Myeloid cells provide important functions in the low oxygen environment (O (2)) created by pathophysiological conditions, including infection sites, inflammation, tissue injuries, and solid tumors. The factors that can be induced hypoxia (HIF) are regulators of the principle of hypoxic adaptation, regulating gene expression involved in glycolysis, erythropoiesis, angiogenesis, proliferation, and stem cell function under O (2). Interestingly, the increasing evidence accumulated over the past few years shows the role of additional important regulations for HIF in inflammation.
In macrophages, HIFS not only regulates the generation of glycolytic energy, but also optimizes innate immunity, controls the expression of pro-inflammatory genes, mediates bacterial murder and affects cell migration. In neutrophils, the HIF-1α promotes the survival under O (2) – repulsive conditions and mediate blood vessel extravasation by modulating β (2) integrinizing expression. In addition, HIF contributes to inflammatory functions in various other components of innate immunity, such as dendritic cells, mast cells, and epithelial cells. This review will dissect the role of each HIF isoform in the function of myeloid cells and discuss its impact on acute and chronic inflammatory disorders.
At present, intensive studies are being carried out to illustrate the relationship between inflammation and tumorigenesis. Detailed investigations express the interaction between micro environmental factors such as hypoxia and immune cells needed. We will also discuss how hypoxia and hypox control macrophages related to tumors and their relationship with tumor formation and development.
Multidrug resistant: molecular mechanism and clinical relevance.
MultidRug Resistance (MDR) describes the phenomenon of simultaneous resistance to non-related drugs. For a decade since the P-Glycoprotein (PGP) gene, which is associated with the form of MDR caused by reducing drug accumulation, cloning. Thus, this seems to be the right time to evaluate our understanding of this form of MDR. Two MDR genes identified in humans to date (MDR related proteins [MRP] and PGP genes) are structurally similar and both are family members of the Transporter ATP-Binding Cassetter (ABC). Although the physiological role of the MRP has not been understood, one PGP gene (MDR1) plays an important role in the blood tissue barrier and the other (MDR2 / 3) involved in phospholipid transportation in the liver. Various compounds (chemosensitizing agents) can interfere with the function of PGP and MRP; Such agents can increase the efficacy of conventional therapy when used in combination with the regimen. Determining the role of cellular MDR mechanisms in the patient’s response to chemotherapy is the main challenge.
Using PGP and MRP as a molecular marker to detect MDR tumor cells technically demand, and solid tumors especially contain heterogeneous cell populations. Because the MDR requires the expression of PGP or MRP genes, a clinically relevant gene threshold needs to be set; Sequential samples of each of the patients are valuable to correlate the expression of the MDR gene with a clinical course of disease. Studies at Leukemia, Myelomas, and some childhood cancers show that PGP expression correlates with a poor response to chemotherapy. However, in some cases, the inclusion of inverters or chemosensitization such as Verapamil or Cyclosporin
A has increased clinical efficacy. Such agents can deactivate PGP in tumor cells or affect the function of PGP in normal cells, produce pharmacokinetics that change. It would be interesting to determine whether patients failed in the treatment before the chemosensitization agent obtained another MDR mechanism. ABC superfamily transporter in prokaryotes and eukaryotes are involved in transporting substrates ranging from ions to large proteins.
Hypoxia-inducible factors as essential regulators of inflammation.
Advance Pivotal: Analysis of proinflammatory activities of eukaryotic recombinant which is very purified HMGB1 (amphoterin).
HMGB1 (amphoterin) is a 30-KDA heparin protein that mediates transendotel migration from monocytes and has activities such as cytokine proinflammation. In this study, we have investigated the proinflammatory activities of eukaryotic HMGB1 which are very pure and recombinant HMGB1 proteins produced by bacteria. Bulk analysis revealed that eukaryotic recombinant HMGB1 has intracain disulfide bonds. In the mass analysis of HMGB1 originating from the network, two forms are detected: Glutamate Acid Residue Terminal Carboxyl Less Shape and Full Shape.
