1062 Ergebnisse für: "Other Essentials"

Supplier: Bioss

Selenium is an essential trace element that confers tolerance to toxicity arising through exposure to heavy metals or other reactive xenobiotics. Selenium exhibits potent anticarcinogenic properties, and deficiency of selenium may cause certain neurologic diseases. Both effects are attributed to selenium-binding proteins. Selenium binding protein 1 is down-regulated in lung adenocarcinoma, colorectal cander and ovarian cancer. It is two-fold upregulated in the brains of patients suffering from schizophrenia, and is therefore a biomarker for this disease.

Supplier: Bioss

Selenium is an essential trace element that confers tolerance to toxicity arising through exposure to heavy metals or other reactive xenobiotics. Selenium exhibits potent anticarcinogenic properties, and deficiency of selenium may cause certain neurologic diseases. Both effects are attributed to selenium-binding proteins. Selenium binding protein 1 is down-regulated in lung adenocarcinoma, colorectal cander and ovarian cancer. It is two-fold upregulated in the brains of patients suffering from schizophrenia, and is therefore a biomarker for this disease.

Supplier: Bioss

Selenium is an essential trace element that confers tolerance to toxicity arising through exposure to heavy metals or other reactive xenobiotics. Selenium exhibits potent anticarcinogenic properties, and deficiency of selenium may cause certain neurologic diseases. Both effects are attributed to selenium-binding proteins. Selenium binding protein 1 is down-regulated in lung adenocarcinoma, colorectal cander and ovarian cancer. It is two-fold upregulated in the brains of patients suffering from schizophrenia, and is therefore a biomarker for this disease.

Supplier: Bioss

Selenium is an essential trace element that confers tolerance to toxicity arising through exposure to heavy metals or other reactive xenobiotics. Selenium exhibits potent anticarcinogenic properties, and deficiency of selenium may cause certain neurologic diseases. Both effects are attributed to selenium-binding proteins. Selenium binding protein 1 is down-regulated in lung adenocarcinoma, colorectal cander and ovarian cancer. It is two-fold upregulated in the brains of patients suffering from schizophrenia, and is therefore a biomarker for this disease.

Supplier: Bioss

Selenium is an essential trace element that confers tolerance to toxicity arising through exposure to heavy metals or other reactive xenobiotics. Selenium exhibits potent anticarcinogenic properties, and deficiency of selenium may cause certain neurologic diseases. Both effects are attributed to selenium-binding proteins. Selenium binding protein 1 is down-regulated in lung adenocarcinoma, colourectal cander and ovarian cancer. It is two-fold upregulated in the brains of patients suffering from schizophrenia, and is therefore a biomarker for this disease.

Supplier: ENZO LIFE SCIENCES

Centromere protein A (CENP-A), a 17-19 kDa centromere-specific histone variant, is 62% identical to the carboxy-terminal domain of histone H3.  In the presence of DNA, CENP-A forms an octameric complex with histones H4, H2A, and H2B.  CENP-A defines active centromere regions by forming centromere-specific nucleosomes on which kinetochores are assembled.  CENP-A resides specifically in the inner plate of the kinetochore, and is essential for kinetochore targeting of CENP-C and other kinetochore components.  CENP-A is required for nucleosomal packaging of centromeric DNA at interphase.

Supplier: Bioss

Essential bifunctional enzyme that catalyses both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA dissacharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response.

Supplier: Bioss

Essential bifunctional enzyme that catalyses both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA dissacharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response.

Supplier: Bioss

H2BFWT (H2B histone family member W testis-specific) is a 175 amino acid nuclear membrane histone that belongs to the histone H2B family. In contrast to most H2B histones, H2BFWT does not contain the conserved C-terminal residue involved in monoubiquitination, but is structurally indistinguishable from conventional H2B histones. Also varying from other H2B histones, H2BFWT does not participate in the recruitment of chromosome condensation factors or in the assembly of mitotic chromsomes. Expressed in testis, H2BFWT is present in sperm cells and may be essential to telomere function.

