"Other Essentials"

Supplier: Bioss

Transforming Growth Factor (TGF) betas mediate many cell to cell interactions that occur during embryonic development. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule. The TGF beta polypeptides are multifunctional; capable of influencing cell proliferation, differentiation, and other functions in a wide range of cell types. Transformed, as well as nonneoplastic tissues, release transforming growth factors; and essentially all mammalian cells possess a specific TGF receptor. The multi modal nature of TGF beta is seen in its ability to stimulate or inhibit cellular proliferation. In general, cells of mesenchymal origin appear to be stimulated by TGF beta whereas cells of epithelial or neuroectodermal origin are inhibited by the peptide. TGF beta 1, TGF beta 2, and TGF beta 1.2 appear to be equivalent in biological activity, although there does appear to be differences in binding to certain types of receptors. TGF beta 2 is produced by many cell types and has been found in the highest concentration in porcine platelets and mammalian bone. Latent TGF beta 2 is the prominent isoform found in body fluids such as amniotic fluid, breast milk, and the aqueous and vitreous humor of the eye.

Supplier: Bioss

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p5 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).

Supplier: ProSci Inc.

CD63 functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli. [UniProt].

Supplier: Bioss

Transforming Growth Factor (TGF) betas mediate many cell to cell interactions that occur during embryonic development. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule. The TGF beta polypeptides are multifunctional; capable of influencing cell proliferation, differentiation, and other functions in a wide range of cell types. Transformed, as well as nonneoplastic tissues, release transforming growth factors; and essentially all mammalian cells possess a specific TGF receptor. The multi modal nature of TGF beta is seen in its ability to stimulate or inhibit cellular proliferation. In general, cells of mesenchymal origin appear to be stimulated by TGF beta whereas cells of epithelial or neuroectodermal origin are inhibited by the peptide. TGF beta 1, TGF beta 2, and TGF beta 1.2 appear to be equivalent in biological activity, although there does appear to be differences in binding to certain types of receptors. TGF beta 2 is produced by many cell types and has been found in the highest concentration in porcine platelets and mammalian bone. Latent TGF beta 2 is the prominent isoform found in body fluids such as amniotic fluid, breast milk, and the aqueous and vitreous humor of the eye.

Supplier: Bioss

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p5 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).

Supplier: Bioss

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p5 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).

Supplier: Bioss

Transforming Growth Factor (TGF) betas mediate many cell to cell interactions that occur during embryonic development. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesised as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule. The TGF beta polypeptides are multifunctional; capable of influencing cell proliferation, differentiation, and other functions in a wide range of cell types. Transformed, as well as nonneoplastic tissues, release transforming growth factors; and essentially all mammalian cells possess a specific TGF receptor. The multi modal nature of TGF beta is seen in its ability to stimulate or inhibit cellular proliferation. In general, cells of mesenchymal origin appear to be stimulated by TGF beta whereas cells of epithelial or neuroectodermal origin are inhibited by the peptide. TGF beta 1, TGF beta 2, and TGF beta 1.2 appear to be equivalent in biological activity, although there does appear to be differences in binding to certain types of receptors. TGF beta 2 is produced by many cell types and has been found in the highest concentration in porcine platelets and mammalian bone. Latent TGF beta 2 is the prominent isoform found in body fluids such as amniotic fluid, breast milk, and the aqueous and vitreous humor of the eye.

Supplier: Bioss

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).

Supplier: ProSci Inc.

Dact3 Antibody: The Wnt signaling cascade is a conserved process in multicellular animals that plays important roles during development and can contribute to cancer and other diseases. Many members of this pathway are also expressed in the postnatal tissues such as brain. One such protein is Dact3, a member of the Dact protein family that was initially identified through binding to Disheveled (Dvl), a cytoplasmic protein essential to Wnt signaling. Dact3 is expressed in the ventral region of maturing somites, limb bud and branchial arch mesenchyme, embryonic CNS, and the adult brain. Recent evidence shows that Dact3 acts as a negative regulator Wnt/beta-catenin signaling that is repressed at the transcriptional level in colorectal cancer and this repression is associated with bivalent histone modifications. This repression can be reversed by pharmacological agents that targets both histone methylation and deacetylation, suggesting that Dact3 may be a potential target for therapeutic treatment of this cancer. At least three isoforms of Dact3 are known to exist.

Supplier: ProSci Inc.

