Saturday, March 31, 2012
The description of Z-Ala-Gly-OMe
Product name:Z-Ala-Gly-OMe
Der Ansatz wird am Abend vorbereitet und unter Ruhren ¨ uber Nacht stehen gelassen. Am ¨nachsten Tag wird abgesaugt um den ausgefallenen Dicyclohexylharnstoff (DCH) zu entfer- ¨nen, es wird mit 60ml Ethylacetat nachgewaschen. Die Losung wird ¨ uber einen Faltenfilter in ¨einen Scheidetrichter gebracht und mit den folgenden Losungen ausgesch ¨ uttelt: 1x mit 20ml ¨Wasser, 2x mit 15ml 5% Na2CO3 Losung und 2x mit 20ml ges ¨ attigter Kochsalzl ¨ osung. Dann ¨wird mit Na2SO4 sicc. getrocknet, abgefiltert und bis zur Trockene abrotiert. Es wird mit rund115ml Ethylacetat im warmen Wasserbad aufgelost, dann werden zum Umkristallisieren zuerst ¨20ml Benzin und dann weitere 60ml zugegeben. Nach dem Abnutschen wird im Exsikkatoruber das Wochenende getrocknet
CAS:4840-29-3
Description:
Size:1mg-1kg
Sequence:Z-Ala-Gly-OMe
Storage:-4℃
Molecular formula:C14H18N2O5
Molecular weight:294.3
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Friday, March 30, 2012
The introduction of Adjuvant Peptides
Fragments of bacterial cell wall peptidoglycan, murein, have long been known to have potent adjuvant properties. Synthetic versions of these molecules and murein-derived components are known as adjuvant Peptides.Johannsen L et al., In 1989 describes the properties of small cell wall monomers (muramyl peptides) that cause a number of short-term effects in vivo and in vitro .
The most studied of these molecules was muramyl dipeptide (adjuvant peptide, N-acetyl-muramyl-L-alanine-D-isoglutamine [MDP]), the minimum active subunit of bacterial peptidoglycan. However, other muramyl peptides that contain 1,6-anhydromuramyl residues were reported to have greater potency as an adjuvant peptides. The acute effects of muramyl peptides include rupture of the blood-aqueous humor, arthritis, cytotoxicity and slow wave sleep. That the monomers of the cell wall can cause sleep has attracted great interest because it explains a major side effect of infection apathy. More controversial has been suggested that muramyl peptides play a role in the sleep of healthy people 1,2,3.
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Thursday, March 29, 2012
The introduction of β-Amyloid (1-42), Rat
β-Amyloid (1-42), Rat production results from cleavage in the extracellular domain of APP by the β-secretase , which results in the production of the APP C-terminal fragment C99. This fragment is further cleaved by the γ-secretase at residues 40-42 to produce β-amyloid 40 and 42 peptides. β-amyloid aggregation and neuritic plaque formation are pathologic hallmarks of ADβ-Amyloid (1-42), Rat -induced learning and memory impairment in rats is believed to be associated with inflammation. Cytokine production is a key pathologic event in the progression of inflammatory processes. In this rat study, soybean isoflavones (SIF) was used to investigate it's protective effects on inflammation caused by β-Amyloid (1-42), Rat which is associated with learning and memory impairment in Alzheimer disease.
We characterized the learning and memory ability. cytokine profiles of circulating interleukin-1β (IL-1β), tumor necrosis factor-α (TNF-α) in the serum and the expression of Toll like receptor4 (TLR4) and nuclear factor-κB p65 (NF-κB p65) mRNA and protein in the brain tissue following intracerebroventricular administration of β-Amyloid (1-42), Rat by miniosmotic pump for 14 days. The results showed that functional deficits of learning and memory in SIF treatment groups were significantly improved compared to the control group without SIF treatment in water maze test. The serum IL-1β and TNF-α level were significantly increased, and the expressions of TLR4 and NF-κB p65 mRNA and protein in the brain were up-regulated, indicating inflammation response was initiated following administration of Aβ1-42. After intragastric pre-treatment with SIF, inflammatory cytokines was significantly reduced and also SIF reversed the Aβ1-42 induced up-regulation of TLR4 and NF-κB p65 mRNA and protein expression in the brain and expression of NF-κB p65 in nuclei. These results suggested that SIF reduced the cytokine cascade and inflammatory response induced by Aβ1-42 which could result in the improvement of spatial learning and memory ability impairment in the rats.
