A Preliminary Examine of the Cross-Reactivity of Canine MAGE-A with Hominid Monoclonal Antibody 6C1 in Canine Mammary Gland Tumors: An Enticing Goal for Most cancers Diagnostic, Prognostic and Immunotherapeutic Improvement in Canines
Melanoma-related antigen-A (MAGE-A), a household of most cancers/testis antigens, has been acknowledged as a possible goal molecule for most cancers immunotherapy.
Nonetheless, there was little or no data obtainable with regard to this antigen in canines. This examine aimed to research the expression of MAGE-A in canine mammary gland tumors (CMTs) utilizing immunohistochemistry and immunoblotting with human monoclonal MAGE-A antibody 6C1.
The current examine has offered proof of cross-reactivity of the canine MAGE-A expression with the human MAGE-A antibody in CMTs. The MAGE-A antigens had been expressed in moderate- and high-grade malignant CMTs (22.22%, 2/9), however no expression was noticed in benign CMTs.
The immunohistochemical staining of canine MAGE antigen in CMT cells confirmed nuclear and nuclear-cytoplasmic expression patterns that could be concerned with the mitotic cell division of tumor cells.
Molecular weights of the canine MAGE-A antigen introduced on this examine had been roughly 42-62 kDa, which had been near these of different earlier research involving people and canines.
The findings on this protein in CMTs may provide beneficial oncological data for the event of novel diagnostic, prognostic and immunotherapeutic tumor markers in veterinary medication.
Description: CD163, also known as hemoglobin scavenger receptor, is a type I transmembrane protein expressed exclusively in monocytes and macrophages. It is a scavenger receptor cysteine-rich superfamily (SRCR-SF) protein that contains nine SRCR motifs in its extracellular region. Two alternatively spliced cytoplasmic variants of human CD163 exist. A soluble form of CD163 can also be released by metalloproteinase-mediated shedding of the extracellular domain. CD163 mediates the endocytosis of haptoglobin-hemoglobin complexes.
Description: GHI/61 is an anti-human monoclonal antibody that forms an immune complex with the CD163 antigen.
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Muscle biopsy in anti-neutrophil cytoplasmic antibody-associated vasculitis: diagnostic yield is dependent upon anti-neutrophil cytoplasmic antibody kind, intercourse and neutrophil depend
Targets:Â
Examine aimed to look at the sensitivity of muscle biopsy (MB) in ANCA-associated vasculitis (AAV), determine components predicting MB positivity and assess the prognostic worth of a constructive MB.
Strategies:Â We performed a single-centre retrospective examine of AAV with an MB carried out at analysis. AAV classification [granulomatosis with polyangiitis (GPA), microscopic polyangiitis (MPA), eosinophilic granulomatosis with polyangiitis (EGPA)] adopted the European Medicines Company algorithm.
A logistic regression mannequin was used to determine the components related to MB positivity.
Survival curves had been generated utilizing the Kaplan-Meier technique.
Outcomes:Â Amongst 276 AAV sufferers (1995-2018), 101 had an MB. Seventy-eight sufferers had been included: 33 with GPA, 25 with MPA and 20 with EGPA.
MB samples had been constructive in 45 circumstances (58%): 17 GPA, 16 MPA and 12 EGPA. Univariate evaluation focussed on GPA and revealed that the MB yield was greater in females [22/31 (71%) vs 11/27 (41%); P = 0.02] and in anti-MPO sufferers [25/37 (68%) vs 6/19 (32%) for anti-PR3; P = 0.01].
By multivariate evaluation, three components predicted MB positivity: anti-MPO ANCA [odds ratio (OR) 10.67 (CI 2.09, 81.68)], feminine intercourse [OR 5.3 (CI 1.16, 32.35)] and neutrophil depend [OR 1.33 (CI 1.07, 1.8)].
MB positivity had no impression on relapse, dying or end-stage renal disease-free survival.
Conclusions:Â MB is a secure and environment friendly diagnostic instrument for AAV. Predictors of MB yield embrace ANCA kind, intercourse and neutrophil depend. MB can’t substitute for kidney biopsy when indicated, however needs to be thought of in different circumstances.
Molecular and structural foundation for Lewis glycan recognition by a cancer-targeting antibody
Immunotherapy has been profitable in treating many tumour varieties. The event of extra tumour-antigen binding monoclonal antibodies (mAbs) will assist broaden the vary of immunotherapeutic targets.
Lewis histo-blood group and associated glycans are overexpressed on many carcinomas, together with these of the colon, lung, breast, prostate and ovary, and may subsequently be selectively focused by mAbs.
Right here we study the molecular and structural foundation for recognition of prolonged Lea and Lexcontaining glycans by a chimeric mAb.
Each the murine (FG88.2) IgG3 and a chimeric (ch88.2) IgG1 mAb variants confirmed reactivity to colorectal most cancers cells resulting in considerably diminished cell viability.
We decided the X-ray construction of the unliganded ch88.2 fragment antigen-binding (Fab) containing two Fabs within the unit cell.
A mix of molecular docking, glycan grafting and molecular dynamics simulations predicts two distinct subsites for recognition of Lea and Lex trisaccharides.
Whereas mild chain residues had been completely used for Lea binding, recognition of Lex concerned each mild and heavy chain residues. An prolonged groove is predicted to accommodate the Lea-Lex hexasaccharide with adjoining subsites for every trisaccharide.
The molecular and structural particulars of the ch88.2 mAb introduced right here present perception into its cross-reactivity for varied Lea and Lexcontaining glycans. Moreover, the expected interactions with prolonged epitopes doubtless explains the selectivity of this antibody for concentrating on Lewis-positive tumours.
Key phrases:Â Carbohydrate-binding antibody; Lewis glycans; cancer-targeting antibody; molecular docking.
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: A sandwich ELISA for quantitative measurement of Mouse Podoplanin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A sandwich ELISA for quantitative measurement of Mouse Podoplanin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A sandwich ELISA for quantitative measurement of Mouse Podoplanin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Podoplanin (PDPN) in samples from tissue homogenates, cell lysates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Podoplanin (PDPN) in samples from tissue homogenates, cell lysates or other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Podoplanin (PDPN) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse PDPN. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse PDPN. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse PDPN, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse PDPN in the samples is then determined by comparing the OD of the samples to the standard curve.
Description: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse PDPN. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse PDPN. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse PDPN, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse PDPN in the samples is then determined by comparing the OD of the samples to the standard curve.
Description: Podoplanin is a well-recognized lymphatic endothelium marker, which can be used to reliably distinguish lymphatic vessels from blood vessels. It was originally discovered in kidney podocytes. This mouse monoclonal antibody (IgG) against rat podoplanin works well for immunohistochemistry with formalin-fixed paraffin embedded sections. This antibody also can be used in FACS sorting.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver (1). Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on O-glycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on O-glycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.
Description: Quantitative sandwich ELISA for measuring Mouse Podoplanin (PDPN) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Mouse Podoplanin (PDPN) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
Description: Quantitative sandwich ELISA for measuring Mouse Podoplanin (PDPN) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