Cell culture studies show that eukaryotic protein and HMGB1 bacteria induce the secretion of TNF-Alpha and the release of nitric oxide from mononuclear cells. Analysis of affinity chromatography reveals that HMGB1 binds strongly to proinflammatory bacteria. The soluble proinflammation substance is separated from the recombinant hmgb1 of bacteria by the treatment of chloroform-methanol. HMGB1 interacts with phosphatidylserine in the binding of solid phases and cell culture tests, indicating that HMGB1 can regulate immune reactions that depend on phosphataidilserine. In conclusion, Polypeptide HMGB1 has a weak proinflammatory activity by itself, and it binds to bacteria, including lipids, which can strengthen the effect. ABC superfamily transporter in prokaryotes and eukaryotes are involved in transporting substrates ranging from ions to large proteins. Of the 15 ABC or more transporter genes characterized by human cells, two (PGP and MRP) caused MDR.
Matched Pair - Total RNA - Human Primary Tumor and Normal Tissue: Breast
Description: Breast cancer with matched metastatic carcinoma of lymph node tissue array, including pathology grade, TNM and clinical stage, 50 cases/100 cores, replacing BR1005a
Multiple types of cancer with matched or unmatched normal adjacent tissue array
Description: Multiple types of cancer with matched or unmatched normal adjacent tissue array, including pathology grade and TNM, 26 cases/48 cores (core size 1.5mm)
Small intestine(most of duodenum) adenocarcinoma tissue array with matched NAT or AT as control
Description: Small intestine(most of duodenum) adenocarcinoma tissue array with matched NAT or AT as control, including TNM, clinical stage and pathology grade, 50 cases/ 150 cores
Matched Pair - cDNA - Human Primary and Matched Metastatic Tumor Tissue: Colon
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).
Description: Cell-mediated immune responses are initiated by T lymphocytes that are themselves stimulated by cognate peptides bound to MHC molecules on antigen-presenting cells (APC). T-cell activation is generally self-limited as activated T cells express receptors such as PD-1 (also known as PDCD-1) that mediate inhibitory signals from the APC. PD-1 can bind two different but related ligands, PDL-1 and PDL-2. Upon binding to either of these ligands, signals generated by PD-1 inhibit the activation of the immune response in the absence of "danger signals" such as LPS or other molecules associated with bacteria or other pathogens. Evidence for this is seen in PD-1-null mice who exhibit hyperactivated immune systems and autoimmune diseases. PD-1 is thus one of a growing number of immune checkpoint proteins.ProSci's Risk-FreeTM antibodies are mouse monoclonal antibodies made to improve in vivo studies. Unlike antibodies developed using proteins made in yeast or bacteria, Risk-FreeTM antibodies are developed with antigens expressed in mammalian cell lines, giving the most native post-translational modifications to the protein. Validated for flow cytometry and ELISA Rigorously tested for the following applications: Immunoblot Immunohistochemistry Immunocytochemistry Immunofluorescence Multiple antibodies per target allowing the user to choose the best antibody for their application Available individually or as a set Risk-FreeTM means they are guaranteed to work for their approved applications
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: Cell-mediated immune responses are initiated by T lymphocytes that are themselves stimulated by cognate peptides bound to MHC molecules on antigen-presenting cells (APC). T-cell activation is generally self-limited as activated T cells express receptors such as PD-1 (also known as PDCD-1) that mediate inhibitory signals from the APC. PD-1 can bind two different but related ligands, PD-L1 and PD-L2. PD-L1 is a B7-related protein that inhibits cell-mediated immune responses by reducing the secretion of IL-2 and IL-10 from memory T cells. This suggests that PD-L1 may be useful in reducing allogenic CD4+ memory T-cell responses to endothelial cells, thereby reducing the likelihood of host immune responses to allografts.ProSci's Risk-FreeTM antibodies are mouse monoclonal antibodies made to improve in vivo studies. Unlike antibodies developed using proteins made in yeast or bacteria, Risk-FreeTM antibodies are developed with antigens expressed in mammalian cell lines, giving the most native post-translational modifications to the protein. Validated for flow cytometry and ELISA Rigorously tested for the following applications: Immunoblot Immunohistochemistry Immunocytochemistry Immunofluorescence Multiple antibodies per target allowing the user to choose the best antibody for their application Available individually or as a set Risk-FreeTM means they are guaranteed to work for their approved applications
