You Searched For: SILICO+

Supplier: New England Biolabs (NEB)

Description: Bst 2.0 WarmStart DNA Polymerase is an in silico designed homologue of Bacillus stearothermophilus DNA Polymerase I, Large Fragment (Bst DNA Polymerase, Large Fragment) with a reversibly-bound aptamer, which inhibits polymerase activity at temperatures below 45°C.

Supplier: New England Biolabs (NEB)

Description: WarmStart RTx Reverse Transcriptase is a unique in silico designed RNA-directed DNA polymerase coupled with a reversibly-bound aptamer that inhibits RTx activity below 40°C

Supplier: New England Biolabs (NEB)

Description: Bst 2.0 DNA Polymerase is an in silico designed homologue of Bacillus stearo thermophilus DNA Polymerase I, Large Fragment (Bst DNA Polymerase, Large Fragment)

Supplier: Hirschmann

Description: BIO-SILICO® stoppers are manufactured in a special process which have regular pores, thus making them ideal for the preparation and sterilization of culture media

Supplier: New England Biolabs (NEB)

Description: Bst 3.0 DNA Polymerase is an in silico designed homologue of Bacillus stearothermophilus DNA Polymerase I, Large Fragment engineered for improved isothermal amplification performance and increased reverse transcription activity

Catalog Number: (10802-758)

Supplier: Rockland Immunochemical

Description: The FCH and double SH3 domains protein 1 (FCHSD1, also known as NWK2) and the related protein FCHSD2 were initially identified in silico as distantly related proteins to FNBP1 and FNBP2. Both share the common domain structure consisting of FCH, FBH, two SH3 and C-terminal proline-rich domains. While little is known of the function of FCHSD1, the related protein NWK is an adaptor protein that is thought to regulate Rho activity downstream of Robo receptors, suggesting that FCHSD1 may be involved in synaptic morphology by regulating actin dynamics in presynaptic terminals.

Catalog Number: (75931-134)

Supplier: Rockland Immunochemical

Description: 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.

Catalog Number: (10750-744)

Supplier: Prosci

Description: 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.

Catalog Number: (75929-318)

Supplier: Rockland Immunochemical

Description: The jumonji domain containing 1C protein (JMJD1C) was initially discovered in silico, and later suggested to be a candidate gene for autism. Like the related proteins JMJD1A and JMJD1B, JMJD1C is a histone H3K9 demethylase implicated in the nuclear hormone receptor-based transcriptional regulation. JMJD1C mRNA is highly expressed in undifferentiated embryonic stem (ES) cells as well as pancreatic islet, diffuse-type gastric cancer, and other tissues and tumors. The JMJD1C gene promoter contain bHLH-, AP-1-, and POU5F1-binding sites, and as preferential expression of POU5F1 has been reported in ES cells, pancreatic islet, and diffuse-type gastric cancer, it has been suggested that POU5F1-mediated expression of JMJD1C reactivates previously silenced genes in ES cells and diffuse-type gastric cancer. At least three isoforms of JMJD1C are known to exist.

Catalog Number: (10751-436)

Supplier: Prosci

Description: FCHSD1 Antibody: The FCH and double SH3 domains protein 1 (FCHSD1, also known as NWK2) and the related protein FCHSD2 were initially identified in silico as distantly related proteins to FNBP1 and FNBP2. Both share the common domain structure consisting of FCH, FBH, two SH3 and C-terminal proline-rich domains. While little is known of the function of FCHSD1, the related protein NWK is an adaptor protein that is thought to regulate Rho activity downstream of Robo receptors, suggesting that FCHSD1 may be involved in synaptic morphology by regulating actin dynamics in presynaptic terminals.

Supplier: SILICO & CHEMICO PORCELAIN SE

Description: Pestles for Porcelain Mortars.

Catalog Number: (10668-818)

Supplier: Bioss

Description: PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration in vivo were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.

Catalog Number: (470148-884)

Supplier: SILICO & CHEMICO PORCELAIN SE

Description: For Microchemistry Experiments

Catalog Number: (10668-822)

Supplier: Bioss

Description: PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration in vivo were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.

Catalog Number: (76107-576)

Supplier: Bioss

Description: PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration <i>in vivo</i> were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.

Catalog Number: (10668-820)

Supplier: Bioss

Description: PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration in vivo were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.