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Phase I Study of Yttrium-90 Radiolabeled M5A Anti-Carcinoembryonic Antigen Humanized Antibody in Patients with Advanced Carcinoembryonic Antigen Producing Malignancies.

M5A is a humanized monoclonal antibody (mAb) directed against carcinoembryonic antigen (CEA) The purpose of this first in human phase I dose-escalation trial was to characterize the toxicities and determine the maximum tolerated dose (MTD) of yttrium-90 (Y)-DOTA-M5A as a single agent and in combination with gemcitabine (gem). Patients with advanced metastatic CEA-producing malignancies who had progressed on standard therapies were first administered indium-111 (In)-DOTA-M5A. If tumor targeting was observed, the patient then received the therapy dose of Y-DOTA-M5A. Serial scans, blood sampling, and 24 h urine collections were then performed to estimate radiation doses to organs and total body. Assays for human antihuman antibody (HAHA) responses were performed out to 6 months. Of the 18 patients who received In-DOTA-M5A, 16 received Y-DOTA-M5A therapy; 1 patient at 14 mCi/m with gem (150 mg/m days 1and 3), 3 patients at 12 mCi/m with gem, 6 patients at 12 mCi/m without gem, and 6 at 10 mCi/m without gem. Prolonged cytopenias resulted in discontinuation of dose escalation with gemcitabine. A single agent MTD of 10 mCi/m was established based on dose-limiting hematopoietic toxicities. HAHA immune response was identified in 2 of 16 patients (12.5%). Stable disease at 3 months was seen in 10 patients and 2 patients demonstrated an 88% and 64% decrease in CEA back to normal levels. In 2 patients In-DOTA-M5A imaging revealed previously unknown brain metastases. This study demonstrates the potential utility of the Y-DOTA-M5A anti-CEA mAb as a therapeutic antibody. There is decreased immunogenicity compared with murine and chimeric mAbs, allowing for the potential of multiple administrations. Combined modality therapy approaches incorporating this agent should continue to be evaluated.

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anti CD66e IgG1 monoclona Mouse Anti-Insulin-Like G Anti 3 DG imidazolone Mon Mouse Anti-Human Carcinoe anti CD54 IgG2b k monoclo Mouse Anti P.aeruginosa s Prostate cancer, hyperpla Mouse Anti Salmonella typ Mouse Anti-Lipoprotein Li Mouse Anti P.aeruginosa s Mouse Anti P. aeruginosa Mouse Anti Shigella boydi

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Universal Affinity Capture Liquid Chromatography-Mass Spectrometry Assay for Evaluation of Biotransformation of Site-Specific Antibody Drug Conjugates in Preclinical Studies.

Antibody drug conjugates (ADCs) can undergo in vivo biotransformation (e.g., payload metabolism, deconjugation) leading to reduced or complete loss of activity. The location/site of conjugation of payload-linker can have an effect on ADC stability and hence needs to be carefully optimized. Affinity capture LC-MS of intact ADCs or ADC subfragments has been extensively used to evaluate ADC biotransformation. However, the current methods have certain limitations such as the requirement of specific capture reagents, limited mass resolution of low mass change metabolites, low sensitivity, and use of capillary or nanoflow LC-MS. To address these challenges, we developed a generic affinity capture LC-MS assay that can be utilized to evaluate the biotransformation of any site-specific ADC independent of antibody type and site of conjugation (Fab and Fc) in preclinical studies. The method involves a combination of some or all of these steps: (1) "mono capture" or "dual capture" of ADCs from serum with streptavidin magnetic beads coated with a generic biotinylated antihuman capture reagent, (2) "on-bead" digestion with IdeS and/or PNGase F, and (3) reduction of interchain disulfide bonds to generate ∼25 kDa ADC subfragments, which are finally analyzed by LC-HRMS on a TOF mass spectrometer. The advantages of this method are that it can be performed using commercially available generic reagents and requires sample preparation time of less than 7 h. Furthermore, by reducing the size of intact ADC (∼150 kDa) to subfragments (∼25 kDa), the identification of conjugated payload and its metabolites can be achieved with excellent sensitivity and resolution (hydrolysis and other small mass change metabolites). This method was successfully applied to evaluate the in vitro and in vivo biotransformation of ADCs conjugated at different sites (LC, HC-Fab, and HC-Fc) with various classes of payload-linkers.