Supplier: Bioss

H2BFWT (H2B histone family member W testis-specific) is a 175 amino acid nuclear membrane histone that belongs to the histone H2B family. In contrast to most H2B histones, H2BFWT does not contain the conserved C-terminal residue involved in monoubiquitination, but is structurally indistinguishable from conventional H2B histones. Also varying from other H2B histones, H2BFWT does not participate in the recruitment of chromosome condensation factors or in the assembly of mitotic chromsomes. Expressed in testis, H2BFWT is present in sperm cells and may be essential to telomere function.

Supplier: Bioss

H2BFWT (H2B histone family member W testis-specific) is a 175 amino acid nuclear membrane histone that belongs to the histone H2B family. In contrast to most H2B histones, H2BFWT does not contain the conserved C-terminal residue involved in monoubiquitination, but is structurally indistinguishable from conventional H2B histones. Also varying from other H2B histones, H2BFWT does not participate in the recruitment of chromosome condensation factors or in the assembly of mitotic chromsomes. Expressed in testis, H2BFWT is present in sperm cells and may be essential to telomere function.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

H2BFWT (H2B histone family member W testis-specific) is a 175 amino acid nuclear membrane histone that belongs to the histone H2B family. In contrast to most H2B histones, H2BFWT does not contain the conserved C-terminal residue involved in monoubiquitination, but is structurally indistinguishable from conventional H2B histones. Also varying from other H2B histones, H2BFWT does not participate in the recruitment of chromosome condensation factors or in the assembly of mitotic chromsomes. Expressed in testis, H2BFWT is present in sperm cells and may be essential to telomere function.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: ProSci Inc.

This protein is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co-immunoprecipitate with MCM4, 6 and 7, which suggests that it may interact with other MCM proteins and play a role in DNA replication.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co-immunoprecipitate with MCM4, 6 and 7, which suggests that it may interact with other MCM proteins and play a role in DNA replication. Alternatively spliced transcript variants encoding distinct isoforms have been described.

Supplier: Bioss

H2BFWT (H2B histone family member W testis-specific) is a 175 amino acid nuclear membrane histone that belongs to the histone H2B family. In contrast to most H2B histones, H2BFWT does not contain the conserved C-terminal residue involved in monoubiquitination, but is structurally indistinguishable from conventional H2B histones. Also varying from other H2B histones, H2BFWT does not participate in the recruitment of chromosome condensation factors or in the assembly of mitotic chromsomes. Expressed in testis, H2BFWT is present in sperm cells and may be essential to telomere function.

Supplier: Bioss

H2BFWT (H2B histone family member W testis-specific) is a 175 amino acid nuclear membrane histone that belongs to the histone H2B family. In contrast to most H2B histones, H2BFWT does not contain the conserved C-terminal residue involved in monoubiquitination, but is structurally indistinguishable from conventional H2B histones. Also varying from other H2B histones, H2BFWT does not participate in the recruitment of chromosome condensation factors or in the assembly of mitotic chromsomes. Expressed in testis, H2BFWT is present in sperm cells and may be essential to telomere function.

Supplier: Bioss

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.

Supplier: Bioss

Thyroid stimulating hormone, also known as thyrotropin, is secreted from cells in the anterior pituitary called thyrotrophs, finds its receptors on epithelial cells in the thyroid gland, and stimulates that gland to synthesize and release thyroid hormones. TSH is a glycoprotein hormone composed of two subunits which are non covalently bound to one another. The alpha subunit of TSH is also present in two other pituitary glycoprotein hormones, follicle stimulating hormone and luteinizing hormone, and, in primates, in the placental hormone chorionic gonadotropin. Each of these hormones also has a unique beta subunit, which provides receptor specificity. In other words, TSH is composed of alpha subunit bound to the TSH beta subunit, and TSH associates only with its own receptor. Free alpha and beta subunits have essentially no biological activity.