"Other Essentials"

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

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

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

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

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

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.