3663 Results for: "Samarium+tribromide+hexahydrate&pageNo=84&view=list"

Supplier: Abcam

Rabbit monoclonal [EPR28346-84] to Heparan Sulfate Proteoglycan 2/Perlecan.

Supplier: Biotium

This antibody recognizes a cell surface glycoprotein of 95/115/135 kDa (depending upon the extent of glycosylation), identified as CD43 (Workshop III). 70-90% of T-cell lymphomas and from 22-37% of B-cell lymphomas express CD43. No reactivity has been observed with reactive B-cells. So a B-lineage population that co-expresses CD43 is highly likely to be a malignant lymphoma, especially a low-grade lymphoma, rather than a reactive B-cell population. When CD43 antibody is used in combination with anti-CD20, effective immunophenotyping of the lymphomas in formalin-fixed tissues can be obtained. Co-staining of a lymphoid infiltrate with anti-CD20 and anti-CD43 argues against a reactive process and favors a diagnosis of lymphoma.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Biotium

This antibody recognizes a cell surface glycoprotein of 95/115/135 kDa (depending upon the extent of glycosylation), identified as CD43 (Workshop III). 70-90% of T-cell lymphomas and from 22-37% of B-cell lymphomas express CD43. No reactivity has been observed with reactive B-cells. So a B-lineage population that co-expresses CD43 is highly likely to be a malignant lymphoma, especially a low-grade lymphoma, rather than a reactive B-cell population. When CD43 antibody is used in combination with anti-CD20, effective immunophenotyping of the lymphomas in formalin-fixed tissues can be obtained. Co-staining of a lymphoid infiltrate with anti-CD20 and anti-CD43 argues against a reactive process and favors a diagnosis of lymphoma.

Supplier: Biotium

This antibody recognizes a cell surface glycoprotein of 95/115/135 kDa (depending upon the extent of glycosylation), identified as CD43 (Workshop III). 70-90% of T-cell lymphomas and from 22-37% of B-cell lymphomas express CD43. No reactivity has been observed with reactive B-cells. So a B-lineage population that co-expresses CD43 is highly likely to be a malignant lymphoma, especially a low-grade lymphoma, rather than a reactive B-cell population. When CD43 antibody is used in combination with anti-CD20, effective immunophenotyping of the lymphomas in formalin-fixed tissues can be obtained. Co-staining of a lymphoid infiltrate with anti-CD20 and anti-CD43 argues against a reactive process and favors a diagnosis of lymphoma.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Abcam

Rabbit monoclonal [EPR29356-84] to Influenza A Polymerase basic protein 2.

Supplier: OriGene

Anti-SPN Mouse Polyclonal Antibody [clone: eBio84-3C1 (84-3C1)]

Supplier: Abcam

Rabbit monoclonal [EPR26994-84] to Phosphoserine Aminotransferase - BSA and Azide free (Detector).

Supplier: Abcam

Rabbit monoclonal [EPR22926-84] to IL-1RA - BSA and Azide free (Detector).

Supplier: Abcam

Rabbit monoclonal [EPR25741-84] to beta Arrestin 1 - BSA and Azide free (Detector).

Supplier: Abcam

Alexa Fluor® 647 Rabbit monoclonal [EPR24781-84] to CCL18.

Supplier: Abcam

Rabbit monoclonal [EPR16803-84] to TNF alpha - BSA and Azide free (Detector).

Supplier: Abcam

Rabbit monoclonal [EPR20165-84] to C1 inhibitor - BSA and Azide free (Detector).

Supplier: Abcam

Alexa Fluor® 488 Rabbit monoclonal [EPR24781-84] to CCL18.

Supplier: Abcam

Rabbit monoclonal [EPR24842-84] to SARS-COV-2 nsp3 - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR28288-84] to Laminin alpha 5/LAMA5 - BSA and Azide free.

Supplier: ANTIBODIES.COM

Anti-GOLGA5/Golgin-84 Rabbit Polyclonal Antibody

Supplier: Abcam

Alexa Fluor® 647 Rabbit monoclonal [EPR26093-84] to Lrp2 / Megalin.

Supplier: Biotium

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (HIF-1 alpha and HIF-1 beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha protein is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIF1s regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.

Supplier: Abcam

Rabbit monoclonal [EPR29356-84] to Influenza A Polymerase basic protein 2 - BSA and Azide free.

Supplier: Biotium

This antibody recognizes a cell surface glycoprotein of 95/115/135 kDa (depending upon the extent of glycosylation), identified as CD43 (Workshop III). 70-90% of T-cell lymphomas and from 22-37% of B-cell lymphomas express CD43. No reactivity has been observed with reactive B-cells. So a B-lineage population that co-expresses CD43 is highly likely to be a malignant lymphoma, especially a low-grade lymphoma, rather than a reactive B-cell population. When CD43 antibody is used in combination with anti-CD20, effective immunophenotyping of the lymphomas in formalin-fixed tissues can be obtained. Co-staining of a lymphoid infiltrate with anti-CD20 and anti-CD43 argues against a reactive process and favors a diagnosis of lymphoma.

Supplier: Abcam

Rabbit monoclonal [EPR28346-84] to Heparan Sulfate Proteoglycan 2/Perlecan - BSA and Azide free.

Supplier: SCHOTT AG Lighting and imaging

TLS adapter Ø = 84 for base plate Ø 100 mm

Supplier: PerkinElmer

Elemental analyser, Axial view purge extension window

Supplier: ProSci Inc.

HIF1 (hypoxia-inducible factor 1), a heterodimeric transcription factor complex central to cellular response to hypoxia, consists of two subunits (alpha and beta) which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family. Expression of HIF-1 alpha is regulated by cellular oxygen level alterations as well as in oxygen-independent manner via different cytokines (through the PI3K-AKT-mTOR pathway), growth factors, oncogenic activation, or loss of tumor suppressor function etc. In normoxic cells, HIF-1 alpha is proline hydroxylated leading to a conformational change that promotes its binding to the VLH (von Hippel Lindau) protein E3 ligase complex; ubiquitination and followed by rapid proteasomal degradation. Hypoxia as well as chemical hydroxylase inhibitors (desferrioxamine, cobalt etc.) inhibit HIF-1 alpha degradation and lead to its accumulation in the cells, whereas, contrastingly, HIF-1 beta/ARNT (AhR nuclear translocator) remains stable under both conditions. Besides their critical role in hypoxic response, HIFs regulates the transcription of genes responsible for angiogenesis, erythropoiesis/iron-metabolism, glucose metabolism, cell proliferation/survival, adipogenesis, carotid body formation, B lymphocyte development and immune reactions.