57711 Results for: "2,5-Dimethyl-1,5-hexanen-3-ol"

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Flexible pipetting platform for fully automated single to multichannel liquid handling.

Supplier: Prosci

RAD23A is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, as well as with ubiquitin protein ligase E6AP, and thus suggests that this protein may be involved in the ubiquitin mediated proteolytic pathway in cells.The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair (NER). This protein was shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair. This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, as well as with ubiquitin protein ligase E6AP, and thus suggests that this protein may be involved in the ubiquitin mediated proteolytic pathway in cells.

Supplier: Tonbo Biosciences

The C17.8 antibody is specific for the 40 kDa (p40) protein subunit shared by the cytokines IL-12 and IL-23. To form IL-12, p40 assembles with a separate 35 kDa protein known as p35, resulting in a 70 kDa functional cytokine. IL-12 is secreted by activated monocytes, macrophages, and dendritic cells, and has been shown to target naïve, resting CD4+ T cells to promote their proliferation and secretion of cytokines. IL-23 contains the p40 subunit in combination with a 19 kDa protein chain, p19; its primary source being activated dendritic cells and other antigen-presenting cells. IL-23 appears to target different cell types than IL-12, acting on memory CD4+ T cells to induce a strong proliferative response and contributing to the generation and expansion of Th17 cells. Like the cytokines themselves, the receptors for IL-12 and IL-23 share one subunit, as well as containing distinct cytokine-specific subunits.

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The blood genomicPrep Mini Spin Kit is designed for the rapid and reproducible isolation of high-quality genomic DNA from whole blood, buffy coat, bone marrow, and nucleated red blood cells.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Tonbo Biosciences

The PC61.5 antibody is specific for mouse CD25, a 55 kDa surface protein also known as the Interleukin-2 Receptor alpha chain, or IL-2R alpha. CD25 may bind IL-2 by itself, although with low affinity and without induction of cell signaling. CD25 is also expressed within a high-affinity complex, along with the IL-2R beta chain (CD122) and the common gamma chain (CD132), to form a signaling receptor complex. Expression of CD25 varies during developmental stages of T and B cells, is induced on activated mature T and B cells, and is present on subsets of dendritic cells. CD25 signaling as part of the IL-2 receptor complex triggers T cell activation and proliferation, as well as modulating the differentiation and function of Th17 cells, T regulatory (Treg) cells, and dendritic cells. The PC61.5 antibody is used as a marker for T cells, B cells and dendritic cell subsets. Expression of CD25, CD4 and the transcription factor Foxp3 is regarded as a phenotypic signature for Treg cells. As such, this antibody is widely used to distinguish Treg cells from na�ve or conventional T cells which are CD25-. This clone has also been reported for depletion of Treg cells in vivo (use format suitable for functional assays).

Supplier: Prosci

PPFIBP1 is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. It has been proposed that liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR family of tyrosine phosphatases. This protein was found to interact with S100A4, a calcium-binding protein related to tumor invasiveness and metastasis.The protein encoded by this gene is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. It has been proposed that liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR family of tyrosine phosphatases. This protein was found to interact with S100A4, a calcium-binding protein related to tumor invasiveness and metastasis. In vitro experiment demonstrated that the interaction inhibited the phosphorylation of this protein by protein kinase C and protein kinase CK2. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier: Prosci

UGT1A1 is a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. The preferred substrate of this enzyme is bilirubin, although it also has moderate activity with simple phenols, flavones, and C18 steroids.This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The preferred substrate of this enzyme is bilirubin, although it also has moderate activity with simple phenols, flavones, and C18 steroids. Mutations in this gene result in Crigler-Najjar syndromes types I and II and in Gilbert syndrome.

