CD44 is a kind I transmembrane protein expressed in varied sorts of regular most cancers cells, together with pancreatic, breast, and oral cancers. CD44 is related to most cancers development, metastases, and remedy resistance. CD44 consists of 20 exons, and varied isoforms exist on account of different splicing of the central 10 exons.
Some splicing variants present cancer-specific expression patterns and are associated to prognosis of sufferers with most cancers. Due to this fact, CD44 concentrating on remedy has been attracting consideration. In a earlier examine, we established an anti-CD44 monoclonal antibody, C44Mab-46 (IgG1, kappa), helpful for circulate cytometry, Western blotting, and immunohistochemistry by immunizing mice with CD44v3-10 ectodomain.
This examine investigated the binding epitope of C44Mab-46 utilizing enzyme-linked immunosorbent assay (ELISA) and the floor plasmon resonance (SPR) with the synthesized peptide. ELISA outcomes utilizing deletion mutants confirmed that C44Mab-46 reacted with the amino acids (aa) of 161-180 aa of CD44. Additional examination of the C44Mab-46 epitope utilizing ELISA with level mutants in 161-180 aa of CD44 demonstrates that the C44Mab-46 epitope comprised Thr174, Asp177, and Val178.
The SPR with level mutants in 161-180 aa of CD44 demonstrated that the C44Mab-46 epitope contains Thr174, Asp175, Asp176, Asp177, and Val178. Collectively, the C44Mab-46 epitope was decided to be positioned in exon 5 of CD44.
Anti–CD44-Conjugated Olive Oil Liquid Nanocapsules for Concentrating on Pancreatic Most cancers Stem Cells
The most recent traits in most cancers analysis and nanomedicine give attention to utilizing nanocarriers to focus on most cancers stem cells (CSCs). Particularly, lipid liquid nanocapsules are often developed as nanocarriers for lipophilic drug supply. Right here, we developed olive oil liquid NCs (O2LNCs) functionalized by covalent coupling of an anti-CD44-fluorescein isothiocyanate antibody (αCD44).
First, O2LNCs are fashioned by a core of olive oil surrounded by a shell containing phospholipids, a nonionic surfactant, and deoxycholic acid molecules. Then, O2LNCs have been coated with an αCD44 antibody (αCD44-O2LNC). The optimization of an αCD44 coating process, an entire physicochemical characterization, in addition to clear proof of their efficacy in vitro and in vivo have been demonstrated.
Our outcomes point out the excessive focused uptake of those αCD44-O2LNCs, and the elevated antitumor efficacy (as much as 4 occasions) of paclitaxel-loaded-αCD44-O2LNC in comparison with free paclitaxel in pancreatic CSCs (PCSCs). Additionally, αCD44-O2LNCs have been in a position to selectively goal PCSCs in an orthotopic xenotransplant in vivo mannequin.
Melanoma cells endure aggressive coalescence in a 3D Matrigel mannequin that’s repressed by anti–CD44.
Utilizing distinctive computer-assisted 3D reconstruction software program, it was beforehand demonstrated that tumorigenic cell traces derived from breast tumors, when seeded in a 3D Matrigel mannequin, grew as clonal aggregates which, after roughly 100 hours, underwent coalescence mediated by specialised cells, finally forming a extremely structured massive spheroid. Non-tumorigenic cells didn’t endure coalescence.
As a result of histological sections of melanomas forming in sufferers recommend that melanoma cells migrate and coalesce to kind tumors, we examined whether or not in addition they underwent coalescence in a 3D Matrigel mannequin. Melanoma cells exiting fragments of three impartial melanomas or from secondary cultures derived from them, and cells from the melanoma line HTB-66, all underwent coalescence mediated by specialised cells within the 3D mannequin. Regular melanocytes didn’t.
