5596 Results for: "Z-Asp-2,6-dichlorobenzoyloxymethylketone"

Supplier: Bachem Americas

PG 97-269 is a selective high affinity VPAC1 receptor antagonist with negligible affinity for the PACAP type I receptor. The Ki values were 15 +/- 5 nM for the rat and 2 +/- 1 nM for the human VPAC1 receptors. PG 97-269 may be useful for the evaluation of the physiological role of VIP in rat and human tissues.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Supplier: Bioss

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of intracellular compartments of eukaryotic cells. V-ATPase dependent acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is one of three V1 domain G subunit proteins. This gene had previous gene symbols of ATP6G and ATP6G2. Alternatively spliced transcript variants encoding different isoforms have been described. Read-through transcription also exists between this gene and the downstream DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B (DDX39B) gene. (provided by RefSeq, Feb 2011).

Supplier: Prosci

DDX3 Antibody: DDX3 contains all of the motifs of the DEAD-box family of RNA helicases, including the Asp-Glu-Ala-Asp sequence that gives the protein family its name and distinguishes it from other RNA helicases. DDX3 is localized to the X chromosome and has a highly conserved functional homolog (DBY) on the Y chromosome. DDX3 is thought to be involved in RNA splicing, RNA transport, and translation initiation. It has also been shown to be involved in cell growth control and is deregulated in hepatitis virus-associated hepatocellular carcinoma. Recent experiments suppressing DDX3 expression blocked HIV-1 RNA export from the nucleus, suggesting that DDX3 functions as a shuttling protein that transports the HIV-1 protein Rev and its cofactor CRM1 from the nucleus to the cytoplasm.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Supplier: Bachem Americas

The sequences given for angiotensin I (H-1680) and II (H-1705) correspond to the sequences of human, horse, sheep, pig, mouse, and rat angiotensins I and II.

Supplier: Bachem Americas

GPenGRGDSPCA (cRGD), a cyclic RGD peptide has been used in the study of vascular wound response. GPenGRGDSPCA caused vasodilation when applied to isolated rat cremaster arterioles. The vasodilation is dependent on interaction of the soluble cRGD sequence with the αvβ3 integrin expressed by smooth muscle cells in the arteriolar wall.

Supplier: Biosensis

The Myc tag contains the amino acids Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu (E-Q-K-L-I-S-E-E-D-L) corresponding to amino acids 410-419 of human Myc. This tag is widely used for monitoring expression of recombinant proteins in bacteria, insect and mammalian cells.

Supplier: Bioss

DCTN6 belongs to the pointed end complex of the dynactin shoulder complex tpgether with the DCTN4, DCTN5 and DCTN6 subunits and ACTR10. DCTN6 contains an RGD (Arg-Gly-Asp) motif in the N terminal region, which confers adhesive properties to macromolecular proteins like fibronectin. The exact function of this gene is not known.

Supplier: Bioss

DCTN6 belongs to the pointed end complex of the dynactin shoulder complex tpgether with the DCTN4, DCTN5 and DCTN6 subunits and ACTR10. DCTN6 contains an RGD (Arg-Gly-Asp) motif in the N terminal region, which confers adhesive properties to macromolecular proteins like fibronectin. The exact function of this gene is not known.

Supplier: Thermo Scientific Chemicals

Powder

Supplier: Bioss

Endoplasmic reticulum Marker. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble endoplasmic reticulum (ER) resident proteins and some membrane proteins. 78 and 94 kDa glucose regulated proteins (GRP 78) and GRP 94 respectively and protein disulfide isomerase (PDI) all share the C-terminal KDEL sequence. The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Supplier: Bioss

DCTN6 belongs to the pointed end complex of the dynactin shoulder complex tpgether with the DCTN4, DCTN5 and DCTN6 subunits and ACTR10. DCTN6 contains an RGD (Arg-Gly-Asp) motif in the N terminal region, which confers adhesive properties to macromolecular proteins like fibronectin. The exact function of this gene is not known.

Supplier: Biosensis

The Myc tag contains the amino acids Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu (E-Q-K-L-I-S-E-E-D-L) corresponding to amino acids 410-419 of human Myc. This tag is widely used for monitoring expression of recombinant proteins in bacteria, insect and mammalian cells.

Supplier: Bioss

DCTN6 belongs to the pointed end complex of the dynactin shoulder complex tpgether with the DCTN4, DCTN5 and DCTN6 subunits and ACTR10. DCTN6 contains an RGD (Arg-Gly-Asp) motif in the N terminal region, which confers adhesive properties to macromolecular proteins like fibronectin. The exact function of this gene is not known.

Supplier: Prosci

WDR3 is a nuclear protein containing 10 WD repeats. WD repeats are approximately 30- to 40-amino acid domains containing several conserved residues, which usually include a trp-asp at the C-terminal end. Proteins belonging to the WD repeat family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation.This gene encodes a nuclear protein containing 10 WD repeats. WD repeats are approximately 30- to 40-amino acid domains containing several conserved residues, which usually include a trp-asp at the C-terminal end. Proteins belonging to the WD repeat family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: Bioss

Endoplasmic reticulum Marker. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble endoplasmic reticulum (ER) resident proteins and some membrane proteins. 78 and 94 kDa glucose regulated proteins (GRP 78) and GRP 94 respectively and protein disulfide isomerase (PDI) all share the C-terminal KDEL sequence. The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Supplier: Prosci

NAT6 belongs to the acetyltransferase family. It contains 1 N-acetyltransferase domain. NAT6 seems to be involved in N-acetylation. Acts on peptides with a N-terminal Met followed by Asp/Glu/Asn. It may act as a tumor suppressor. Defects in NAT6 are found in non-small cell lung cancer (NSCLC) cell lines.

Supplier: MilliporeSigma

A potent, cell-permeable, and irreversible inhibitor of caspase-1 (ICE) and caspase-4.

Supplier: Thermo Scientific

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp and a protein kinase C-activating compound, mezerein . Irreversible reprogramming of melanomas can be achieved by treatment with both these agents; treatment with either agent alone only achieves reversible differentiation.

Supplier: Thermo Scientific Chemicals

Molecular Formula: C35H41N5O12
Formula Weight: 723.72
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White to off-white
MDL No.: MFCD01631266

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: Prosci

WDR13 is a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. WDR13 gene is widely expressed in various tissues, and located in chromosome X. The function of this gene has not been determined.This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This gene is widely expressed in various tissues, and located in chromosome X. The function of this gene has not been determined.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: TCI America

CAS Number: 71989-14-5
MDL Number: MFCD00037131
Molecular Formula: C23H25NO6
Molecular Weight: 411.45
Purity/Analysis Method: >98.0% (HPLC,T)
Form: Crystal
Melting point (°C): 150
Specific rotation [a]20/D: -25 deg (C=1, DMF)