216376 Results for: "Nucleic+Acid+Sample+Prep"

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: RSP AMINO ACIDS, LLC MS

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

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: Prosci

ULBP1, also known as RAET1I and NKG2DL1, is a member of the ULBP/RAET1 gene family. ULBP1 plays an important role in immune responses, especially in cancer and infectious diseases, and is well-known to bind to NKG2D together with at least ULBP 2 and 3. These proteins are distantly related to major histocompatibility class I (MHC I) molecules, possessing the alpha 1 and alpha 2 Ig-like domains, but lacking the alpha 3 domain. Unlike MHC Class I, they have no capacity to bind peptide or interact with beta2-microglobulin. It can activate multiple signaling pathways in primary NK cells, gamma delta T cells, and CD8+ alpha beta T cells, resulting in the production of cytokines and chemokines.ULBP1 is expressed in wide range of tissues including heart, brain, lung, liver, bone marrow and some tumor cells, T-cells, B-cells, As an unconventional member of the MHC class I family, ULBP1 is able to interact with soluble CMV glycoprotein UL16 in CMV infected cells. The interaction with UL16 blocked the interaction with the NKG2D receptor, and thus might escape the immune surveillance. Furthermore, UL16 also causes ULBP1 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. The ULBP1 regulation may have implications for development of new therapeutic strategies against cancer cells.

Supplier: MP Biomedicals

Tweens® are a series of nonionic surfactants derived from sorbitan esters. They are soluble or dispersible in water but differ widely in organic and oil solubilities. Used as oil-in-water emulsifiers in pharmaceuticals, cosmetics, cleaning compounds, etc.
Tween® 80 has been widely used in biochemical applications including: solubilizing proteins, isolating nuclei from cells in culture selective protein extraction growing of tubercule bacilli, and emulsifying and dispersing substances in medicinal and food products. It has little or no activity as an anti-bacterial agent. It has been shown to have an adverse effect on the antibacterial effect of methyl paraben and related compounds. Non-ionic detergent used for selective protein extraction and isolation of nuclei from mammalian cell lines.
Soluble/miscible in water to give a clear yellow solution; miscible with alcohol, dioxane, and ethyl acetate; practically insoluble in liquid paraffin and fixed oils (such as mineral oil).
Autoclaving of solutions is not recommended. Sterile filtering is suggested with a 0.22 micron filter. Tween® may need to be warmed to about 40 °C and alternated with portions of hot distilled water while being poured through the filter.
Store at Room Temperature (15-30 °C).

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: VWR International

The CENCO® Mechanics System Kits include activities in mechanics and fluid mechanics topics.

Supplier: Binder

KMF constant climate chambers ensure constant test conditions throughout the stainless steel chamber even with a full load and only require a small amount of bench space. Units can be operated with pure aqua service, a flexible water purification system (optional) or deionized water. Units self-test for comprehensive status analysis.

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: Bioss

Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Activated by (-)-baclofen, cgp27492 and blocked by phaclofen. Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites.

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: Labconco

These low-profile enclosures provide user protection by keeping powders, particulates, and fumes contained during weighing procedures

Supplier: Thermo Scientific Chemicals

2.5KG

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.

Supplier: Thermo Scientific Chemicals

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