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Supplier: AVANTOR PERFORMANCE MATERIAL LLC
Description: J.T.Baker® Viral Inactivation Solution Ultrapure bioreagent is a highly effective, ready-to-use product, specifically developed for detergent-based viral inactivation in biopharmaceutical operations and plasma derived therapy processes. J.T.Baker® Viral Inactivation Solution is formulated with non-ionic detergent, that is readily biodegradable and alkylphenol ethoxylate free, addressing environmental concerns associated with REACH. This innovative solution is optimized to have low protein reactive impurities, low viscosity and compatibility with typical downstream processes. J.T.Baker® Viral Inactivation Solution Ultrapure bioreagent is available in a variety of sizes to support development to large scale commercial batches. Detail description provided in technical literature.

Environmentally Preferable

Supplier: AVANTOR PERFORMANCE MATERIAL LLC
Description: J.T.Baker® Viral Inactivation Solution Biotech Reagent is a highly effective, ready-to-use product, specifically developed for detergent-based viral inactivation in biopharmaceutical operations and plasma derived therapy processes. J.T.Baker® Viral Inactivation Solution is formulated with non-ionic detergent, that is readily biodegradable and alkylphenol ethoxylate free, addressing environmental concerns associated with REACH. This innovative solution is optimized to have low protein reactive impurities, low viscosity and compatibility with typical downstream processes. J.T.Baker® Viral Inactivation Solution Biotech Reagent is cGMP and available in a variety of sizes to support development to large scale commercial batches. Detail description provided in technical literature.

Environmentally Preferable

Catalog Number: (10489-446)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


Catalog Number: (10487-388)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


Catalog Number: (10664-682)
Supplier: Bioss
Description: RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.


Catalog Number: (10664-686)
Supplier: Bioss
Description: RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.


Catalog Number: (10487-392)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


Catalog Number: (10489-462)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


Catalog Number: (10489-460)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


Catalog Number: (10664-688)
Supplier: Bioss
Description: RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.


Catalog Number: (10664-690)
Supplier: Bioss
Description: RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.


Catalog Number: (10349-236)
Supplier: Bioss
Description: E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription (By similarity).


Catalog Number: (76109-598)
Supplier: Bioss
Description: RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.


Catalog Number: (10664-684)
Supplier: Bioss
Description: RSAD2 is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.


Catalog Number: (10489-458)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


Catalog Number: (10487-390)
Supplier: Bioss
Description: LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.


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