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Wednesday, March 28, 2012
The description of β-Amyloid (1-33)
GenScript β-Amyloid (1-33) is produced when purified metalloendopeptidase cleaves the Gly33-Leu34 bond of Alzheimer Aß (1-40) peptide, producing soluble 1-33 and 34-40 fragments of Aß (1-40) without any neurotoxic effects.
Alzheimer’s disease and cerebral amyloid angiopathy are characterized by the deposition of β-amyloid fibrils consisting of 40- and 42-mer peptides (Aβ40 and Aβ42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of Aβ40 and Aβ42 fibrils have been carried out. Aβ42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of Aβ40. This review summarizes mainly our own recent findings from the structural analysis of Aβ42 fibrils and discusses its relevance to their neurotoxicity in vitro.
Extensive β-Amyloid (1-33) deposits in brain parenchyma in the form of senile plaques and in blood vessels in the form of amyloid angiopathy are pathological hallmarks of Alzheimer's disease (AD). The mechanisms underlying Aβ deposition remain unclear. Major efforts have focused on Aβ production, but there is little to suggest that increased production of Aβ plays a role in Aβ deposition, except for rare familial forms of AD. Thus, other mechanisms must be involved in the accumulation of Aβ in AD. Recent data shows that impaired clearance may play an important role in Aβ accumulation in the pathogenesis of AD. This review focuses on our current knowledge of Aβ-degrading enzymes, including neprilysin (NEP), endothelin-converting enzyme (ECE), insulin-degrading enzyme (IDE), angiotensin-converting enzyme (ACE), and the plasmin/uPA/tPA system as they relate to amyloid deposition in AD.
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Tuesday, March 27, 2012
The Characteristics of Beta Amyloid [1-40] Peptide
Beta Amyloid [1-40] Peptide production results from cleavage in the extracellular domain of APP by the beta-secretase (BACE1) , which results in the production of the APP C-terminal fragment C99. This fragment is further cleaved by the gamma-secretase at residues 40-42 to produce beta-amyloid 40 and 42 peptides. Beta-amyloid aggregation and neuritic plaque formation are pathologic hallmarks of Alzheimer disease. Each vial contains 1 mg of lyophilized solid packaged under an inert gas and supplied as a trifluoroacetate salt
Storage:Store at -20°C. The product is hygroscopic and must be protected from light. Product is guaranteed one year from the date of shipment.
Beta Amyloid [1-40] Peptide corresponds to the rat beta-amyloid 1-40 peptide.We recommend using 100% dimethyl sulfoxide (DMSO). Alternatively, hexafluoroisopropanol (HFIP) can be used.Beta Amyloid peptides are derived from amyloid precursor protein (APP) and are thought to play a role in the development of the senile plaques associated with Alzheimer's Disease.
Beta Amyloid [1-40] Peptide is stored at -20°C. The product is hygroscopic and must be protected from light. Product is guaranteed one year from the date of shipment. Following reconstitution, aliquot and store at -20°C.
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Monday, March 26, 2012
The information of Beta Amyloid [25-35] Peptide
Fragment of Beta Amyloid [25-35] Peptide , functionally required for the neurotrophic and neurotoxic effects associated with Alzheimer's disease.Beta Amyloid [25-35] Peptide may cause malfunction and death of neurons in Alzheimer’s disease. We investigated the effect of Aβ on key transporters of amino acid neurotransmission in cells cultured from rat cerebral cortex. The cultures were treated with Beta Amyloid [25-35] Peptide at 3 and 10 μM for 12 and 24 h followed by quantitative analysis of immunofluorescence intensity.
