72794 Results for: "4-[(2-ethlbutanol)amino]benzoic acid"

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. pNL2.1[Nluc/Hygro] and pNL2.2[NlucP/Hygro] Vectors are used for cloning putative promoters; select for stable cell lines using hygromycin.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Biosensis

BDNF belongs to the neurotrophin family and regulates the survival and differentiation of neurons during development. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. FUNCTION: Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. POst translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family.

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a small enzyme (19.1kDa) engineered for optimal performance as a luminescent reporter. pNL2.1[Nluc/Hygro] and pNL2.2[NlucP/Hygro] Vectors are used for cloning putative promoters; select for stable cell lines using hygromycin.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: RSP AMINO ACIDS, LLC MS

FMOC-L-SER(O-ALLYL)-OH 1G

Supplier: Promega Corporation

NanoLuc (Nluc) luciferase is a 19.1kDa luminescent reporter enzyme that is about 100-fold brighter than either firefly or Renilla luciferase. Use the pNL3.2.NF-κB-RE[NlucP/NF-κB-RE/Hygro] Vector to measure changes in the levels of NF-kappaB in cells.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Promega Corporation

The pNL1.3[secNluc], pNL3.3[secNluc/minP], pNL2.3[secNluc/Hygro] and pNL1.3.CMV[secNluc/CMV] Vectors offer a secreted small luciferase reporter in various promoter-driven or promoterless configurations for expression in mammalian cells.

Supplier: Biosensis

FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer composed of two large adaptins (gamma1/AP1G1 or gamma2/AP1G2 and beta1A/AP1B1 or beta1B/AP1B1), a medium adaptin (mu1A/AP1M1 or mu1B/AP1M2) and a small adaptin (sigma1A/AP1S1 or sigma1B/AP1S2 or sigma1C/AP1S3). SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle; cytoplasmic vesicle membrane; peripheral membrane protein; cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Widely expressed. DISEASE: Deletion of the AP1B1 gene may play a role in the tumorigenesis of meningiomas. SIMILARITY: Belongs to the adaptor complexes large subunit family.

Supplier: List Biological Laboratories, Inc.

The potent toxicity of both the botulinum neurotoxins and anthrax lethal toxin is due to a zinc-dependent proteolytic activity associated with the toxins.  Measurement of this enzymatic activity provides for both a potentially sensitive and direct means for detection of the toxin, and a method for identifying potential toxin inhibitors using high throughput screening. A highly efficient approach for monitoring enzymatic activity is based on the use of fluorescence resonance energy transfer (FRET) substrates. These fluorogenic peptides contain a donor fluorescent group at one end and a suitable chromogenic acceptor group at the other.  The fluorescence is quenched initially by intramolecular energy transfer between the donor/acceptor pair.  Cleavage of the FRET substrate by the appropriate enzyme releases the fluorophore and full fluorescence is restored.  The increase in fluorescence intensity is directly proportional to the amount of enzyme present.  Enzymatic activity can be monitored continuously by recording the increase in fluorescence intensity with time.  The change in the relative fluorescence units (RFU) as cleavage occurs can be converted to nmoles of cleaved substrate from a standard curve generated using a Calibration Peptide which is the cleaved substrate containing only the N-terminally attached fluorophore.  For Botulinum neurotoxin type A, a Control FRET peptide substrate that is not cleaved by the neurotoxin but contains all remaining non-specific sites in the sequence can be used to screen background cleavage of the substrate that can occur in complex matrices.

Supplier: SCIEX

The Sciex Triple Quad 4500 System is a high sensitivity, bench top triple quadrupole mass spectrometer designed for LC-MS/MS analyses. This instrument provides excellent robustness and long term stability for the most demanding assays.

Supplier: Biosensis

GDNF is a glycosylated, disulfide-bonded homodimer molecule. It was first discovered as a potent survival factor for midbrain dopaminergic neurons and was then shown to rescue these neurons in animal models of Parkinson's disease. GDNF is about 100 times more efficient survival factor for spinal motor neurons than the neurotrophins. FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Secreted protein. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. DISEASE: Defects in GDNF may be a cause of Hirschsprung disease (HSCR). In association with mutations of RET gene, defects in GDNF may be involved in Hirschsprung disease. This genetic disorder of neural crest development is characterized by the absence of intramural ganglion cells in the hindgut, often resulting in intestinal obstruction. DISEASE: Defects in GDNF are a cause of congenital central hypoventilation syndrome (CCHS); also known as congenital failure of autonomic control or Ondine curse. CCHS is a rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.

Supplier: Biosensis

The spectrin family of proteins were originally discovered as major components of the submembraneous cytoskeleton of osmotically lysed red blood cells (1). The lysed blood cells could be seen as clear red blood cell shaped objects in the light microscope and were referred to as red cell "ghosts". The major proteins of these ghosts proved to be actin, ankyrin, band 4.1 and several other proteins, including two major bands running at about 240kDa and 260kDa on SDS-PAGE gels. This pair of bands was named "spectrin" since they were discovered in these red blood cell ghosts (1). Later work showed that similar high molecular bands were seen in membrane preparations from other eukaryotic cell types. Work by Levine and Willard described a pair of about ~240-260kDa molecular weight bands which were transported at the slowest rate along mammalian axons (2). They named these proteins "fodrin" as antibody studies showed that they were localized in the sheath under the axonal membrane, but not in the core of the axon (2; fodros is Greek for sheath). Subsequently fodrin was found to be a member of the spectrin family of proteins, and the spectrin nomenclature is now normally used (3). Spectrins form tetramers of two alpha and two beta subunits, with the alpha corresponding to the lower molecular weight ~240kDa band and the beta corresponding to the ~260kDa or in some case much larger band. The alpha-II subunit is widely expressed in tissues but, in the nervous system, is found predominantly in neurons. The antibody can therefore be used to identify neurons and fragments derived from neuronal membranes in cells in tissue culture and in sectioned material.