Supplier: Prosci

TSG101 belongs to a group of apparently inactive homologs of ubiquitin-conjugating enzymes. TSG101 contains a coiled-coil domain that interacts with stathmin, a cytosolic phosphoprotein implicated in tumorigenesis. TSG101 may play a role in cell growth and differentiation and act as a negative growth regulator. In vitro steady-state expression of TSG101 appears to be important for maintenance of genomic stability and cell cycle regulation. Mutations and alternative splicing in TSG101 gene occur in high frequency in breast cancer. The protein encoded by this gene belongs to a group of apparently inactive homologs of ubiquitin-conjugating enzymes. The gene product contains a coiled-coil domain that interacts with stathmin, a cytosolic phosphoprotein implicated in tumorigenesis. The protein may play a role in cell growth and differentiation and act as a negative growth regulator. In vitro steady-state expression of this tumor susceptibility gene appears to be important for maintenance of genomic stability and cell cycle regulation. Mutations and alternative splicing in this gene occur in high frequency in breast cancer and suggest that defects occur during breast cancer tumorigenesis and/or progression.

Supplier: Rockland Immunochemical

KLF4 belong to the Kruppel like factors/Zinc fingers C2H2-type family. This gene encodes a protein that belongs to the Kruppel family of transcription factors. KLF4 can act both as activator and as repressor. It can bind the 5-CACCC-3 core sequence, the promoter region of its own gene, and can activate its own transcription. KLF4 regulates the expression of key transcription factors during embryonic development, playing an important role in maintaining embryonic stem cells, and in preventing their differentiation. This protein is required for normal development of the barrier function of skin postnatal, maintenance of the ocular surface, function in skeletal and kidney development, and thought to control the G1-to-S transition of the cell cycle following DNA damage by mediating the tumor suppressor gene p53. KLF4 may be associated with diseases such as Venous Hemangioma, Skin Squamous Cell Carcinoma, and pediatric lymphoma. Anti-KLF4 Antibody is useful for researchers interested in Peptide hormone metabolism, Stem Cell Differentiation Pathway Research, Wnt/Notch Pathway Research, and Cancer Research.

Supplier: Celestron International

StarSense Explorer is ideal for beginners thanks to the app’s user-friendly interface and detailed tutorials.

Supplier: Rockland Immunochemical

HbS antibodies detect the E6V mutant in the hemoglobin beta subunit. Functional adult hemoglobin (Hb) is a hetero tetramer composed of 2 alpha and 2 beta subunits (α2β2). Common isoform variants of hemoglobin include HbA, HbS, HbC, HbF, and HbA2. Hemoglobin S is the predominant hemoglobin in people with sickle cell disease. The alpha chain is normal. The disease-producing mutation exists in the beta chain, giving the molecule the structure, α2βS2. People who have one sickle mutant gene and one normal beta gene have sickle cell trait which is benign. Globin gene mutations affect the structure and expression levels of Hb. Sickle cell disease and the more benign sickle cell trait are observed in more than 100 million people globally. Perhaps the most significant mutation is the E6V in the beta subunit and the cause of SCD, but other relevant isoforms of Hb are observed. HbS antibody does not react to other forms of Hb. This antibody is ideal for investigators involved in Cardiovascular and developmental biology research.

Supplier: Labconco

Designed for the needs of histologists and pathologists, these workstations rid the lab of dangerous organic solvent fumes, such as formaldehyde and xylene, and restore clean air

Supplier: Prosci

The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. ZP2 is a structural component of the zona pellucida and functions in secondary binding and penetration of acrosome-reacted spermatozoa. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a consensus furin cleavage site, and a C-terminal transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies.The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The protein encoded by this gene is a structural component of the zona pellucida and functions in secondary binding and penetration of acrosome-reacted spermatozoa. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a consensus furin cleavage site, and a C-terminal transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies.

Supplier: Prosci

Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is a 28S subunit protein that belongs to the ribosomal protein S15P family. The protein is more than two times the size of its E. coli counterpart, with the 12S rRNA binding sites conserved. Between human and mouse, the protein is the least conserved among small subunit ribosomal proteins.Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S15P family. The encoded protein is more than two times the size of its E. coli counterpart, with the 12S rRNA binding sites conserved. Between human and mouse, the encoded protein is the least conserved among small subunit ribosomal proteins. Pseudogenes corresponding to this gene are found on chromosomes 15q and 19q.

