"Other Essentials"

Supplier: Bioss

Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression.

Supplier: Bioss

BIVM (for basic, immunoglobulin like variable motif containing) refers to a recently identified gene product that maps to human chromosome 13q32-q33 and is predicted to encode a 503 amino acid protein. BIVM shows ubiquitous expression in normal human tissue and the presence of a 5' CpG island suggests it is a housekeeping gene. BIVM is likely essential for some aspect of basic cellular function. BIVM is highly charged and localizes to the cytoplasm and nucleus where it may bind to either DNA or RNA or associate with other cellular proteins. Significant sequence homology exists with many organisms.

Supplier: Bioss

Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic genes expression.

Supplier: Bioss

Polyadenylation of mRNA precursors is a two-step reaction that requires multiple protein factors. The first step, endonucleolytic cleavage of polyadenylation substrates, requires CstF (cleavage stimulation factor), a heterotrimer that is composed of three distinct subunits. Heterotrimeric CstF recognizes GU- and U-rich sequences located downstream of the polyadenylation site on RNA. CstF-77 (cleavage stimulation factor, 77 kDa subunit), also known as CstF3, is one of the three subunits comprising CstF. It can exist as a homodimer and functions as the bridge, directly interacting with the other two CstF subunits, namely CstF-64 and CstF-50. CstF-77 is highly conserved among eukaryotes. It contains an Alpha-helical structure with 11 HAT (Half-a-TPR-containing) repeats and is essential for CstF assembly. In addition, CstF-77 is capable of interacting with CPSF1 and FCP1, other factors involved in polyadenylation.

Supplier: Bioss

Polyadenylation of mRNA precursors is a two-step reaction that requires multiple protein factors. The first step, endonucleolytic cleavage of polyadenylation substrates, requires CstF (cleavage stimulation factor), a heterotrimer that is composed of three distinct subunits. Heterotrimeric CstF recognizes GU- and U-rich sequences located downstream of the polyadenylation site on RNA. CstF-77 (cleavage stimulation factor, 77 kDa subunit), also known as CstF3, is one of the three subunits comprising CstF. It can exist as a homodimer and functions as the bridge, directly interacting with the other two CstF subunits, namely CstF-64 and CstF-50. CstF-77 is highly conserved among eukaryotes. It contains an Alpha-helical structure with 11 HAT (Half-a-TPR-containing) repeats and is essential for CstF assembly. In addition, CstF-77 is capable of interacting with CPSF1 and FCP1, other factors involved in polyadenylation.

Supplier: ProSci Inc.

This intronless gene encodes a member of the SOX (SRY-related HMG-box) family of transcription factors involved in the regulation of embryonic development and in the determination of the cell fate. The encoded protein may act as a transcriptional activator after forming a protein complex with other proteins. In mice, a similar protein regulates the gamma-crystallin genes and is essential for lens development.

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: Bioss

Polyadenylation of mRNA precursors is a two-step reaction that requires multiple protein factors. The first step, endonucleolytic cleavage of polyadenylation substrates, requires CstF (cleavage stimulation factor), a heterotrimer that is composed of three distinct subunits. Heterotrimeric CstF recognizes GU- and U-rich sequences located downstream of the polyadenylation site on RNA. CstF-77 (cleavage stimulation factor, 77 kDa subunit), also known as CstF3, is one of the three subunits comprising CstF. It can exist as a homodimer and functions as the bridge, directly interacting with the other two CstF subunits, namely CstF-64 and CstF-50. CstF-77 is highly conserved among eukaryotes. It contains an Alpha-helical structure with 11 HAT (Half-a-TPR-containing) repeats and is essential for CstF assembly. In addition, CstF-77 is capable of interacting with CPSF1 and FCP1, other factors involved in polyadenylation.

Supplier: ProSci Inc.

MCM8 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.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

BIVM (for basic, immunoglobulin like variable motif containing) refers to a recently identified gene product that maps to human chromosome 13q32-q33 and is predicted to encode a 503 amino acid protein. BIVM shows ubiquitous expression in normal human tissue and the presence of a 5' CpG island suggests it is a housekeeping gene. BIVM is likely essential for some aspect of basic cellular function. BIVM is highly charged and localizes to the cytoplasm and nucleus where it may bind to either DNA or RNA or associate with other cellular proteins. Significant sequence homology exists with many organisms.

Supplier: ProSci Inc.

The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria.The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Alternatively spliced transcript variants encoding different isoforms have been identified.

Supplier: ProSci Inc.

The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria.The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Alternatively spliced transcript variants encoding different isoforms have been identified.

Supplier: ProSci Inc.

Interleukin-2(IL-2) is an interleukin, a type of cytokine signaling molecule in the immune system，belongs to the IL-2 family. It is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes.

Supplier: ProSci Inc.

Ubiquitin-Conjugating Enzyme E2 B (UBE2B) belongs to the ubiquitin-conjugating enzyme family. UBE2B can catalyze the covalent attachment of ubiquitin to other proteins, and is essential for the multi-ubiquitination and degradation of N-end rule substrates. UBE2B is indispensability for postreplication repair of UV-damaged DNA and may be involved in neurite outgrowth.Additionally, UBE2B may have a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.