2306 Results for: "small 200"

Supplier: Bioss

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Supplier: Bioss

Human papilloma viruses (HPVs) can be classified as either high risk or low risk according to their association with cancer. HPV16 and HPV18 are the most common of the high risk group while HPV6 and HPV11 are among the low risk types. Approximately 90% of cervical cancers contain HPV DNA of the high risk types. Mutational analysis have shown that the E6 and E7 genes of the high risk HPVs are necessary and sufficient for HPV transforming function. The specific interactions of the E6 and E7 proteins with p53 and pRB, respectively, correlate with HPV high and low risk classifications. The high risk HPV E7 proteins bind to pRB with a higher affinity than do the low risk HPV proteins, and only the high risk HPV E6 proteins form detectable complexes with p53 in vitro. Human papillomaviruses (HPV) are small DNA viruses which infect epithelia of the skin and mucosa. Over 90 types have been identified and they mostly cause a variety of benign lesions such as warts and verrucae. However, some subtypes, notably types 16 and 18, 31 and 33, have been confirmed as agents which cause cervical cancer. The E6 protein is a transcriptional transactivator. Binds double-stranded DNA. This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus).

Supplier: Bioss

p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

Supplier: Bioss

p21-activated kinases (PAKs) belong to the family of serine/threonine kinases involved in the control of various cellular processes, including the cell cycle, dynamics of the cytoskeleton, apoptosis, oncogenic transformation, and transcription. All PAK family members are characterized by the presence of p21-binding domain. p21-activated kinases are regulated by the small GTP-binding proteins Rac and Cdc42, and lipids, which stimulate autophosphorylation and phosphorylation of exogenous substrates. Serine (Ser-474) is the likely autophosphorylation site in the kinase domain of PAK4 in vivo. Phosphospecific directed against serine 474 detect activated PAK4 on the Golgi membrane when PAK4 is co-expressed with activated Cdc42. Current data strongly implicates PAK-4 in oncogenesis. PAK4 is frequently overexpressed in human tumor cell lines of various tissue origins. Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates the proto-oncogene RAF1 and stimulates its kinase activity. Promotes cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Phosphorylates CTNND1, probably to regulate cytoskeletal organization and cell morphology. Keeps microtubules stable through MARK2 inhibition and destabilizes the F-actin network leading to the disappearance of stress fibers and focal adhesions.

Supplier: Bioss

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

Supplier: Bioss

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Supplier: Bioss

Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes. GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis. GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability. Oxyntomodulin significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness. Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: Bioss

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Supplier: Bioss

In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.

Supplier: Bioss

In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.

Supplier: Bioss

In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.

Supplier: Bioss

In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.

Supplier: Bioss

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Proteintech

TPK1(Thiamin pyrophosphokinase 1) is also named as PP20(placental protein 20) and belongs to the thiamine pyrophosphokinase family. It is a cellular enzyme involved in the regulation of thiamine metabolism and catalyzes the conversion of thiamine, a form of vitamin B1, to thiamine pyrophosphate (TDP, or TPP). There is no difference in TPK1 expression in cultured fibroblasts from normal subjects or from patients with thiamine-responsive megaloblastic anemia. It can exsit as a dimer. Defects in TPK1 are the cause of thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5).

Supplier: Bioss

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.

Supplier: Bioss

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants.

Supplier: Bioss

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

Supplier: Bioss

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

Supplier: Bioss

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined. [provided by RefSeq]. Hsp27, also referred to as the Estrogen regulated 24K protein and HSP28, is one of several small heat shock proteins (HSP) produced by all organisms studied. Hsp27 synthesis is induced by elevated temperature, as well as estrogen in hormone responsive cells. This protein is involved in stress resistance and actin organization. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSP's and mammalian a-crystalline lens protein. Because of the estrogen responsive nature of Hsp27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. This work has led to the suggestion that Hsp27 may be a useful marker in classifying various hormone sensitive tumors.