Supplier: Prosci

RBMS3 is a member of a small family of proteins which bind single stranded DNA/RNA. These proteins are characterized by the presence of two sets of ribonucleoprotein consensus sequence (RNP-CS) that contain conserved motifs, RNP1 and RNP2, originally described in RNA binding proteins, and required for DNA binding. These proteins have been implicated in such diverse functions as DNA replication, gene transcription, cell cycle progression and apoptosis.The protein encoded by this gene is a member of a small family of proteins which bind single stranded DNA/RNA. These proteins are characterized by the presence of two sets of ribonucleoprotein consensus sequence (RNP-CS) that contain conserved motifs, RNP1 and RNP2, originally described in RNA binding proteins, and required for DNA binding. These proteins have been implicated in such diverse functions as DNA replication, gene transcription, cell cycle progression and apoptosis. The encoded protein was isolated by virtue of its binding to an upstream element of the alpha2 (I) collagen promoter. The observation that this protein localizes mostly in the cytoplasm suggests that it may be involved in a cytoplasmic function such as controlling RNA metabolism, rather than transcription. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Supplier: Prosci

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. RPS14 is a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S11P family of ribosomal proteins. It is located in the cytoplasm. In Chinese hamster ovary cells, mutations in this gene can lead to resistance to emetine, a protein synthesis inhibitor.Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S11P family of ribosomal proteins. It is located in the cytoplasm. Transcript variants utilizing alternative transcription initiation sites have been described in the literature. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. In Chinese hamster ovary cells, mutations in this gene can lead to resistance to emetine, a protein synthesis inhibitor. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.

Supplier: Prosci

HNRPUL1 is a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important role in nucleocytoplasmic RNA transport, and its function is modulated by E1B-55kDa in adenovirus-infected cells.This gene encodes a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important role in nucleocytoplasmic RNA transport, and its function is modulated by E1B-55kDa in adenovirus-infected cells. Four transcript variants encoding different isoforms have been found for this gene. Another variant has also been found, but its full-length nature has not been determined.This gene encodes a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important role in nucleocytoplasmic RNA transport, and its function is modulated by E1B-55kDa in adenovirus-infected cells. Four transcript variants encoding different isoforms have been found for this gene. Another variant has also been found, but its full-length nature has not been determined.

Supplier: Prosci

GNB1L is a G-protein beta-subunit-like polypeptide which is a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 6 WD repeats and is highly expressed in the heart. Therefore, this gene may contribute to the etiology of those disorders.This gene encodes a G-protein beta-subunit-like polypeptide which is a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 6 WD repeats and is highly expressed in the heart. The gene maps to the region on chromosome 22q11, which is deleted in DiGeorge syndrome, trisomic in derivative 22 syndrome and tetrasomic in cat-eye syndrome. Therefore, this gene may contribute to the etiology of those disorders.

Supplier: Biosensis

The Biosensis Mature BDNF/proBDNF Combo RapidTM enzyme-linked immunosorbent assay (ELISA) Kit combines individual, but complementary ELISA kits for the two most important BDNF isoforms: Mature BDNF (BEK-2211) and full-length proBDNF (BEK-2237).

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di-Sodium L(+)-tartrate dihydrate 99.0-101.0%, crystals, BAKER ANALYZED® ACS suitable for standardization of Karl Fischer reagents, J.T.Baker®

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WNT proteins are secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. WNT16 contains two transcript variants diverging at the 5' termini. These two variants are proposed to be the products of separate promoters and not to be splice variants from a single promoter. They are differentially expressed in normal tissues, one of which (variant 2) is expressed at significant levels only in the pancreas, whereas another one (variant 1) is expressed more ubiquitously with highest levels in adult kidney, placenta, brain, heart, and spleen.The WNT gene family consists of structurally related genes which encode secreted signaling proteins. These proteins have been implicated in oncogenesis and in several developmental processes, including regulation of cell fate and patterning during embryogenesis. This gene is a member of the WNT gene family. It contains two transcript variants diverging at the 5' termini. These two variants are proposed to be the products of separate promoters and not to be splice variants from a single promoter. They are differentially expressed in normal tissues, one of which (variant 2) is expressed at significant levels only in the pancreas, whereas another one (variant 1) is expressed more ubiquitously with highest levels in adult kidney, placenta, brain, heart, and spleen.