Description: Cell-mediated immune responses are initiated by T lymphocytes that are themselves stimulated by cognate peptides bound to MHC molecules on antigen-presenting cells (APC). T-cell activation is generally self-limited as activated T cells express receptors such as PD-1 (also known as PDCD-1) that mediate inhibitory signals from the APC. PD-1 can bind two different but related ligands, PD-L1 and PD-L2. PD-L1 is a B7-related protein that inhibits cell-mediated immune responses by reducing the secretion of IL-2 and IL-10 from memory T cells. This suggests that PD-L1 may be useful in reducing allogenic CD4+ memory T-cell responses to endothelial cells, thereby reducing the likelihood of host immune responses to allografts.ProSci's Risk-FreeTM antibodies are mouse monoclonal antibodies made to improve in vivo studies. Unlike antibodies developed using proteins made in yeast or bacteria, Risk-FreeTM antibodies are developed with antigens expressed in mammalian cell lines, giving the most native post-translational modifications to the protein. Validated for flow cytometry and ELISA Rigorously tested for the following applications: Immunoblot Immunohistochemistry Immunocytochemistry Immunofluorescence Multiple antibodies per target allowing the user to choose the best antibody for their application Available individually or as a set Risk-FreeTM means they are guaranteed to work for their approved applications
Description: Cell-mediated immune responses are initiated by T lymphocytes that are themselves stimulated by cognate peptides bound to MHC molecules on antigen-presenting cells (APC). T-cell activation is generally self-limited as activated T cells express receptors such as PD-1 (also known as PDCD-1) that mediate inhibitory signals from the APC. PD-1 can bind two different but related ligands, PD-L1 and PD-L2. PD-L1 is a B7-related protein that inhibits cell-mediated immune responses by reducing the secretion of IL-2 and IL-10 from memory T cells. This suggests that PD-L1 may be useful in reducing allogenic CD4+ memory T-cell responses to endothelial cells, thereby reducing the likelihood of host immune responses to allografts.ProSci's Risk-FreeTM antibodies are mouse monoclonal antibodies made to improve in vivo studies. Unlike antibodies developed using proteins made in yeast or bacteria, Risk-FreeTM antibodies are developed with antigens expressed in mammalian cell lines, giving the most native post-translational modifications to the protein. Validated for flow cytometry and ELISA Rigorously tested for the following applications: Immunoblot Immunohistochemistry Immunocytochemistry Immunofluorescence Multiple antibodies per target allowing the user to choose the best antibody for their application Available individually or as a set Risk-FreeTM means they are guaranteed to work for their approved applications
Description: The immune checkpoint protein TIM3 is a member of the immunoglobulin superfamily and TIM family of proteins that was initially identified as a specific marker of fully differentiated IFN-γ producing CD4 T helper 1 (Th1) and CD8 cytotoxic cells. It is a Th1-specific cell surface protein that regulates macrophage activation and negatively regulates Th1-mediated auto- and alloimmune responses, and is also highly expressed on regulatory T cells, monocytes, macrophages, and dendritic cells (1). TIM3 and PD-1 are co-expressed on most CD4 and CD8 T cells infiltrating solid tumors or in hematologic malignancy in mice; blocking TIM3 in conjugation with a PD-1 blockade increases the functionality of exhausted T cells and synergizes with to inhibit tumor growth (2,3).ProSci's Risk-FreeTM antibodies are mouse monoclonal antibodies made to improve in vivo studies. Unlike antibodies developed using proteins made in yeast or bacteria, Risk-FreeTM antibodies are developed with antigens expressed in mammalian cell lines, giving the most native post-translational modifications to the protein. Validated for flow cytometry and ELISA Rigorously tested for the following applications: Immunoblot Immunohistochemistry Immunocytochemistry Immunofluorescence Multiple antibodies per target allowing the user to choose the best antibody for their application Available individually or as a set Risk-FreeTM means they are guaranteed to work for their approved applications
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: TIGIT Antibody: The T cell immunoreceptor with Ig and ITIM domains (TIGIT) is a member of the PVR (poliovirus receptor) family of immunoglobin proteins. It is expressed on several classes of T cells including follicular B helper T cells (TFH). TIGIT has been shown to bind PVR with high affinity; this binding is thought to assist interactions between TFH and dendritic cells to regulate T cell dependent B cell responses (1). Similar to other immune checkpoint proteins such as PD-1, TIGIT is upregulated on exhausted T cells in chronic viral infections and cancer. Blockade of both TIGIT and PD-1 pathways leads to tumor rejection in mice suggesting that it may be of therapeutic use against cancer (2).