Nonetheless, coalescence of melanoma cells differed from that of breast-derived tumorigenic cell traces in that they 1) coalesced instantly, 2) underwent coalescence as particular person cells in addition to aggregates, 3) underwent coalescence far sooner and 4) in the end fashioned lengthy, flat, fenestrated aggregates that have been extraordinarily dynamic.
A display of 51 purified monoclonal antibodies (mAbs) concentrating on cell surface-associated molecules revealed that two mAbs, anti-beta 1 integrin/(CD29) and anti-CD44, blocked melanoma cell coalescence. Additionally they blocked coalescence of tumorigenic cells derived from a breast tumor.
These outcomes add weight to the commonality of coalescence as a attribute of tumorigenic cells, in addition to the usefulness of the 3D Matrigel mannequin and software program for each investigating the mechanisms regulating tumorigenesis and screening for potential anti-tumorigenesis mAbs.
Syngeneic Mouse Fashions of Oral Most cancers Are Successfully Focused by Anti–CD44-Primarily based NIR-PIT.
Oral cavity squamous cell carcinoma (OSCC) is taken into account one of the crucial aggressive subtypes of most cancers. Anti-CD44 monoclonal antibodies (mAb) are a possible remedy towards CD44 expressing OSCC; nonetheless, to this point the therapeutic results have been disappointing.
Right here, a brand new most cancers remedy is described, near-infrared photoimmunotherapy (NIR-PIT), that makes use of anti-CD44 mAbs conjugated to the photoabsorber IR700DX. This conjugate is injected into mice harboring one in all three CD44 expressing syngeneic murine oral most cancers cell (MOC) traces, MOC1 (immunogenic), MOC2 mKate2 (reasonably immunogenic), and MOC2-luc (poorly immunogenic).
Binding of the anti-CD44-IR700 conjugate was proven to be particular and cell-specific cytotoxicity was noticed after publicity of the cells to NIR mild in vitro The anti-CD44-IR700 conjugate, when assessed in vivo, demonstrated deposition inside the tumor with a excessive tumor-to-background ratio. Tumor-bearing mice have been separated into 4 cohorts: no remedy; 100 μg of anti-CD44-IR700 i.v. solely; NIR mild publicity solely; and 100 μg of anti-CD44-IR700 i.v. with NIR mild publicity.
NIR-PIT remedy, in contrast with the opposite teams, considerably inhibited tumor progress and extended survival in all three cell mannequin methods. In conclusion, these information reveal that anti-CD44 antibodies are appropriate as mAb-photoabsorber conjugates for NIR-PIT in MOC cells.
Self-assembled twin fluorescence nanoparticles for CD44-targeted supply of anti-miR-27a in liver most cancers theranostics.
Regardless of the very important position miRNA-27a performs in driving the event and progress of liver most cancers, miRNA-based inhibition remedy is hampered on account of its undesired degradation and off-target results. Herein, a multifunctional nanoparticle for noninvasive monitoring of focused supply of anti-miR-27a oligonucleotides towards liver most cancers was constructed.
Strategies: Twin-fluorescent conjugates (QD-HA-PEI) have been first fabricated by means of crosslinking hyaluronic acid (HA), polyethyleneimine (PEI) and near-infrared (NIR) fluorescent quantum dots (QDs) through a facile one-pot strategy. Antisense oligonucleotide was then encapsulated by QD-HA-PEI to kind anti-miR-27a/QD-HA-PEI through electrostatic interactions. Concentrating on, biodistribution, bioimaging, in vitro cytotoxicity and in vivo anti-tumor results have been evaluated and the underlying mechanism was studied.
Outcomes: The NIR fluorescence of anti-miR-27a/QD-HA-PEI may very well be employed to watch CD44 receptor-targeted mobile uptake and tumor accumulation. Importantly, the intrinsic fluorescence of anti-miR-27a/QD-HA-PEI remained within the “ON” state in extracellular or blood surroundings, however switched to the “OFF” state within the intracellular surroundings, indicating pH-responsive oligonucleotide launch.
