You Searched For: SIMS+PORTEX

Catalog Number: (BOSSBS-11446R-CY7)

Supplier: Bioss

Description: BMAL2 is a 636 amino acid protein that localizes to the nucleus and contains one bHLH (basic helix-loop-helix) domain, one PAC (PAS-associated C-terminal) domain and two PAS (PER-ARNT-SIM) domains. Expressed at high levels in placenta and brain and at lower levels in liver, thymus, heart, lung and kidney, BMAL2 functions as a component of the circadian core oscillator, which includes a variety of proteins that work in tandem to activate the transcription of target genes. More specifically, BMAL2, when functioning as a component of the core oscillator, binds to the E-box element (3'-CACGTG-5') of target DNA, thus inducing transcription. Multiple isoforms of BMAL2 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11446R-HRP)

Supplier: Bioss

Description: BMAL2 is a 636 amino acid protein that localizes to the nucleus and contains one bHLH (basic helix-loop-helix) domain, one PAC (PAS-associated C-terminal) domain and two PAS (PER-ARNT-SIM) domains. Expressed at high levels in placenta and brain and at lower levels in liver, thymus, heart, lung and kidney, BMAL2 functions as a component of the circadian core oscillator, which includes a variety of proteins that work in tandem to activate the transcription of target genes. More specifically, BMAL2, when functioning as a component of the core oscillator, binds to the E-box element (3'-CACGTG-5') of target DNA, thus inducing transcription. Multiple isoforms of BMAL2 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11446R-FITC)

Supplier: Bioss

Description: BMAL2 is a 636 amino acid protein that localizes to the nucleus and contains one bHLH (basic helix-loop-helix) domain, one PAC (PAS-associated C-terminal) domain and two PAS (PER-ARNT-SIM) domains. Expressed at high levels in placenta and brain and at lower levels in liver, thymus, heart, lung and kidney, BMAL2 functions as a component of the circadian core oscillator, which includes a variety of proteins that work in tandem to activate the transcription of target genes. More specifically, BMAL2, when functioning as a component of the core oscillator, binds to the E-box element (3'-CACGTG-5') of target DNA, thus inducing transcription. Multiple isoforms of BMAL2 exist due to alternative splicing events.

UOM: 1 * 100 µl

Supplier: Biotium

Description: 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

Description: 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

Description: 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

Description: 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.

Catalog Number: (BOSSBS-2350R)

Supplier: Bioss

Description: In mammals, several genes that encode members of the basic helix-loop helix (bHLH) PAS (PER-ARNT-SIM) transcription factor family have been shown to play a significant role in regulating circadian oscillations. Transactivation of CLOCK-induced genes is mediated via an E box enhancer (CACGTG) found upstream of target genes. CLOCK-ARNT 3 heterodimers bind to E box regulatory elements and stimulate gene transcription. CLOCK has been shown to transactivate the mammalian homolog of Drosophila PER. PER, in concert with the product of the mammalian timeless gene (TIM), negatively regulates its own transcription by blocking the activity of the CLOCK-BMAL 1 transactivation complex.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11446R-A350)

Supplier: Bioss

Description: BMAL2 is a 636 amino acid protein that localizes to the nucleus and contains one bHLH (basic helix-loop-helix) domain, one PAC (PAS-associated C-terminal) domain and two PAS (PER-ARNT-SIM) domains. Expressed at high levels in placenta and brain and at lower levels in liver, thymus, heart, lung and kidney, BMAL2 functions as a component of the circadian core oscillator, which includes a variety of proteins that work in tandem to activate the transcription of target genes. More specifically, BMAL2, when functioning as a component of the core oscillator, binds to the E-box element (3'-CACGTG-5') of target DNA, thus inducing transcription. Multiple isoforms of BMAL2 exist due to alternative splicing events.

UOM: 1 * 100 µl

Supplier: Biotium

Description: 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

Description: 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

Description: 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.

Catalog Number: (PRSI27-472)

Supplier: ProSci Inc.

Description: ARNTL is a general dimerization partner for a subset of the basic-helix-loop-helix (bHLH)-PER-ARNT-SIM (PAS) superfamily of transcriptional regulators.

UOM: 1 * 100 µG

Catalog Number: (HIMEM181-500G)

Supplier: HIMEDIA

Description: Controlled quality of materials. The different media comply with international standards. For the method of preparation and technical data sheets, please contact the customer service.

UOM: 1 * 500 g

Catalog Number: (BNUM0084-50)

Supplier: Biotium

Description: 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.

UOM: 1 * 50 µl

Supplier: Biotium

Description: 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.