"Other Essentials"

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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.

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The homeobox protein, HESX1, which is also known as Rathke’s pouch homeobox, HANF, homeodomain transcription factor, and anterior-restricted homeobox protein is a transcription factor that belongs to the homeodomain family of DNA binding proteins. HESX1 is initially expressed in embryonic stem cells and the primitive forebrain, and is essential for normal development of the eyes and other anterior CNS structures, such as the hypothalamus, the pituitary gland and the olfactory bulbs. The homeobox gene Hesx1 is expressed in the anterior visceral endoderm (AVE), anterior axial mesendoderm (AME), and anterior neural ectoderm (ANE) during early embryogenesis. Mutations in the Hesx1 gene are associated with disorders that are comparable with septo-optic dysplasia (SOD). These disorders are characterized by hypoplasia of the optic nerve, various types of forebrain defects and pituitary hormone deficiencies, including hypothyroidism. Hesx1 also acts as a transcriptional repressor of reporter gene constructs in tissue culture assays.

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The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. STK33 (serine/threonine kinase 33) is a 514 amino acid protein that belongs to the CaMK (calcium/calmodulin dependent kinase) subfamily of structurally related serine/threonine kinases. Widely expressed at low levels with predominant expression in testis, lung, retina and fetal organs such as brain, heart and spinal cord, STK33 contains one protein kinase domain and functions as a Ser/Thr protein kinase with a possible role in spermatogenesis. The gene encoding STK33 lies within a region on chromosome 11 that has been associated with a variety of defects, including Long QT syndrome, T-cell leukemia, Beckwith-Wiedemann syndrome, Usher syndrome 1C and various other malignancies.

Supplier: Bioss

The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. STK33 (serine/threonine kinase 33) is a 514 amino acid protein that belongs to the CaMK (calcium/calmodulin dependent kinase) subfamily of structurally related serine/threonine kinases. Widely expressed at low levels with predominant expression in testis, lung, retina and fetal organs such as brain, heart and spinal cord, STK33 contains one protein kinase domain and functions as a Ser/Thr protein kinase with a possible role in spermatogenesis. The gene encoding STK33 lies within a region on chromosome 11 that has been associated with a variety of defects, including Long QT syndrome, T-cell leukemia, Beckwith-Wiedemann syndrome, Usher syndrome 1C and various other malignancies.

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MCM7 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that is 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 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 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumor suppressor protein RB1/RB.

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Metastasis suppressor protein in malignant melanomas and in some breast cancers. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. Kp-1 is a decapeptide derived from the primary translation product, isolated in conditioned medium of first trimester trophoblast. Kp-1, but not other kisspeptins, increased intracellular Ca(2+) levels in isolated first trimester trophoblasts. Kp-1 is a paracrine/endocrine regulator in fine-tuning trophoblast invasion generated by the trophoblast itself. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood.

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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: Bioss

The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. STK33 (serine/threonine kinase 33) is a 514 amino acid protein that belongs to the CaMK (calcium/calmodulin dependent kinase) subfamily of structurally related serine/threonine kinases. Widely expressed at low levels with predominant expression in testis, lung, retina and fetal organs such as brain, heart and spinal cord, STK33 contains one protein kinase domain and functions as a Ser/Thr protein kinase with a possible role in spermatogenesis. The gene encoding STK33 lies within a region on chromosome 11 that has been associated with a variety of defects, including Long QT syndrome, T-cell leukemia, Beckwith-Wiedemann syndrome, Usher syndrome 1C and various other malignancies.

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TIRP Antibody: TIRP is a member of the Toll/interleukin-1 receptor (TIR) family, a group of proteins that include the Toll-like receptors (TLRs). TLRs are signaling molecules that recognize different pathogen-associated molecular patterns (PAMPs) and serve as an important link between the innate and adaptive immune responses. TIRP, along with other molecules such as TRIF, MAL, and MyD88, serves as an adaptor protein that allows for the interaction and activation of the IL-1R-associated kinase (IRAK) family, the subsequent activation of TNF receptor associated factor (TRAF)-6, and ultimately the activation of NF-kappa B. Expression of TIRP appears to be essential for TLR4 signalling.

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DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

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Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. This protein is normally expressed in the dendritic cells, macrophages, microglia, eosinophils, fibroblasts, endothelial cells, and most tumour cells. IDO activity is associated with immunosuppression and immune attenuation. Several studies showed that IDO can contribute to immune escape when expressed directly in tumour cells or when expressed in immunosuppressive antigen presenting cells such as tolerogenic dendritic cells or tumour associated macrophages. IDO also is a promising therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterized by pathological immune suppression.

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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.

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TTYH1 Antibody: TTYH1 is a member of the tweety family of proteins, a family of chloride anion channels containing five transmembrane regions. TTYH1 is a Ca2+-independent, volume-sensitive large conductance chloride (Cl-) channel. TTYH1 is primarily expressed in neural tissue and upregulated in astrocytoma, glioma, and several other cancers. Recent experiments have shown that TTYH1 is an integral endoplasmic reticulum (ER) membrane protein involved in cell proliferation and is thought to play an essential role in embryonic cell growth, possibly through the Ca2+ storage/release process in ER membranes during early development.

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The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. Two transcript variants encoding distinct isoforms have been identified for this gene. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by one transcript.

Supplier: Bioss

The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. STK33 (serine/threonine kinase 33) is a 514 amino acid protein that belongs to the CaMK (calcium/calmodulin dependent kinase) subfamily of structurally related serine/threonine kinases. Widely expressed at low levels with predominant expression in testis, lung, retina and fetal organs such as brain, heart and spinal cord, STK33 contains one protein kinase domain and functions as a Ser/Thr protein kinase with a possible role in spermatogenesis. The gene encoding STK33 lies within a region on chromosome 11 that has been associated with a variety of defects, including Long QT syndrome, T-cell leukemia, Beckwith-Wiedemann syndrome, Usher syndrome 1C and various other malignancies.

Supplier: ProSci Inc.

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.