The results indicate that Beta Amyloid [25-35] Peptide may impair neuronal function and transmitter synthesis, and perhaps reduce excitotoxicity, through a reduction in neuronal glutamine uptake. In mixed neuronal–glial cell cultures (from P1 rats), Aβ reduced the concentration of system A glutamine transporter 1 (SAT1), by up to 50% expressed relative to the neuronal marker microtubule-associated protein 2 (MAP2) in the same cell. No significant effects were detected on vesicular glutamate transporters VGLUT1 or VGLUT2 in neurons, or on glial system N glutamine transporter 1 (SN1). In neuronal cell cultures (from E18 rats), Beta Amyloid [25-35] Peptide did not reduce SAT1 immunoreactivity, suggesting that the observed effect depends on the presence of astroglia.
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Friday, March 23, 2012
The introduction of Sulforhodamine G
Sulforhodamine G is used as a polar tracer as sulforhodamine B. Compared to rhodamine B it is more fluorescent. Fig 8 Comparison of uranine and sulforhodamine G. a BTCs measured at inspection well 20DX inside the tunnel: the uranine BTC shows 20 times higher maximum concentrations and a shorter tail than the sulforhodamine G curve, although uranine was injected further upstream in Veccione Stream, suggesting that uranine behaves more conservatively in fractured turbidites (injection and sampling site are shown in Fig. ). b) Uranine and sulforhodamine G BTCs measured by means of a continuous fluorometer at the total drainage of the northern sector of the tunnel.
The uranine recovery is about 100 times higher than the sulforhodamine G recovery, further confirming the more conservative behaviour of uranine.In our initial experiments, we microinjected a range of fluorescent probes (fluorescein, Lucifer yellow CH [LYCH], sulforhodamine G) into the basal trichome cell to determine symplasmic continuity between the basal trichome cell and the underlying epidermis (Fig. 1A ). As all dyes gave the same result, we present here data for the most membrane impermeant of these, LYCH. Given the large numbers of PD at the e/t interface (Faulkner et al., 2008), we were surprised that in 35 of 39 injections, LYCH failed to move across the e/t boundary and enter the epidermis (Fig. 1A).
However, in each injection, LYCH moved apically into other trichome cells (Fig. 1A). In all cases, cytoplasmic streaming resumed immediately after dye injection. When dye was observed to have crossed the e/t barrier, only extremely weak fluorescence was observed in the underlying epidermal cell. In contrast, if we injected LYCH into the supporting epidermal cell, dye moved apically across the e/t boundary into the trichome (Fig. 1B). With time (1–3 h), all dyes were sequestered slowly into the central vacuoles of the trichome cells, sulforhodamine G showing the highest rate of vacuolar sequestration .
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Thursday, March 22, 2012
The information of L-Alaninol
N-protection1; oxidation of N-protected derivative of the aldehyde .2, 3.4 L-alanine, also known as (2S)-2-aminopropanoic acid, is a member of a class of nutrients known amino acids, which are used by the body for assembling the proteins that serve the basic building blocks of life. since the human body is able to produce enough L-Alaninolto meet its needs, and from both animal and plant sources of the amino acid are abundant in nature, most dietary supplementation is generally considered non-essential. the main functions of L-Alaninol in the human body relate to the metabolism of glucose and pyruvate as well as transport of nitrogen to the liver. though rarely used in alternative medicine, some practitioners have suggested that people with conditions that affect the serum levels ofL-Alaninol can benefit from supplements to promote liver health, relieve muscle degeneration, treat levels reduced energy, and facilitate the use of vitamin B. researchers from Imperial College London can call these applications in question, however, that their 2011 study found a correlation between increased levels of the amino acid in the blood and a higher incidence of hypertension and obesity.
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Wednesday, March 21, 2012
The information of Fmoc-Cit-OH
This report provides general information on FMOC-CIT-OH situation at world chemical science and general market review.
The report can be interesting for chemical markets investors, technologists and scientific researchers.
