4-Amino-1-phenylpyrrolidin-2-one+hydrochloride
Catalog Number:
(10667-226)
Supplier:
Bioss
Description:
The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.
Catalog Number:
(76012-532)
Supplier:
Prosci
Description:
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia.
Catalog Number:
(10406-476)
Supplier:
Bioss
Description:
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq].
Catalog Number:
(10406-484)
Supplier:
Bioss
Description:
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq].
Catalog Number:
(10667-228)
Supplier:
Bioss
Description:
The death domain (DD) superfamily of proteins share one or more of the following domains: the DD, DED (death-effector domain), CARD (caspase-recruitment domain) and PYD (Pyrin domain). Each of these domains is characterized by a canonical death domain fold, which consists of a bundle of five or six antiparallel α-helices. As their names suggest, these domains play prominent roles in programmed cell death. ASC2 (apoptosis-associated speck-like protein containing a CARD 2), also known as Pyrin-only protein 1 or PADD-only protein 1, is an 89 amino acid member of the DD superfamily that contains one Pyrin domain. Localized to the cytoplasm, ASC2 interacts with ASC to modulate NF-κB and pro-caspase-1 regulation. ASC2 is predominantly expressed in monocytes, macrophages and granulocytes.
Supplier:
PeproTech, Inc.
Description:
FGF-acidic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors. Recombinant Human FGF-acidic is a 16.8 kDa protein consisting of 141 amino acid residues.
Catalog Number:
(10406-482)
Supplier:
Bioss
Description:
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq].
Catalog Number:
(10406-478)
Supplier:
Bioss
Description:
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq].
Catalog Number:
(10406-424)
Supplier:
Bioss
Description:
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family, which is a family of mitochondrial flavoenzymes involved in fatty acid and branched chain amino-acid metabolism. This protein is one of the four enzymes that catalyze the initial step of mitochondrial beta-oxidation of straight-chain fatty acid. Defects in this gene are the cause of long-chain acyl-CoA dehydrogenase (LCAD) deficiency, leading to nonketotic hypoglycemia. [provided by RefSeq].
Supplier:
PeproTech, Inc.
Description:
FGF-basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Human FGF-basic is a 16.4 kDa protein consisting of 146 amino acid residues.
Catalog Number:
(76011-496)
Supplier:
Prosci
Description:
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
Supplier:
PeproTech, Inc.
Description:
FGF-basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Rat FGF-basic is a 16.3 kDa protein consisting of 145 amino acid residues.
Supplier:
PeproTech, Inc.
Description:
FGF-basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Human FGF-basic is a 17.2 kDa protein consisting of 154 amino acid residues.
Catalog Number:
(10750-704)
Supplier:
Prosci
Description:
FRMPD4 Antibody: The FERM and PDZ domain containing (FRMPD) protein family consists of four proteins that contain a FERM (Four-point-one, erzin, radixin, moesin) domain and at least one PDZ (PSD-95/Discs large/Zonula-occuldens-1) domain. FRMPD4, also known as Preso, also contains another protein interaction domain termed WW (domain with two conserved Trp residues) at its amino terminus. It was identified through a yeast two-hybrid screen using the PDZ domain of PSD-95 as bait and is highly expressed in multiple regions of the brain and is enriched in the postsynaptic density (PSD) fractions. Overexpression of FRMPD4 in cultured hippocampal neurons significantly increased the linear density of dendritic spines without changing their length and width; conversely, knockdown experiments using RNAi caused a decrease in spine density, indicating FRMPD4 positively regulates dendritic spine density but not morphology. The decreased level of FRMPD4 also resulted in reduced levels of excitatory synaptic transmission, suggesting that FRMPD4 is required for maintenance of excitatory synaptic transmission.
Catalog Number:
(10671-956)
Supplier:
Bioss
Description:
Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.
Catalog Number:
(10667-942)
Supplier:
Bioss
Description:
Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.
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