You Searched For: mRNA

Catalog Number: (10397-786)

Supplier: Bioss

Description: Microtubule-associated proteins (MAPs) regulate microtubule stability and play critical roles in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP-light chain 3 beta (MAP-LC3 Beta) and MAP-light chain 3 alpha (MAP-LC3 alpha) are subunits of both MAP1A and MAP1B. MAP-LC3M Beta, a homolog of Apg8p, is essential for autophagy and associated to the autophagosome membranes after processing. Two forms of LC3 Beta, the cytosolic LC3-I and the membrane-bound LC3-II, are produced post-translationally. LC3-I is formed by the removal of the C-terminal 22 amino acids from newly synthesized LC3∫, followed by the conversion of a fraction of LC3-I into LC3-II. LC3 enhances fibronectin mRNA translation in ductus arteriosus cells through association with 60S ribosomes and binding to an AU-rich element in the 3’ untranslated region of fibronectin mRNA. This facilitates sorting of fibronectin mRNA onto rough endoplasmic reticulum and translation. MAP LC3 Beta may also be involved in formation of autophagosomal vacuoles. It is expressed primarily in heart, testis, brain and skeletal muscle.

Catalog Number: (10397-782)

Supplier: Bioss

Description: Microtubule-associated proteins (MAPs) regulate microtubule stability and play critical roles in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP-light chain 3 beta (MAP-LC3 Beta) and MAP-light chain 3 alpha (MAP-LC3 alpha) are subunits of both MAP1A and MAP1B. MAP-LC3M Beta, a homolog of Apg8p, is essential for autophagy and associated to the autophagosome membranes after processing. Two forms of LC3 Beta, the cytosolic LC3-I and the membrane-bound LC3-II, are produced post-translationally. LC3-I is formed by the removal of the C-terminal 22 amino acids from newly synthesized LC3∫, followed by the conversion of a fraction of LC3-I into LC3-II. LC3 enhances fibronectin mRNA translation in ductus arteriosus cells through association with 60S ribosomes and binding to an AU-rich element in the 3’ untranslated region of fibronectin mRNA. This facilitates sorting of fibronectin mRNA onto rough endoplasmic reticulum and translation. MAP LC3 Beta may also be involved in formation of autophagosomal vacuoles. It is expressed primarily in heart, testis, brain and skeletal muscle.

Catalog Number: (10097-194)

Supplier: Proteintech

Description: Exoribonuclease I (XRN1), also known as Sep1 or Rar5, is a 1,694-amino acid protein that functions as the major cytoplasmic 5 prime to 3 prime exoribonuclease and plays an important role in mRNA turnover. XRN1 may also function in the microtubular cytoskeleton as well as in DNA recombination and replication. XRN1 induces the expression of stress granules (SGs), cytoplasmic aggregates of stalled translational preinitiation complexes that accumulate during stress, and GW bodies/processing bodies (PBs), distinct cytoplasmic sites of mRNA degradation. There are several isoforms of XRN1 that are produced as a result of alternative splicing events.Loss of XRN1 markedly affects cell growth rates.This antibody is specific to the XRN1 protein.

Catalog Number: (10371-964)

Supplier: Bioss

Description: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.

Catalog Number: (10366-432)

Supplier: Bioss

Description: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA, HSF1, HSP27/HSPB1, KRT18, KRT2, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.

Catalog Number: (10371-970)

Supplier: Bioss

Description: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.

Catalog Number: (10366-434)

Supplier: Bioss

Description: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA, HSF1, HSP27/HSPB1, KRT18, KRT2, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.

Catalog Number: (10751-814)

Supplier: Prosci

Description: HEPACAM2 Antibody: HEPACAM2 (Hepatocyte cell adhesion molecule 2), a type I N-linked transmembrane glycoprotein, belongs to the immunoglobulin superfamily. The exact function of HEPACAM2 is currently unknown, but the related protein HEPACAM forms cishomodimers on the cell surface to regulate the cell adhesion and may inhibit cell growth through suppression of cell proliferation. HEPACAM and HEPACAM2 mRNA are differentially regulated in canine tumors, with HEPACAM2 mRNA showing increased levels in adenomas, but decreased levels in metastatic carcinomas compared to normal tissues, while HEPACAM protein levels decreased in adenomas. It is therefore likely that HEPACAM2 plays a different role than HEPACAM in the development and progression to tumors.

Catalog Number: (10402-744)

Supplier: Bioss

Description: Associates with the spliceosome late in the splicing pathway and may function in the second step of pre-mRNA splicing.

Catalog Number: (10388-590)

Supplier: Bioss

Description: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.

Catalog Number: (10388-594)

Supplier: Bioss

Description: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.

Catalog Number: (10751-048)

Supplier: Prosci

Description: YBX2 Antibody: Germ cell specific Y-box binding protein (YBX2), a germ-cell-specific member of the Y-box family of DNA-/RNA-binding proteins, is a major constituent of messenger ribonucleoprotein particles (mRNPs) and involved in the regulation of the stability and/or translation of germ cell mRNAs. It is proposed to function as a coactivator of transcription in the nucleus and to stabilize and store maternal and paternal mRNAs in the cytoplasm. YBX2 binds to the Y-box consensus promoter element and is expressed in oocytes and testicular germ cells in the stage of spermatogonia to spermatocyte. Recent studies show that deletion of YBX2 leads to the disruption of both spermatogenesis and oogenesis.

Catalog Number: (10665-924)

Supplier: Bioss

Description: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).

Catalog Number: (10665-922)

Supplier: Bioss

Description: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).

Catalog Number: (10665-904)

Supplier: Bioss

Description: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).

Catalog Number: (10108-122)

Supplier: Prosci

Description: As a RNA-binding protein, KHDRBS3 plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. KHDRBS3 may play a role as a negative regulator of cell growth. It inhibits cell proliferation and involved in splice site selection of vascular endothelial growth factor. It induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. RNA-binding abilities are down-regulated by tyrosine kinase PTK6. It also involved in post-transcriptional regulation of HIV-1 gene expression.