"Other Essentials"

Supplier: Biowest

L-glutamine is an essential amino acid required by virtually all mammalian and insect cells grown in culture. It is a crucial component of many cell culture media and serves as a major energy source for cells in culture. L-glutamine is very stable as a dry powder and as a frozen solution. However, in liquid media or stock solutions, L-glutamine can degrade relatively rapidly. L-glutamine is also more labile in cell culture solution than other amino acids.

Supplier: JUSTRITE MANUFACTURING

These oily waste cans with galvanised steel body construction with durable powder-coat finish are essential when using solvent soaked cloths and wiping rags. Rags and cloths soaked with thinners, linseed oil, combustible adhesives and other flammable liquids present a serious fire risk when discarded improperly.

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

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

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: Enzo Life Sciences

Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins during development at the neuromuscular junction. Agrin, MuSK and Rapsyn are all essential components for AChR aggregation through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface, and induces AChR aggregation. The central region contains two O-linked glycosylation sites and a domain homologous to domain III of laminin. The N-terminal region anchors agrin to the extracellular matrix via other basal membrane components. This region also contains a protease inhibitor domain and glycosaminoglycan attachment sites, increasing the predicted MW from 200kDa to ~600kDa. The diagram shown indicates the domain structure and functional regions of agrin, as well as domains required for AChR aggregation and alpha-dystroglycan and heparin binding.  Various agrin isoforms are generated by alternative splicing at the X, Y and Z sites, and differ in the presence or absence of small inserts. The isoforms can determine the biological activity of agrin and their expression in specific tissues and stages of development. While no difference in functional activity has been detected between splicing variants at site X, insertion of a 4 aa peptide at site Y modestly increases agrins nAChR clustering activity. Insertion of an 8 aa peptide at splicing site Z increases the clustering activity of soluble rat agrin 10,000 fold.

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.