"Other Essentials"

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

IKK alpha Antibody: Nuclear factor kappa B (NF-kappa B) is a ubiquitous transcription factor and an essential mediator of gene expression during activation of immune and inflammatory responses. NF-kappa B mediates the expression of a great variety of genes in response to extracellular stimuli including IL-1, TNF alpha and bacteria product LPS. NF-kappa B is associated with I kappa B proteins in the cell cytoplasm, which inhibit NF-kappa B activity. The long-sought I kappa B kinase (IKK), which phosphorylates I kappa B, and mediates I kappa B degradation and NF-kappa B activation, was recently identified by several laboratories. IKK is a serine protein kinase, and the IKK complex contains alpha and beta subunits (IKK alpha and IKK beta ). IKK alpha and IKK beta interact with each other and both are essential for the NF-kappa B activation. IKK alpha specifically phosphorylates I kappa B-alpha. IKK alpha is expressed in a variety of human tissues.

Supplier: Thermo Scientific

This gene encodes a transcription factor that belongs to the homeobox gene family. Genes of this family are highly conserved among vertebrates and essential for vertebrate embryonic development. This gene has been implicated to play a role in fetal skin development and cutaneous regeneration. In mice, a similar gene was shown to exhibit temporal and spatial colinearity in the main body axis of the embryo, but was not expressed in the secondary axes, which suggests functions in body patterning along the axis. This gene and other HOXB genes form a gene cluster at chromosome the 17q21-22 region.

Supplier: Diagnostic Biosystems

SMADs are members of the MAD-related family of molecules. MAD-related proteins are a family of intracellular proteins that are essential components in the signaling pathways of the serine/threonine kinase receptors of the transforming growth factor beta superfamily. Alterations in the SMAD4 gene was primarily discovered in pancreatic cancer (duct adenocarcinoma) but occur in a variety of cancers such as colorectal cancer, gastric cancer, prostate cancer, melanomas, head and neck cancers and many others, though with higher frequencies in gastrointestinal tract cancers. Loss of SMAD4 expression in tumors has also been shown to affect cancer progression and therapy, such as reduced response to adjuvant chemotherapy.

Supplier: Diagnostic Biosystems

SMADs are members of the MAD-related family of molecules. MAD-related proteins are a family of intracellular proteins that are essential components in the signaling pathways of the serine/threonine kinase receptors of the transforming growth factor beta superfamily. Alterations in the SMAD4 gene was primarily discovered in pancreatic cancer (duct adenocarcinoma) but occur in a variety of cancers such as colorectal cancer, gastric cancer, prostate cancer, melanomas, head and neck cancers and many others, though with higher frequencies in gastrointestinal tract cancers. Loss of SMAD4 expression in tumors has also been shown to affect cancer progression and therapy, such as reduced response to adjuvant chemotherapy.

Supplier: Proteintech

The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions. The serine/threonine protein phosphatases (PP) are intimately involved in this process. Serine/threonine protein phosphatase X (PPX; also called protein phosphatase 4 (PP4)) are specifically associated with nuclear factor-kappa B (NF-kappa B) p50, c-Rel, and RelA, which are pleiotropic transcription factors that play central roles in the immune and inflammatory responses, as well as apoptosis. Overexpression of PPX stimulated the DNA-binding activity of c-Rel and activated NF-kappa B-mediated transcription. Although the mechanism by which PPX activates Rel/NF-kappa B-mediated transcription is unclear, PPX appeared to act on Rel/NF-kappa B proteins directly through augmentation of c-Rel activity. It is also possible that PPX may dephosphorylate and subsequently activate other c-Rel-associated transcription factors or other kinases regulating I kappaB (e.g. I kappa B kinases or MEKK1). These data suggest that PPX is an activator, but not an inhibitor, of c-Rel/NF-kappa B, which is in contrast to other protein phosphatases.

Supplier: Bioss

Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. RUVBL1 plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May be able to bind plasminogen at cell surface and enhance plasminogen activation.
Essential for cell proliferation.

Supplier: Prosci

Human sDLL-1 comprises the extracellular signaling domain of DLL1, a member of a structurally-related family of single-pass type I trans-membrane proteins that serve as ligands for Notch receptors. It is expressed in the heart and pancreas, and to a lesser extent in various other tissues. DLL-1 functions to specifically activate the Notch-1 and Notch-2 receptors. The Notch signaling pathway regulates endothelial-cell differentiation, proliferation and apoptosis, and is essential for the development, maintenance and remodeling of the vascular system. DLL-1 suppresses differentiation of hematopoietic progenitor cells into the B-cell lineage while promoting differentiation to T-cell and NK cell precursors. Recombinant human sDLL-1 is a 57.0-60.0 kDa glycoprotein containing 522 amino-acid residues.

Supplier: Proteintech

GEMIN5 also named as Gem associated protein 5 is a 1508 amino-acid protein, which belongs to the WD repeat gemin-5 family. The molecular weight of GEMIN5 is 168 kDa GEMIN5 is a component of SMN complex, which plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. GEMIN5 is identified as the factor that allows the SMN complex to distinguish snRNAs from other cellular RNAs for snRNP biogenesis. GEMIN5 is found in nucleoplasm, nuclear bodies and cytoplasm.

Supplier: Proteintech

Mitofusin-1 (MFN1) is a mediator of mitochondrial fusion. This protein and mitofusin 2 are homologs of the Drosophila protein fuzzy onion (Fzo). Mitofusins are large predicted GTPases located in outer mitochondrial membrane. They are essential for outer membrane fusion by interacting with each other to facilitate mitochondrial targeting. The mitofusins are the first known protein mediator of mitochondrial fusion, and mediate developmentally regulated post-meiotic fusion of mitochondria.Mfn1 is required on adjacent mitochondria to mediate fusion via interactions of a heptad repeat region that mediates oligomerization of the protein.

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: Prosci

ZNF687 Antibody: The zinc finger protein 687 (ZNF687) was initially identified as a translocation partner gene with RUNX1 in patients with acute myeloid leukemia (AML). Little is known of the function of the ZNF687 protein, but it has been shown to weakly interact with the Ring1/Rnf2 RING finger protein member of the Polycomb group of proteins, suggesting it may be involved in the chromatin-modifying complexes essential for embryonic development and stem cell renewal. Other evidence suggests that ZNF687 may be part of a transcriptional network that also includes ZNF592 and ZMYMD8.

Supplier: Bioss

This gene encodes an estrogen receptor, a ligand-activated transcription factor 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 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. [provided by RefSeq, Jul 2008]

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.