ASH2L (human recombinant) Reference: 10946-50 Recombinant protein expressed in E. coli with a SUMO tag • ASH2L is a component of various multisubunit protein complexes, including the large complex of proteins associated with the SET1 (MLL) family of lysine methyltransferases.
Caspase 3 blocking peptide Reference: GTX31698-PEP This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 1. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq, Jul 28]
RbBP5 (human recombinant) Reference: 10947-50 Source: Recombinant protein expressed in E. coli • RbBP5 is a ubiquitously expressed nuclear protein that contains WD40 repeat-like domains. RbBP5 binds directly to tumor suppressor retinoblastoma protein (RB) and regulates cell proliferation. RbBP5 is also an important component of the multi-subunit SET1 lysine methyltransferase protein complex, which includes MLL1.
Caspase 2 blocking peptide Reference: GTX31699-PEP This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Caspases mediate cellular apoptosis through the proteolytic cleavage of specific protein substrates. The encoded protein may function in stress-induced cell death pathways, cell cycle maintenance, and the suppression of tumorigenesis. Increased expression of this gene may play a role in neurodegenerative disorders including Alzheimer's disease, Huntington's disease and temporal lobe epilepsy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 211]
Core Histones (human) Reference: 11010-100 Source: Highly purified mixture of human core histones (H2A, H2B, H3, and H4) isolated via hydroxyapatite chromatography from HeLa S3 (human cervical adenocarcinoma) nuclear pellet
Caspase 5 blocking peptide Reference: GTX31700-PEP This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein; this process requires Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Aug 21]
BRD4 bromodomains 1 and 2 (human, recombinant, aa 49-460) Reference: 11052-100 Source: Recombinant human N-terminal GST-tagged BRD4 bromodomains 1 and 2 expressed in E. coli • Amino acids: 49-460 • MW: 73.4 kDa
Caspase 5 blocking peptide Reference: GTX31701-PEP This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein; this process requires Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Aug 21]
BRD4 bromodomain 2 (human, recombinant, GST-tagged) Reference: 11066-1 Source: Recombinant N-terminal GST-tagged BRD4 bromodomain 2 expressed in E. coli • Amino acids: 342-460 • MW: 40.6 kDa
Caspase 1 blocking peptide Reference: GTX31702-PEP This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Mar 212]
BRD4 bromodomain 2 (human, recombinant, GST-tagged) Reference: 11066-100 Source: Recombinant N-terminal GST-tagged BRD4 bromodomain 2 expressed in E. coli • Amino acids: 342-460 • MW: 40.6 kDa
Caspase 7 blocking peptide Reference: GTX31704-PEP This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The precursor of the encoded protein is cleaved by caspase 3 and 1, is activated upon cell death stimuli and induces apoptosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 212]