 2 (SCARB2) is linked to Gaucher disease (GD) and Parkinson's disease (PD). Deficiency in the SCARB2 gene causes progressive myoclonus epilepsy (PME), a rare group of inherited neurodegenerative diseases characterized by myoclonus. We found that Scarb2 deficiency in mice leads to age-dependent dietary lipid malabsorption, accompanied with vitamin E deficiency. Our investigation revealed that Scarb2 deficiency is associated with gut dysbiosis and an altered bile acid pool, leading to hyperactivation of FXR in intestine. Hyperactivation of FXR impairs epithelium renewal and lipid absorption. Patients with SCARB2 mutations have a severe reduction in their vitamin E levels and cannot absorb dietary vitamin E. Finally, inhibiting FXR or supplementing vitamin E ameliorates the neuromotor impairment and neuropathy in Scarb2 knockout mice. These data indicate that gastrointestinal dysfunction is associated with SCARB2 deficiency-related neurodegeneration, and SCARB2-associated neurodegeneration can be improved by addressing the nutrition deficits and gastrointestinal issues. - Source: PubMed
Publication date: 2024/04/18
Li YinghuiLiu XingchenSun XueLi HuiWang ShigeTian WotuXiang ChenZhang XuyuanZheng JiajiaWang HaifangZhang LiguoCao LiWong Catherine C LLiu Zhihua - Enterovirus 71 (EV71) is a significant causative agent of hand, foot, and mouth disease, with potential serious neurologic complications or fatal outcomes. The lack of effective treatments for EV71 infection is attributed to its elusive pathogenicity. Our study reveals that human plasmacytoid dendritic cells (pDCs), the main type I IFN-producing cells, selectively express scavenger receptor class B, member 2 (SCARB2) and P-selectin glycoprotein ligand 1 (PSGL-1), crucial cellular receptors for EV71. Some strains of EV71 can replicate within pDCs and stimulate IFN-α production. The activation of pDCs by EV71 is hindered by Abs to PSGL-1 and soluble PSGL-1, whereas Abs to SCARB2 and soluble SCARB2 have a less pronounced effect. Our data suggest that only strains binding to PSGL-1, more commonly found in severe cases, can replicate in pDCs and induce IFN-α secretion, highlighting the importance of PSGL-1 in these processes. Furthermore, IFN-α secretion by pDCs can be triggered by EV71 or UV-inactivated EV71 virions, indicating that productive infection is not necessary for pDC activation. These findings provide new insights into the interaction between EV71 and pDCs, suggesting that pDC activation could potentially mitigate the severity of EV71-related diseases. - Source: PubMed
Publication date: 2024/04/17
Zhang XuyuanYin ZhaoZhang JialongGuo HaoLi JingyunNie XiaohuaWang ShouliZhang Liguo - Enterovirus A71 (EV-A71) infection involves a variety of receptors. Among them, two transmembrane protein receptors have been investigated in detail and shown to be critical for infection: P-selectin glycoprotein ligand-1 (PSGL-1) in lymphocytes (Jurkat cells), and scavenger receptor class B member 2 (SCARB2) in rhabdomyosarcoma (RD) cells. PSGL-1 and SCARB2 have been reported to be expressed on the surface of Jurkat and RD cells, respectively. In the work reported here, we investigated the roles of PSGL-1 and SCARB2 in the process of EV-A71 entry. We first examined the expression of SCARB2 in Jurkat cells, and detected it within the cytoplasm, but not on the cell surface. Further, using PSGL-1 and SCARB2 knockout cells, we found that although both PSGL-1 and SCARB2 are essential for virus infection of Jurkat cells, virus attachment to these cells requires only PSGL-1. These results led us to evaluate the cell surface expression and the roles of SCARB2 in other EV-A71-susceptible cell lines. Surprisingly, in contrast to the results of previous studies, we found that SCARB2 is absent from the surface of RD cells and other susceptible cell lines we examined, and that although SCARB2 is essential for infection of these cells, it is dispensable for virus attachment. These results indicate that a receptor other than SCARB2 is responsible for virus attachment to the cell and probably for internalization of virions, not only in Jurkat cells but also in RD cells and other EV-A71-susceptible cells. SCARB2 is highly concentrated in lysosomes and late endosomes, where it is likely to trigger acid-dependent uncoating of virions, the critical final step of the entry process. Our results suggest that the essential interactions between EV-A71 and SCARB2 occur, not at the cell surface, but within the cell. - Source: PubMed
Publication date: 2024/02/15
Nishimura YorihiroSato KeiKoyanagi YoshioWakita TakajiMuramatsu MasamichiShimizu HiroyukiBergelson Jeffrey MArita Minetaro - Heart failure (HF) is a widespread cardiovascular condition that poses significant risks to a wide spectrum of age groups and leads to terminal illness. Although our understanding of the underlying mechanisms of HF has improved, the available treatments still remain inadequate. Recently, long non-coding RNAs (lncRNAs) have emerged as crucial players in cardiac function, showing possibilities as potential targets for HF therapy. These versatile molecules interact with chromatin, proteins, RNA, and DNA, influencing gene regulation. Notable lncRNAs like Fendrr, Trpm3, and Scarb2 have demonstrated therapeutic potential in HF cases. Additionally, utilizing lncRNAs to forecast survival rates in HF patients and distinguish various cardiac remodeling conditions holds great promise, offering significant benefits in managing cardiovascular disease and addressing its far-reaching societal and economic impacts. This underscores the pivotal role of lncRNAs in the context of HF research and treatment. - Source: PubMed
Publication date: 2023/12/28
Jha ShambhaviThasma Loganathbabu Vasanth KanthKumaran KasinathanKrishnasamy GopinathAruljothi Kandasamy Nagarajan - Enterovirus A71 (EV-A71) is the main pathogen causing hand, foot and mouth disease (HFMD) in children and occasionally associated with neurological diseases such as aseptic meningitis, brainstem encephalitis (BE) and acute flaccid paralysis. We report here that cellular pseudokinase tribbles 3 (TRIB3) facilitates the infection of EV-A71 via dual mechanisms. In one hand, TRIB3 maintains the metabolic stability of scavenger receptor class B member 2 (SCARB2), the receptor of EV-A71, to enhance the infectious entry and spreading of the virus. On the other hand, TRIB3 facilitates the replication of EV-A71 RNA in a SCARB2-independent manner. The critical role of TRIB3 in EV-A71 infection and pathogenesis was further demonstrated in mice. In comparison to wild-type C57BL/6 mice, EV-A71 infection in TRIB3 knockdown mice () resulted in significantly lower viral loads in muscular tissues and reduced lethality and severity of clinical scores and tissue pathology. In addition, TRIB3 also promoted the replication of coxsackievirus B3 (CVB3) and coxsackievirus A16 (CVA16) . In conclusion, our results suggest that TRIB3 is one of key host cellular proteins required for the infection and pathogenesis of EV-A71 and some other human enteroviruses and may thus be a potential therapeutic target for combating the infection of those viruses. - Source: PubMed
Publication date: 2024/01/30
Wang HuiqiangLi KeCui BomingYan HaiyanWu ShuoWang KunYang GeJiang JiandongLi Yuhuan