"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: 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

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Supplier: Prosci

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Supplier: Prosci

NSA1 Antibody: The yeast nucleolar protein NOP7 is necessary for the maturation of 66S preribosomes and interacts with numerous other proteins. One such protein is an essential, conserved WD repeat protein, NOP seven-associated protein 1 (NSA1), that is also required for the yeast 66S ribosome assembly. NSA1 is also associated with the AAA ATPase Rix7, and release of NSA1 from a novel late nucleolar pre-60S requires the Rix7 function. NSA1 has also been found upregulated in mammalian cancer cells, suggesting it may also play a role in cell proliferation.

Supplier: Prosci

NSA1 Antibody: The yeast nucleolar protein NOP7 is necessary for the maturation of 66S preribosomes and interacts with numerous other proteins. One such protein is an essential, conserved WD repeat protein, NOP seven-associated protein 1 (NSA1), that is also required for the yeast 66S ribosome assembly. NSA1 is also associated with the AAA ATPase Rix7, and release of NSA1 from a novel late nucleolar pre-60S requires the Rix7 function. NSA1 has also been found upregulated in mammalian cancer cells, suggesting it may also play a role in cell proliferation.

Supplier: Bioss

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Supplier: Bioss

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Supplier: Bioss

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Supplier: Prosci

Estrogen Receptor is a major ligand-activated transcription factor belonging to the nuclear hormone receptor superfamily. Estrogen Receptor is composed of several domains important for hormone binding, DNA binding, and activation of transcription. The protein localizes to the nucleus where it may form a homodimer or a heterodimer with estrogen receptor 2. Estrogen and its receptors are essential for sexual development and reproductive function, but they also play a role in other tissues such as bone. Estrogen receptors are also involved in pathological processes including breast cancer, endometrial cancer, and osteoporosis. Alternative splicing results in several transcript variants, which differ in their 5' UTRs and use different promoters.

Supplier: Prosci

NSA1 Antibody: The yeast nucleolar protein NOP7 is necessary for the maturation of 66S preribosomes and interacts with numerous other proteins. One such protein is an essential, conserved WD repeat protein, NOP seven-associated protein 1 (NSA1), that is also required for the yeast 66S ribosome assembly. NSA1 is also associated with the AAA ATPase Rix7, and release of NSA1 from a novel late nucleolar pre-60S requires the Rix7 function. NSA1 has also been found upregulated in mammalian cancer cells, suggesting it may also play a role in cell proliferation.

Supplier: Bioss

Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.

Supplier: ACCUFORM MANUFACTURING, INC

Floor signs alert and remind those to practice social and physical distancing to prevent the spread of COVID-19, the Coronavirus. 

Supplier: Prosci

APH1 Antibody: APH1 was initially identified as a component of the Notch pathway in C. elegans. Along with nicastrin, PEN2, and presenilin-1 APH1 is an essential component of the gamma-secretase complex which cleave the amyloid precursor protein (APP) at what are known as the gamma- and epsilon-sites and can lead to the accumulation of the Amyloid beta peptide (Abeta) cleavage product that is associated with Alzheimer's disease. APH1 exists in at least three distinct isoforms with APH1a as the principal isoform present in the gamma-secretase complex. Mice deficient in this isoform, but not the other two, were lethal at E10.5, with impaired vascular and neural development observed.

Supplier: Proteintech

ADP-ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily, with 20kda protein size. ARFs bind and regulate GTP/GDP cycle by alternating between the active GTP-bound and inactive GDP-bound conformations. ARF family proteins are essential and ubiquitous in eukaryotes. Six highly conserved members of the family have been identified in mammalian cells. They function in vesicular traffic and actin remodelling and other bioprocesses in cells. ARF4 and ARF5 are class II ARFs. . This antibody can bind ARFs for the close sequences.

Supplier: Prosci

The protein encoded by the MCM6 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. The MCM complex consisting of this protein and MCM2, 4 and 7 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. The phosphorylation of the complex by CDC2 kinase reduces the helicase activity, suggesting a role in the regulation of DNA replication.