288 Results for: "Základny+exsikátor\\u016F"

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: ProSci Inc.

LAMTOR1 is a 161 amino acid membrane protein belonging to the LAMTOR family. It has been identified to interact with and recruit the four Rag GTPases (Rag A-D) to the surface of lysosomes. The mTORC1 kinase complex is a critical component in the regulation of cell growth. As part of the ragulator complex, LAMTOR1 recruits the Rag GTPases and the mTORC1 complex to lysosomes, a key step in activation of the TOR signaling cascade by amino acids. LAMTOR1 may be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes / lysosomes.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioworld Technology

Chemokines have been implicated in the regulation of stem/progenitor cell proliferation and movement. C-C chemokines myeloid progeni tor inhibitory factor-1 (MPIF)-1 and eotaxin-2 (also known as MPIF-2, CK b-6 or small inducible cytokine A24) both ma 1 * 100 µG

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: Bioss

Plays a role as negative regulator of myoblast differentiation, in part through effects on MTOR signaling. Has no detectable enzymatic activity.PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: ProSci Inc.

ULK1 Antibody: ULK1, also known as ATG1, is a key serine/threonine protein kinase probably acting at the most upstream step of autophagosome formation. Knockout of ULK1 results in a severe defect in the autophagy pathway. ULK1 is highly conserved among eukaryotes, and are the Unc-51-like kinases, ULK1 and ULK2 in mammals. ULK1 is ubiquitously expressed and involved in autophagy in response to starvation. It is the target of the TOR kinase signaling pathway that regulates autophagy through the control of phosphorylation status of ATG13. ULK1 also plays a role early in neuronal differentiation.

Supplier: Bioworld Technology

Originally isolated from osteoblastic cells, the TGFβ1-inducible early gene-1 (TIEG1) is a Krupel-like zinc finger transcription fac tor-encoding gene which regulates cellular growth and differentiation. TIEG1 is regulated as an early response gene b 1 * 100 µG

Supplier: Bioworld Technology

Chemokines have been implicated in the regulation of stem/progenitor cell proliferation and movement. C-C chemokines myeloid progeni tor inhibitory factor-1 (MPIF)-1 and eotaxin-2 (also known as MPIF-2, CK b-6 or small inducible cytokine A24) both ma 1 * 100 µG

Supplier: ProSci Inc.

PPAPDC3 Antibody: PPAPDC3, also known as nuclear envelope transmembrane protein 39 (NET39), was initially discovered in an in silico screen for secreted or membrane proteins. It is a member of the PAP2 superfamily of phosphatases and haloperoxidases. PPAPDC3 has recently been shown to act as a negative regulator of myoblast differentiation by diminishing the activity of the mammalian target of rapamycin TOR. PPAPDC3 is highly expressed in cardiac and skeletal muscle and becomes strongly upregulated during cultured myoblast differentiation tissues. Overexpression of PPAPDC3 in myoblasts repressed myogenesis while knockdown by RNA interference promoted differentiation indicating its part in the regulatory mechanism for myogenesis.

Supplier: ProSci Inc.

4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1/BP-1/PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13 kDa). Binding of eIF4EBP1 to eIF4E is reversible and is dependent on the phosphorylation status of eIF4EBP1. Non phosphorylated eIF4EBP1 will bind strongly to eIF4E while(24 kDa), the phosphorylated form will not. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating eIF4EBP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 64. Although, not all phosphorylation events equally block the eIF4EBP1-eIF4E interaction.

Supplier: ProSci Inc.

ATG3 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG3 (APG3) is a widely expressed conjugating enzyme for APG8 lipidation, an essential step for the initiation of autophagy. It functions as an E2-like enzyme during the initial stages of autophagosome formation by catalyzing the formation of the Atg8-phosphatidylethanolamine (Atg8-PE) conjugate, which is critical for autophagy.

Supplier: ProSci Inc.

4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1/BP-1/PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13 kDa). Binding of eIF4EBP1 to eIF4E is reversible and is dependent on the phosphorylation status of eIF4EBP1. Non phosphorylated eIF4EBP1 will bind strongly to eIF4E while(24 kDa), the phosphorylated form will not. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating eIF4EBP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 64. Although, not all phosphorylation events equally block the eIF4EBP1-eIF4E interaction.

Supplier: ProSci Inc.