1. FMOC-CIT-OH GENERAL INFORMATION, PHYSICAL AND CHEMICAL PROPERTIES
Includes main physical, chemical and technical information such as: composition, information on ingredients, hazards and transport information, handling and storage, toxicological & ecological information etc
2. FMOC-CIT-OH RELATED TECHNICAL INFORMATION
Includes information on application areas, patents, FMOC-CIT-OH related scientific articles
3. MAIN REGIONAL AND GLOBAL FMOC-CIT-OH PRODUCERS AND SUPPLIERS, CONTACT DETAILS
Regions covered: Europe, Asia, North America
4. LABORATORY PRICES FROM MAIN SUPPLIERS
Description:
Appearance:White to off-white powder
Melting Point:>160℃
Purity:>98%
Storage:Cool and dry place protected from light..
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Tuesday, March 20, 2012
The decription of Rhodamine 6G
Rhodamine 6G is also used as a laser dye, or gain medium, in dye lasers,and is pumped by the 2nd (532 nm) harmonic from an Nd:YAG laser or nitrogen laser. The dye has a remarkably high photostability, high fluorescence quantum yield (0.95 , low cost, and its lasing range has close proximity to its absorption maximum (approximately 530 nm). The lasing range of the dye is 555 to 585 nm with a maximum at 566 nm .Rhodamine 6G usually comes in three different forms. Rhodamine 6G chloride is a bronze/red powder with the chemical formula C27H29ClN2O3. Although highly soluble, this formulation is very corrosive to all metals except stainless steel. Other formulation are less soluble, but also less corrosive. Rhodamine 6G Perchlorate, (C27H29ClN2O7), comes in the form of red crystals, while rhodamine 6G tetrafluoroborate, (C27H29BF4N2O3), appears as maroon crystals.
Rhodamine 6G is a chemical compound and a dye. It is often used as a tracer dye within water to determine the rate and direction of flow and transport. Rhodamine dyes fluoresce and can thus be detected easily and inexpensively with instruments called fluorometers. Rhodamine dyes are used extensively in biotechnology applications such as fluorescence microscopy, flow cytometry, fluorescence correlation spectroscopy and ELISA.
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Monday, March 19, 2012
The introduction of β-Amyloid (42-1)
Beta amyloid (42-1) is the reverse of beta amyloid (1-42), the latter is a member of beta amyloid-peptides, which are involved in the amyloid beta-peptide (A beta)-associated free radical oxidative stress model for neuronal death in Alzheimer's disease (AD) brain.
:Beta amyloid (42-1) is the reverse of beta amyloid (1-42), the latter is a member of beta amyloid-peptides, which are involved in the amyloid beta-peptide (A beta)-associated free radical oxidative stress model for neuronal death in Alzheimer's disease (AD) brain.
Formula :C203H311N55O60S1
M.W.:4514.4
Purity: 95%
Storage :Store at -20°C. Keep tightly closed. Store in a cool dry place.Cognitive impairment in Alzheimer's disease (AD) patients is associated with a decline in the levels of growth factors, impairment of axonal transport and marked degeneration of basal forebrain cholinergic neurons (BFCNs). Neurogenesis persists in the adult human brain, and the stimulation of regenerative processes in the CNS is an attractive prospect for neuroreplacement therapy in neurodegenerative diseases such as AD. Currently, it is still not clear how the pathophysiological environment in the AD brain affects stem cell biology. Previous studies investigating the effects of the β-amyloid (Aβ) peptide on neurogenesis have been inconclusive, since both neurogenic and neurotoxic effects on progenitor cell populations have been reported.