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: Colon cancer with matched colon tissue array, including pathology grade,with MMR (MLH1/PMS2/MSH2/MSH6) IHC results, TNM and clinical stage, containing 90 cases of adenocarcinoma, and 90 cancer adjacent or adjacent normal colon tissue, 90 cases/180 cores, replacing CO1801
Description: Breast cancer with matched breast tissue array, including pathology grade, IHC info (ER,PR,Her-2,Ki67),TNM\Stage, 6 cases/24 cores (core size 1.5mm), replacing BR251d
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Lung cancer and matched adjacent lung tissue array
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus. The disease is the cause of the 2019–20 coronavirus outbreak (1). SARS-CoV-2 is the seventh member of the enveloped, positive-stranded RNA viruses that are able to infect humans. The SARS-CoV-2 genome, like other coronaviruses, encodes for multiple structural and nonstructural proteins. The structural proteins include spike protein (S), envelope protein (E), membrane glycoprotein (M), nucleocapsid phosphoprotein (N), and the nonstructural proteins include open reading frame 1ab (ORF1ab), ORF3a, ORF6, ORF7a, ORF8, and ORF10 (2). Nucleocapsid (N) protein is the most abundant protein of coronavirus. It is also one of the major structural proteins and is involved in the transcription and replication of viral RNA, packaging of the encapsidated genome into virions (3), and interference with cell cycle processes of host cells (4). Moreover, in many coronaviruses, including SARS-CoV, the N protein has high immunogenic activity and is abundantly expressed during infection (5). It can be detected in various patient samples including nasopharyngeal aspirate, urine, and fecal. Both S and N proteins may be potential antigens for serodiagnosis of COVID-19, just as many diagnostic methods have been developed for diagnosing SARS based on S and/or N proteins (6).
Matched Pair Tissue Slides - Small Intestine Tissue
Description: The Matched Pair Paraffin Tissue (MPPT) slides are designed for identifying tumor-specific/metastasis genes or proteins. Slices from normal and malignant tissues are mounted on each MPPT slide which can then be treated as a single histological slide for H&E staining, immunohistochemistry, or in situ hybridization. This format allows a rapid analysis of protein expression and localization across normal and cancerous tissue.
Description: Colon cancer with matched adjacent normal colon tissue, including pathology grade, TNM and clinical stage, 16 cases/32 cores, replacing CO321
Matched Pair - DNA - Human Primary Tumor and Normal Tissue: Breast
Description: Rectum cancer with matched adjacent normal tissue array, including pathology grade, TNM and clinical stage, 40 cases/80 cores
×
Therefore, it will be relevant to determine the number of genes like that in the human genome; However, extrapolation of the amount of ABC transporter genes in bacteria, human genes may contain a minimum of 200 members of the Superfamily ABC Transporter. Thus, tumor cells have the potential to use many ABC transporters to install resistance to known therapeutic agents and in the future. The challenge is to determine which ABC transporter is clinically relevant. Apart from the potential of tumor cells to protect themselves, various malignancies can be treated with chemotherapy. This can provide unique insights.
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