Supplier: Prosci

FBXO25 is a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein belongs to the Fbxs class. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Supplier: Labconco

These enclosures provide practical, economical protection of operator and environment for applications that generate fine dusts or aerosols but do not provide product protection

Supplier: Celestron International

StarSense Explorer is ideal for beginners thanks to the app’s user-friendly interface and detailed tutorials.

Supplier: IMPLEN, INC. CA

Implen has become the leading expert for innovative, high-quality spectroscopy instruments and the NanoPhotometer® is trusted by thousands of researchers worldwide.

Supplier: Prosci

Three classes of protein carboxyl methyltransferases, distinguished by their methyl-acceptor substrate specificity, have been found in prokaryotic and eukaryotic cells. The type II enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the free carboxyl groups of D-aspartyl and L-isoaspartyl residues. These methyl-accepting residues result from the spontaneous deamidation, isomerization, and racemization of normal L-aspartyl and L-asparaginyl residues and represent sites of covalent damage to aging proteins PCMT1 (EC 2.1.1.77) is a protein repair enzyme that initiates the conversion of abnormal D-aspartyl and L-isoaspartyl residues to the normal L-aspartyl form.Three classes of protein carboxyl methyltransferases, distinguished by their methyl-acceptor substrate specificity, have been found in prokaryotic and eukaryotic cells. The type II enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the free carboxyl groups of D-aspartyl and L-isoaspartyl residues. These methyl-accepting residues result from the spontaneous deamidation, isomerization, and racemization of normal L-aspartyl and L-asparaginyl residues and represent sites of covalent damage to aging proteins PCMT1 (EC 2.1.1.77) is a protein repair enzyme that initiates the conversion of abnormal D-aspartyl and L-isoaspartyl residues to the normal L-aspartyl form.[supplied by OMIM]. 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.

Supplier: Prosci

DMAP1 is a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.This gene encodes a subunit of several, distinct complexes involved in the repression or activation of transcription. The encoded protein can independently repress transcription and is targeted to replication foci throughout S phase by interacting directly with the N-terminus of DNA methyltransferase 1. During late S phase, histone deacetylase 2 is added to this complex, providing a means to deacetylate histones in transcriptionally inactive heterochromatin following replication. The encoded protein is also a component of the nucleosome acetyltransferase of H4 complex and interacts with the transcriptional corepressor tumor susceptibility gene 101 and the pro-apoptotic death-associated protein 6, among others. Alternatively spliced transcript variants encoding the same protein have been described.

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Prosci

The developmentally regulated expression of the globin genes depends on upstream regulatory elements termed locus control regions (LCRs). LCRs are associated with powerful enhancer activity that is mediated by the transcription factor NFE2. NFE2 recognition sites are also present in the gene promoters of 2 heme biosynthetic enzymes, PBGD and FECH. NFE2 DNA-binding activity consists of a heterodimer containing an 18-kD Maf protein (MafF, MafG, or MafK) and p45. Both subunits are members of the activator protein-1 superfamily of bZIP proteins. Maf homodimers suppress transcription at NFE2 sites.The developmentally regulated expression of the globin genes depends on upstream regulatory elements termed locus control regions (LCRs). LCRs are associated with powerful enhancer activity that is mediated by the transcription factor NFE2 (nuclear factor erythroid-2). NFE2 recognition sites are also present in the gene promoters of 2 heme biosynthetic enzymes, porphobilinogen deaminase (PBGD; MIM 176000) and ferrochelatase (FECH; MIM 177000). NFE2 DNA-binding activity consists of a heterodimer containing an 18-kD Maf protein (MafF, MafG (MIM 602020), or MafK) and p45 (MIM 601490). Both subunits are members of the activator protein-1 superfamily of basic leucine zipper (bZIP) proteins (see MIM 165160). Maf homodimers suppress transcription at NFE2 sites.[supplied by OMIM].