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Friday, March 16, 2012
The decription of β-Amyloid (1-16)
The fragment adsorption and aggregation of β-amyloid (1-16) at the air-water interface was studied by the combination of second-harmonic generation (SHG) spectroscopy, Brewster angle microscopy (BAM), and molecular dynamics (MD). The Gibbs free energy of surface adsorption was measured at -10.3 kcal / mol for bulk pH of 7.4 and 3, but no adsorption was observed for pH 10-11. The fragment 1-16 is estimated not to be involved in fibril formation of β-amyloid protein, but it presents an interesting behavior at the air-water interface, as manifested in the two time scales for SHG response observed. The shorter time scale (minutes) reflects the adsorption surface, and the longer time scale (hours) reflects a rearrangement and aggregation of the peptide to the air-water interface. These two processes are also highlighted by BAM measurements. Molecular dynamics simulations confirm the pH dependence of behavior of the surface of the β-amyloid, with an affinity greater surface area is at pH = 7. It also follows from the simulations phenylalanine residue is the most exposed surface, followed by tyrosine and histidine in their neutral form.
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Thursday, March 15, 2012
The decription of β-Amyloid (11-22)
Product name: β-Amyloid (11-22)
Sequence
(one-letter code)
EVHHQKLVFFAE
Sequence
(three-letter code)
{Glu}{Val}{His}{His}{Gln}{Lys}{Leu}{Val}{Phe}{Phe}{Ala}{Glu}
Description
Beta-amyloid peptide (Abeta), the major constituent of amyloid plaques in the brains of Alzheimers patients, is thought to be the cause of Alzheimers Disease (AD). AD is the most common neurodegenerative disease and afflicts about 10% of the population over 60.
Formula:C70H102N18O18
M.W.:1483.68
Purity:95%
Storage:Store GenScript β-amyloid (11-22) at -20°C
Purity
95%
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Wednesday, March 14, 2012
The decription of β-Amyloid (12-28)
The neurotoxicity of β-Amyloid (12-28) fragments may be a result of their solution conformation, which is very sensitive to solution conditions. In this work we describe NMR and CD studies of the conformation of
β-Amyloid (12-28) in lipid (micelle) environments as a function of pH and lipid type. The interaction of beta AP(12-28) with zwitterionic dodecylphosphocholine (DPC) micelles is weak and alters the conformation when compared to water solution alone. By contrast, the interaction of the peptide with anionic sodium dodecylsulfate (SDS) micelles is strong:
β-Amyloid (12-28) is mostly bound, is alpha-helical from K16 to V24, and aggregates slowly. The pH-dependent conformation changes of
β-Amyloid (12-28) in solution occur in the pH range at which the side-chain groups of E22, D23, H13, and H14 are deprotonated (pKas ca. 4 and 6.5); the interaction of
β-Amyloid (12-28) with SDS micelles alters the pH-dependent conformational transitions of the peptide whereas the weak interaction with DPC micelles causes little change.
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Monday, March 5, 2012
Some information of β-Amyloid (42-1)
Alias of β-Amyloid (42-1) :βAmyloid; b-Amyloid; Amyloid;
beta-Amyloid; beta Amyloid
Sequence(one-letter code): AIVVGGVMLGIIAGKNSGVDEAFFVLKQHHVEYGSDHRFEAD
Sequence:(three-letter code)
{ALA}{ILE}{VAL}{VAL}{GLY}{GLY}{VAL}{MET}{LEU}{GLY}{ILE}{ILE}{ALA}{GLY}{LYS}{ASN}{SER}{GLY}{VAL}{ASP}{GLU}{ALA}{PHE}{PHE}{VAL}{LEU}{LYS}{GLN}{HIS}{HIS}{VAL}{GLU}{TYR}{GLY}{SER}{ASP}{HIS}{ARG}{PHE}{GLU}{ALA}{ASP}
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Thursday, March 1, 2012
Carbonyl iron powder Information
BASF carbonyl iron powder (CIP) is an exceptionally fine and pure iron powder with unique morphological properties. BASF discovered the process of producing carbonyl iron powder 85 years ago, and is still the world's leading producer of CIP. Working with our customers, we use our experience and expertise to develop innovative solutions for a whole spectrum of different applications. The result is a wide range of carbonyl iron powders tailored to the specific needs of our customers.
Applications
Inductive electronic components
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Diamond tools
Microwaves and radar absorption
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