Supplier: Bioss

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Supplier: Bioss

The protein encoded by this gene is a component of the multi-subunit protein complex EIF4F. This complex facilitates the recruitment of mRNA to the ribosome, which is a rate-limiting step during the initiation phase of protein synthesis. The recognition of the mRNA cap and the ATP-dependent unwinding of 5'-terminal secondary structure is catalyzed by factors in this complex. The subunit encoded by this gene is a large scaffolding protein that contains binding sites for other members of the EIF4F complex. A domain at its N-terminus can also interact with the poly(A)-binding protein, which may mediate the circularization of mRNA during translation. Alternative splicing results in multiple transcript variants, some of which are derived from alternative promoter usage. [provided by RefSeq].eIF4G1 (eukaryotic translation Initiation Factor 4 Gamma 1) is a component of the protein complex eIF-4 which is involved in the recognition of the mRNA cap ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of mRNA to the ribosome. eIF4G plays a critical role in protein expression and is at the center of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex which scans along the mRNA to the translation start codon. Human eIF4G contains three consecutive HEAT domains, as well as long unstructured regions involved in multiple protein-protein interactions. The interactions of eIF4G1 with other factors are largely unknown.

Supplier: Bioss

Human papilloma viruses (HPVs) can be classified as either high risk or low risk according to their association with cancer. HPV16 and HPV18 are the most common of the high risk group while HPV6 and HPV11 are among the low risk types. Approximately 90% of cervical cancers contain HPV DNA of the high risk types. Mutational analysis have shown that the E6 and E7 genes of the high risk HPVs are necessary and sufficient for HPV transforming function. The specific interactions of the E6 and E7 proteins with p53 and pRB, respectively, correlate with HPV high and low risk classifications. The high risk HPV E7 proteins bind to pRB with a higher affinity than do the low risk HPV proteins, and only the high risk HPV E6 proteins form detectable complexes with p53 in vitro. Human papillomaviruses (HPV) are small DNA viruses which infect epithelia of the skin and mucosa. Over 90 types have been identified and they mostly cause a variety of benign lesions such as warts and verrucae. However, some subtypes, notably types 16 and 18, 31 and 33, have been confirmed as agents which cause cervical cancer. The E6 protein is a transcriptional transactivator. Binds double-stranded DNA. This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus).

Supplier: Bioss

Human papilloma viruses (HPVs) can be classified as either high risk or low risk according to their association with cancer. HPV16 and HPV18 are the most common of the high risk group while HPV6 and HPV11 are among the low risk types. Approximately 90% of cervical cancers contain HPV DNA of the high risk types. Mutational analysis have shown that the E6 and E7 genes of the high risk HPVs are necessary and sufficient for HPV transforming function. The specific interactions of the E6 and E7 proteins with p53 and pRB, respectively, correlate with HPV high and low risk classifications. The high risk HPV E7 proteins bind to pRB with a higher affinity than do the low risk HPV proteins, and only the high risk HPV E6 proteins form detectable complexes with p53 in vitro. Human papillomaviruses (HPV) are small DNA viruses which infect epithelia of the skin and mucosa. Over 90 types have been identified and they mostly cause a variety of benign lesions such as warts and verrucae. However, some subtypes, notably types 16 and 18, 31 and 33, have been confirmed as agents which cause cervical cancer. The E6 protein is a transcriptional transactivator. Binds double-stranded DNA. This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus).

Supplier: Bioss

Human papilloma viruses (HPVs) can be classified as either high risk or low risk according to their association with cancer. HPV16 and HPV18 are the most common of the high risk group while HPV6 and HPV11 are among the low risk types. Approximately 90% of cervical cancers contain HPV DNA of the high risk types. Mutational analysis have shown that the E6 and E7 genes of the high risk HPVs are necessary and sufficient for HPV transforming function. The specific interactions of the E6 and E7 proteins with p53 and pRB, respectively, correlate with HPV high and low risk classifications. The high risk HPV E7 proteins bind to pRB with a higher affinity than do the low risk HPV proteins, and only the high risk HPV E6 proteins form detectable complexes with p53 in vitro. Human papillomaviruses (HPV) are small DNA viruses which infect epithelia of the skin and mucosa. Over 90 types have been identified and they mostly cause a variety of benign lesions such as warts and verrucae. However, some subtypes, notably types 16 and 18, 31 and 33, have been confirmed as agents which cause cervical cancer. The E6 protein is a transcriptional transactivator. Binds double-stranded DNA. This protein may be involved in the oncogenic potential of this virus (cervical neoplasia-associated virus).

Supplier: Bioss

Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier.

Supplier: Bioss

DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

Supplier: Bioss

Required for the function of light chain amino-acid transporters. Involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. Involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. Required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity LAT2 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with SLC7A5, plays an important role in transporting L-leucine from the circulating blood to the retina across the inner blood-retinal barrier.