"Other Essentials"

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IL-2 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 which 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. Recombinant murine IL-2 is a 17.2 kDa protein, containing 149 amino acid residues. Recombinant rat IL-2 is a 15.3 kDa protein containing 134 amino acid residues. Recombinant human IL-2 is a 15.5 kDa protein, containing 134 amino acid residues including one intrachain disulfide bond.

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: 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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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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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.

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.

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.

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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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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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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.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

MCM7 encodes a protein that 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 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 tumorsuppressor protein RB1/RB.

Supplier: ProSci Inc.

WIPI2 Antibody: WD repeat proteins play a role in many essential biologic functions, regulating the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. WIPI2, also known as ATG18B or ATG21, is a human homolog to yeast ATG18 and contains three WD repeats and has a 7-bladed propeller structure with a conserved motif that facilitates its interaction with other proteins. It is recruited to early autophagosomal structures along with Atg16L and ULK1 and is required for the formation of LC3-positive autophagosomes. Along with the highly related WIPI1, WIPI2 is found at the plasma membrane in addition to autophagosomal membranes.

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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.