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MOUSE ANTI HUMAN CD15, Pr Th1 Th2 Th17 (Human) Anti Caspase 8 Inhibitor Drug Cytokine (Human) Antibody Cell cycle antibody array RABBIT ANTI GSK3 BETA (pS Cytokine (Human) Antibody Cytokine (Rat) Antibody A Th1 Th2 Th17 (Human) Anti Cytokine (Human) Antibody Anti AGO2 Human, Monoclon Cytokine (Mouse) Antibody

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Modeling antimalarial and antihuman African trypanosomiasis compounds: a ligand- and structure-based approaches.

This study examines the interaction of 137 antimalarial and antihuman African trypanosomiasis compounds [bis(2-aminoimidazolines), bisguanidinediphenyls and polyamines] on three different in vitro assays (Trypanosoma brucei rhodesiense (T.b.r.), Plasmodium falciparum (P.f.) and cytotoxicity-L6 cells). ΔT values, wherever available, were also examined for the considered ligands. Eight DNA-ligand complexes and one DNA structure without ligand were selected from protein data bank (PDB) based on the structural similarity. Geometry optimization of all the considered ligands was carried out at the B3LYP/6-31G(d) level of theory. The AutoDock4 tool was utilized for the docking of these molecules at the minor groove of nine selected DNA crystal structures. We observed DT20, DA6, DT8 and DT19 residues generally interact with most of the considered ligands. Molecular dynamics simulations, molecular mechanics-generalized born surface area and molecular mechanics-Poisson Boltzmann surface area calculations indicate that the docked poses are generally stable and docked ligands do not show much deviation in the minor groove of DNA until 10 ns simulation. Efficient and statistically significant quantitative structure-activity relationship models for T.b.r., P.f., C-L6 and ΔT values were developed. All the generated models are internally and externally validated. We predicted a few ligands with significant IC values against P.f. based on the developed models. These results may help to design new and potent antimalarial and antihuman African trypanosomal compounds.

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19 Hydroxy 4 androstene 3 Rabbit Anti-Rat Androgen Androgen Receptor (Ab-650 5α-N-Acetyl-2'H-androst- Androgen Receptor , Mouse 3β-O-Acetyl-androsta-5,1 5α-Androstan-3β-ol � Androstane 3a, 17b diol 5 ∆1-Androstene-3α,17β- Goat Anti-Human Androgen Androgen Receptor (Phosph Andrographolide CAS Numbe

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Immunohistochemical expression of P53, Ki-67, and CD34 in psoriasis and psoriasiform dermatitis.

Psoriasis is the prime example of psoriasiform tissue pattern and should be differentiated from other psoriasiform dermatoses both clinically and histopathologically.

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Androgen Receptor (Phosph Androgen Receptor (Phosph Androgen Receptor Ab-1 An Andrographolide C20H30O5 rac Androst-16-en-2,2,5,6 3-O-Acetyl 5,14-Androstad CAR,CAR,Constitutive acti ∆2-Androstene-1α,17β- Androstenedione 19 Androgen Receptor Antibod Androgen Receptor Antibod 5α-N-Acetyl-2'H-androst-

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CD30 Cross-Reactivity and Expression in Feline Normal Tissues and Lymphomas.