POLR3F Antibody: The human POLR3F is a component of RNA III polymerase. RNA polymerase III transcribes many essential, small, noncoding RNAs, including the 5S rRNAs and tRNAs. While most pol III-transcribed genes are found scattered throughout the linear chromosome maps or in multiple linear clusters, there is increasing evidence that many of these genes prefer to be spatially clustered, often at or near the nucleolus. This association could create an environment that fosters the coregulation of transcription by pol III with transcription of the large ribosomal RNA repeats by RNA polymerase I (pol I) within the nucleolus. Given the high number of pol III-transcribed genes in all eukaryotic genomes, the spatial organization of these genes is likely to affect a large portion of the other genes in a genome. POLR3F has also been recently identified as an HIV dependency factor (HDF), suggesting that POLR3F may be an important drug target in HIV treatment. At least two isoforms of POLR3F are known to exist.

Supplier: ProSci Inc.

PAK4 Antibody: The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first of which include PAK1, 2 and 3, and can be activated by Cdc42/Rac binding. Group 1 PAKs contain an autoinhibitory domain whose activity is regulated by Cdc42/Rac binding. The group 1 PAKs are known to be involved in cellular processes such as gene transcription, apoptosis, and cell morphology and motility. Much less is known about the second group, which includes PAK4, 5 and 6. These proteins are not activated by Cdc42/Rac binding. PAK4 was initially identified as a novel effector of Cdc42Hs. Co-expression of PAK4 and Cdc42Hs resulted in induction of filopodia and actin polymerization, showing that it is involved in cytoskeletal reorganization. Other experiments have shown PAK4 to be essential for embryonic viability and proper neuronal development. PAK4 has also been implicated in anchorage-independent growth of tumor cells and is required for activation of several cancer prosurvival pathways.

Supplier: Bioss

Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Plays a role in the inflammatory responses, both as a target and as a component of the NF-kappa-B signaling and regulates a subset of proinflammatory cytokines such as IL1B, MIP2, and TNF. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses.

Supplier: Bioss

Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration.

Supplier: ProSci Inc.

The Cell-division cycle protein 20 is an essential regulator of cell division that is encoded by the CDC20 gene in humans. To the best of current knowledge its most important function is to activate the anaphase promoting complex (APC/C), a large 11-13 subunit complex that initiates chromatid separation and entrance into anaphase. The APC/C-Cdc20 protein complex has two main downstream targets. Firstly, it targets securin for destruction, enabling the eventual destruction of cohesin and thus sister chromatid separation. It also targets S and M-phase (S/M) cyclins for destruction, which inactivates S/M cyclin-dependent kinases (Cdks) and allows the cell to exit from mitosis. A closely related protein, Cdc20homologue-1 (Cdh1) plays a complementary role in the cell cycle.

Cdc20 appears to act as a regulatory protein interacting with many other proteins at multiple points in the cell cycle. It is required for two microtubule-dependent processes: nuclear movement prior to anaphase, and chromosome separation. [Wiki].

Supplier: ProSci Inc.

TMEM38B Antibody: TMEM38A and TMEM38B are two recently identified trimeric intracellular cation (TRIC) channel subtypes. TMEM38B is expressed in most mammalian tissues, while TMEM38A is preferentially expressed in excitable tissues such as striated muscle and brain. Mice deficient in both TMEM38A and TMEM38B suffer embryonic cardiac failure; the cardiac myocytes display severe dysfunction in SR Ca2+ handling, weakened Ca2+ release, and reduced K+ permeability indicating that the TRIC cation channels are likely to act as counter-ion channels that function in synchronization with Ca2+ release from intracellular stores. Mice that were lacking only TMEM38B however, die shortly after birth due to respiratory failure and have lungs exhibiting severe histological defect and ultrastructural abnormalities in their alveolar type II epithelial cells, indicating that TMEM38B are essential for perinatal lung maturation. Other experiments have shown that TMEM38A and TMEM38B can act with junctophilin proteins to support efficient ryanodine receptor-mediated Ca2+ release in muscle cells.

Supplier: ProSci Inc.

Kit ligand (KITLG) is also known as stem cell factor (SCF), mast cell growth factor (MGF), steel factor (SF), which belongs to the SCF family, and is a widely expressed 28 - 40 kDa type I transmembrane glycoprotein. KITLG is the ligand for the receptor-type protein-tyrosine kinase KIT. SCF / MGF plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG / SCF binding can activate several signaling pathways. KITLG / SF Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG / SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG / SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG / SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1, 4, 5 - trisphosphate. KITLG / SCF acts synergistically with other cytokines, probably interleukins.