ATG9A Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG9A, a multi-spanning membrane protein localizing to the Golgi apparatus and late endosomes, has been proposed to mediate membrane transport to generate autophagosomes. ATG9A has also been implicated as a regulator of STING (stimulator of interferon genes)-mediated innate immune response.

Supplier: ProSci Inc.

4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1/BP-1/PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13 kDa). Binding of eIF4EBP1 to eIF4E is reversible and is dependent on the phosphorylation status of eIF4EBP1. Non phosphorylated eIF4EBP1 will bind strongly to eIF4E while(24 kDa), the phosphorylated form will not. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating eIF4EBP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 64. Although, not all phosphorylation events equally block the eIF4EBP1-eIF4E interaction.

Supplier: ProSci Inc.

LAMP-2 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components and is negatively regulated by TOR (Target of rapamycin). LAMP-2, a highly glycosylated protein associated with the lysosome, has recently been shown to be important in autophagy as mice deficient in this protein failed to convert autophagic vacuoles into vacuoles leading to impaired degradation of long-lived proteins. This correlates with the finding that human LAMP-2 deficiency causing Danon's disease is associated with the accumulation of autophagic material in striated myocytes. LAMP-2 exists in multiple isoforms.

Supplier: ProSci Inc.

ATG2B Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. Another member of the autophagy family of proteins is ATG2B, one of two homologs of ATG2 that is essential for autophagosome formation and important for regulation of size and distribution of lipid droplets. Relatively high rates of ATG2B mutations were observed in gastric and colorectal carcinomas, suggesting that deregulating the autophagy process may contribute to cancer development.

Supplier: ProSci Inc.

ATG5 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG5, another member of the autophagy protein family, forms a conjugate with ATG12; this conjugate has a ubiquitin-protein ligase (E3)-like activity for protein lipidation in autophagy. This conjugate also associates with innate immune response proteins such as RIG-I and VISA (also known as IPS-1), inhibiting type I interferon production and permitting viral replication in host cells.

Supplier: ProSci Inc.

LAMP-1 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components and is negatively regulated by TOR (Target of rapamycin). A protein recently found to be involved in autophagy, LAMP-2, is a highly glycosylated protein associated with the lysosome. LAMP-1 shares much homology to LAMP-2 and is thought to have overlapping functions. Mice lacking LAMP-1 had very minor defects compared to those deficient in LAMP-2 expression. However, the loss of both proteins resulted in embryonic lethality, suggesting that each protein possesses some unique and necessary functions.

Supplier: ProSci Inc.

ATG5 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG5, another member of the autophagy protein family, forms a conjugate with ATG12; this conjugate has a ubiquitin-protein ligase (E3)-like activity for protein lipidation in autophagy. This conjugate also associates with innate immune response proteins such as RIG-I and VISA (also known as IPS-1), inhibiting type I interferon production and permitting viral replication in host cells.

Supplier: ProSci Inc.

PIST Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components and is negatively regulated by TOR (Target of rapamycin). PIST, a PDZ-containing protein, was discovered in a yeast two-hybrid system as a binding partner to Beclin-1, a Bcl-2-interacting protein homologous to the yeast autophagy gene apg6. Experiments with mutant PIST proteins lacking the PDZ domain showed that PIST interaction with Beclin-1 through its coiled-coil domain can modulate Beclin-1 activity and suggest that PIST interactions with other proteins through its PDZ domain may regulate the activity of PIST and Beclin-1.

Supplier: ProSci Inc.

PIST Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components and is negatively regulated by TOR (Target of rapamycin). PIST, a PDZ-containing protein, was discovered in a yeast two-hybrid system as a binding partner to Beclin-1, a Bcl-2-interacting protein homologous to the yeast autophagy gene apg6. Experiments with mutant PIST proteins lacking the PDZ domain showed that PIST interaction with Beclin-1 through its coiled-coil domain can modulate Beclin-1 activity and suggest that PIST interactions with other proteins through its PDZ domain may regulate the activity of PIST and Beclin-1.

Supplier: ProSci Inc.

APG7 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. Another member of the autophagy family of proteins is APG7 which was identified in yeast as a ubiquitin-E1-like enzyme; this function is conserved in the mammalian homolog. In mammalian cells, APG7 is essential for autophagy conjugation systems, autophagosome formation, starvation-induced bulk degradation of proteins and organelles. It has been suggested that caspase-8 may alter APG7 levels and thus the APG7 program of autophagic cell death.