CD30 is a transmembrane glycoprotein of the tumor necrosis factor receptor superfamily included in the diagnostic algorithm of human cutaneous, anaplastic large cell and Hodgkin lymphomas and represents an optimal therapeutic target for CD30 tumors. Similar diagnostic and therapeutic approaches are largely missing for feline lymphomas. Cross-reactivity of the antihuman CD30 receptor clone Ber-H2 was investigated in feline lymphomas. Comparative analysis of feline and human CD30 identified 61% identity of the amino acid sequence, with 100% identity of the main sequence of the epitope targeted by the antibody (RKQCEPDYYL). CD30 expression in normal feline tissues was restricted to rare lymphoid cells in perifollicular and interfollicular lymph node areas and in the thymic medulla. In feline lymphoma, CD30 was expressed in 4 of 33 (13%) T-cell lymphomas, 3 of 22 (14%) B-cell lymphomas, and 5 of 7 (71%) mixed-cell lymphomas, showing diffuse (1/5) or multifocal (4/5) positivity restricted to neoplastic multinucleated lymphoid cells and binucleated cells consistent with Reed-Sternberg-like cells. Based on the human classification system, cell morphology, expression of multiple markers (mixed cell components), and CD30 positivity, these cases were considered most consistent with classical Hodgkin-like lymphoma (HLL). The other 2 mixed-cell lymphomas were CD30 negative and thus most consistent with either T-cell-rich large B-cell lymphoma (TCRLBCL) or nodular lymphocyte-predominant Hodgkin lymphoma (NLPHL). These findings provide multiple data supporting the cross-reactivity of the Ber-H2 anti-CD30 clone in feline tissues and give evidence of the usefulness of CD30 in the diagnostic evaluation of feline lymphoma.

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Multiple stomach cancer t Cervix cancer test tissue Liver cancer tissue array Prostate cancer test tiss Skin cancer test tissue a Liver cancer test tissue High density ovarian canc Kidney cancer tissue arra Esophageal cancer tissue High density stomach canc Multiple breast cancer ti Colon cancer tissue array

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Acidification of plasma for detection of pHdependent antibodies.

Most antibodies to blood group antigens react optimally at a pH range of 6.5-7.5, similar to that of normal plasma or serum. Some antibodies, however, including anti-M, react preferentially or exclusively in an acidic environment with a pH below 6.5. Antibodies with anti-M specificity often show dosage. They can be weakly reactive and even look like nonspecific reactivity at the antihuman globulin phase especially when immediate spin and/or room temperature testing is not part of routine screening. Acidification of serum or plasma may help to identify these antibodies as clinically insignificant versus as an unidentified antibody for which clinical significance is unknown.

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Antibodies, Rabbit: Anti Formaldehyde Detection Ki Rat Forkhead Box P3(FOXP3 Ofloxacin CAS Number [824 Mouse Anti-Fibronectin (P Proteins and Antibodies H MarkerGeneTM Fluorescent Non Swiss Albino Mouse Pl Rat Anti-Mouse SIGN-R1 [+ Mouse Anti-HSV-2 gG Antib 5-Acetylamino-6-formylami Goat Anti- AVPR2, (C Term

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Matrine Promotes Human Myeloid Leukemia Cells Apoptosis Through Warburg Effect Mediated by Hexokinase 2.

Matrine, an alkaloid compound isolated from the medicinal plant , inhibits many types of cancer proliferation. However, the precise mechanism of the matrine antihuman chronic myeloid leukemia remains unclear. In this study, we showed that matrine significantly inhibited the cell proliferation and induced apoptosis by regulating Warburg effect through controlling hexokinases 2 (HK2) expression in myeloid leukemia cells. Interestingly, matrine inhibited the expression of HK2 mediated by reduction in c-Myc binding to HK2 gene intron and led to downregulation of HK2, which upregulated proapoptotic protein Bad and then induced apoptosis. We further demonstrated that matrine could synergize with lonidamine, an inhibitor of HK2, for the treatment of myeloid leukemia, both and . Taken together, our findings reveal that matrine could promote human myeloid leukemia cells apoptosis regulating Warburg effect by controlling HK2.

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RFP Expressing Human Reti Rabbit Anti-Apoptosis enh Mouse Anti-Human Follicul Human Small Intestine Mic Mouse Anti-Human Follicul Epidermal Growth Factor ( Human Cardiac Microvascul Recombinant Human THPO [f Human Factor related Apop GFP Expressing Human Brai Apoptosis-enhancing nucle Apoptosis Related Protein

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The efficacy of third generation anti‑HER2 chimeric antigen receptor T cells in combination with PD1 blockade against malignant glioblastoma cells.