PRMT5 Antibody |
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| 48880-100ul | SAB | 100ul | EUR 399.6 |
PRMT5 Antibody |
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| 48880-50ul | SAB | 50ul | EUR 286.8 |
PRMT5 Antibody |
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| E031262 | EnoGene | 100μg/100μl | EUR 255 |
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Description: Available in various conjugation types. |
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PRMT5 Antibody |
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| 1-CSB-PA018734GA01HU | Cusabio |
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Description: A polyclonal antibody against PRMT5. Recognizes PRMT5 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC |
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PRMT5 Antibody |
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| 1-CSB-PA018734LA01HU | Cusabio |
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Description: A polyclonal antibody against PRMT5. Recognizes PRMT5 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC, IF; Recommended dilution: IHC:1:20-1:200, IF:1:50-1:200 |
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PRMT5 Antibody |
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| DF6439 | Affbiotech | 200ul | EUR 420 |
PRMT5 Antibody |
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| DF6439-100ul | Affinity Biosciences | 100ul | EUR 280 |
PRMT5 Antibody |
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| DF6439-200ul | Affinity Biosciences | 200ul | EUR 350 |
PRMT5 Antibody |
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| E92290 | EnoGene | 100μg | EUR 255 |
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Description: Available in various conjugation types. |
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PRMT5 antibody |
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| CAF50275-100ug | Biomatik Corporation | 100ug | EUR 312 |
PRMT5 antibody |
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| 70R-12201 | Fitzgerald | 100 ug | EUR 343 |
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Description: Rabbit polyclonal PRMT5 antibody |
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PRMT5 antibody |
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| 70R-1032 | Fitzgerald | 100 ug | EUR 407 |
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Description: Rabbit polyclonal PRMT5 antibody raised against the N terminal of PRMT5 |
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PRMT5 antibody |
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| 70R-19537 | Fitzgerald | 50 ul | EUR 289 |
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Description: Rabbit polyclonal PRMT5 antibody |
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PRMT5 Antibody |
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| 1-CSB-PA077190 | Cusabio |
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Description: A polyclonal antibody against PRMT5. Recognizes PRMT5 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:1000-1:2000, WB:1:200-1:1000, IHC:1:15-1:50 |
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PRMT5 Antibody |
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| 1-CSB-PA107290 | Cusabio |
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Description: A polyclonal antibody against PRMT5. Recognizes PRMT5 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:1000-1:2000, WB:1:200-1:1000, IHC:1:25-1:100 |
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PRMT5 Antibody |
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| ABD6439 | Nova Lifetech | 100ug | EUR 325 |
PRMT5 Antibody |
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| F43243-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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Description: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono-and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. |
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PRMT5 Antibody |
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| F43243-0.4ML | NSJ Bioreagents | 0.4 ml | EUR 322.15 |
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Description: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono-and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. |
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PRMT5 Antibody |
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| F40460-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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Description: Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed. |
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PRMT5 Antibody |
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| F40460-0.4ML | NSJ Bioreagents | 0.4 ml | EUR 322.15 |
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Description: Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed. |
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PRMT5 Antibody |
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| F40463-0.08ML | NSJ Bioreagents | 0.08 ml | EUR 140.25 |
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Description: Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed. |
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PRMT5 Antibody |
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| F40463-0.4ML | NSJ Bioreagents | 0.4 ml | EUR 322.15 |
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Description: Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed. |
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Moreover, anti-miR-27a/QD-HA-PEI exhibited efficient and selective anti-cancer results in vitro and in vivo with fewer uncomfortable side effects through the direct down-regulation of oncogenic transcription elements FOXO1 and PPAR-γ. Conclusion: Our findings validate the dual-fluorescent nanoparticles as supply vectors of therapeutic miRNA, able to simultaneous tumor imaging and monitoring of miRNA-based modulation remedy, thereby offering an environment friendly and protected strategy for liver most cancers theranostics.