Without effective treatment, glioblastoma is one of the deadliest cancers worldwide. The aim of the present study was to explore whether combinational immunotherapy is effective for treating malignant glioblastoma in vitro. The therapeutic efficacy of third generation anti‑human epidermal growth factor receptor 2 (HER2) chimeric antigen receptor (CAR)‑T cells alone and in combination with PD1 blockade was investigated for the treatment of malignant glioblastoma cells in vitro. Anti‑HER2 CAR‑T cells were prepared by transducing activated primary human T cells with lentiviruses which expressed third generation anti‑HER2 CAR. The CAR‑positive cell ratio was detected using flow cytometry. The expression level of CAR was detected by western blot analysis. The binding of anti‑HER2 CAR‑T cells to HER2+ U251 glioblastoma cells was examined under a fluorescence microscope. The cytokine secretion of CAR‑T cells induced by target cells was analyzed via ELISA. The cytotoxicity of anti‑HER2 CAR‑T cells alone or in combination with anti‑programmed death‑1 (PD1) antibody against HER2+/PDL1+ U251 cells was examined using an LDH assay. The CAR‑positive cell ratio and expression level of CAR in prepared CAR‑T cells were both high enough. Anti‑HER2 CAR‑T cells could specifically bind to U251 cells. The IL‑2 and IFN‑γ secretion of CAR‑T cells increased after being co‑cultured with U251 cells, and further increased in the presence of anti‑PD1 antibody. Anti‑HER2 CAR‑T cells displayed a potent cytotoxicity against U251 cells. In addition, the presence of anti‑PD1 antibody further enhanced the efficacy of anti‑HER2 CAR‑T cells against U251 cells. The present results indicated that blocking PD1 immuno‑suppression can increase the activation of CAR‑T cells after they are activated by a targeting antigen. Third generation anti‑HER2 CAR‑T cells along with PD1 blockade have a great therapeutic potential for combatting malignant glioblastoma.

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anti Transferrin receptor anti HSV (II) gB IgG1 (mo anti CD38 Hematopoietic p anti HCMV IE pp65 IgG1 (m Rat monoclonal anti mouse anti CD45 RA B cells, T c Mouse Anti-Human CD34 Tar Dog Receptor-binding canc Rat Anti-Mouse Dendritic Rat monoclonal anti mouse anti CD7 All T cells Reco anti HCMV gB IgG1 (monocl

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Design and Biological Evaluation of -Xylene Thioether-Stapled Short Helical Peptides Targeting the HIV-1 gp41 Hexameric Coiled-Coil Fusion Complex.

Short peptide-based inhibition of fusion remains an attractive goal in antihuman immunodeficiency virus (HIV) research based on its potential for the development of technically and economically desirable antiviral agents. Herein, we report the use of the dithiol bisalkylation reaction to generate a series of -xylene thioether-stapled 22-residue α-helical peptides that have been identified as fusion inhibitors targeting HIV-1 glycoprotein 41 (gp41). The peptide sequence is based on the helix-zone binding domain of the gp41 C-terminal heptad repeat region. We found that one of these stapled peptides, named hCS6ERE, showed promising inhibitory potency against HIV-1 Env-mediated cell-cell fusion and viral replication at a level comparable to the clinically used 36- peptide T20. Furthermore, combining hCS6ERE with a fusion inhibitor having a different target site, such as HP23, produced synergistic anti-HIV-1 activity. Collectively, our study offers new insight into the design of anti-HIV peptides with short sequences.

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Recombinant HIV Type-O gp coiled-coil domain contai Recombinant HIV-1 gp41 [M Anti-Androgen Receptor pr Rabbit Anti-Human Androge Androstane-3a,17b-diol Gl Rhodamine B octadecyl est Sterile filtered human se TCP-1 theta antibody Sour Recombinant HIV-1 gp41 Lo Androgen Receptor (Ab-650 Androgen Receptor Antibod

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Evaluation of Human Anti IgG Polyclonal Antibody Production Conjugated with Peroxidase in Egg Yolk.

Egg yolk is a rich and accessible source of yolk immunoglobulin (Y immunoglobulin). Presently, polyclonal antibodies from mammalian sources are used for diagnosis. Antibody production from egg yolk gives a higher yield and turnover than that from lab animals, and invasive methods such as phlebotomy and causing stress to the animals are not required. Due to the issues regarding mammalian antibodies, we aimed to evaluate the human anti-IgG polyclonal antibody production conjugated with peroxidase in egg yolk.

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