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Purity: =99.66%
Amyloid β-Peptide (1-42) human is a human form of amyloid β-peptide composed of 42-amino acids and can be found in the brains of patients with Alzheimer's disease. It plays a key role during the pathogenesis of Alzheimer disease (AD).
Amyloid β-Peptide (1-42) human (CAS: 107761-42-2) is a 42-amino acid proteolytic fragment derived from amyloid precursor protein and constitutes the primary protein component of senile plaques (neuritic plaques) in the brains of patients with Alzheimer's disease, playing a central role in its pathogenesis. This peptide exhibits a high propensity for aggregation, and its pathogenic forms exert synaptic toxicity and neurotoxicity through the formation of soluble oligomers, which bind to various neuronal surface receptors (such as PrPc, mGluR5, and NMDA receptors), triggering oxidative stress, calcium homeostasis imbalance, and downstream signaling pathway activation, ultimately leading to neuronal dysfunction and death. As a key molecular tool in Alzheimer's disease research, this peptide is widely used in disease modeling, drug screening, and investigations of pathogenic mechanisms.| Targets |
Peptide; AD biomarker
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| ln Vitro |
Guidelines for beta-amyloid aggregation (The following are our recommended protocols. This is a guide only and may be modified to suit your specific needs).
1. Dissolve solid Aβ peptide in cold hexafluoro-2-propanol (HFIP). The peptide was incubated at room temperature for at least 1 hour to establish monomers and structural randomization. 2. HFIP is removed by evaporation and the resulting peptide is stored in the form of a thin film at -20 or -80℃. 3. Dissolve the resulting film in 5mM anhydrous DMSO, and then vortex and dilute to the appropriate concentration and buffer (serum and phenol red free medium). 4. Next, leave the solution at 4-8°C for 48 hours. The sample was then centrifuged at 14000g at 4-8°C for 10 minutes; Soluble oligomers in the supernatant. Dilute the supernatant by 10-200 times before the experiment. Methods vary depending on downstream application. Note: The aggregated form is unstable in solution and is recommended for immediate use. In vitro studies demonstrate that Aβ(1-42) exhibits potent neurotoxicity. At 2.5 μM, it reduces SH-SY5Y cell viability to 65% of control levels. It enhances inactivation of Ca²⁺ currents and blocks Ca²⁺-dependent K⁺ currents in neuronal cells. Aβ(1-42) oligomers localize to both the cytoplasm and nucleus within 30 minutes of treatment, with extensive accumulation observed after 8 hours. The peptide also increases APP mRNA expression levels in treated cells. Soluble oligomers of Aβ(1-42) are highly toxic to neuronal cells, impairing synaptic function and serving as the primary neurotoxic species in Alzheimer's disease pathogenesis. The aggregated form is unstable in solution, requiring immediate use after preparation . |
| ln Vivo |
Alzheimer's disease models in animals can be created using human TFA and β-Amyloid (1-42).
In vivo, Aβ(1-42) is widely used to establish animal models of Alzheimer's disease via stereotaxic injection into the hippocampus or lateral ventricle. Bilateral hippocampal injection of 10 μg (1 μL) of Aβ(1-42) per side in rats induces significant cognitive deficits, as measured by Morris water maze tests (prolonged escape latency and reduced platform crossings). The peptide induces neurodegeneration, characterized by reduced neuron numbers, nuclear pyknosis, and increased expression of advanced glycation end product receptor (AGER) in the cerebral cortex and hippocampus. Compared to single-factor models (D-galactose or Aβ alone), combined administration produces more severe cognitive impairment. This model is best suited for short-term studies focusing on Aβ effects on specific brain regions . |
| Enzyme Assay |
The possibility to monitor, in solution, the steps of beta-amyloid (Abeta) nucleation and therefore to describe this dynamic process by using capillary electrophoresis and under optimized experimental conditions is described. Striking differences in the electrophoretic patterns of Abeta 1-42 and Abeta 1-40 over time are here shown, and different aggregation states are elucidated, which reflect the very diverse oligomerization behavior of two very similar peptides. The isolation of one aggregated species of high molecular weight by ultracentrifugation allowed us to assess its role as toxic oligomer. The perturbation of the existing equilibrium among the identified species by the addition of small molecules can in principle interfere with the aggregation process of the peptides and ultimately prevent the plaque formation in vitro.[3]
For cell-free aggregation studies of Aβ(1-42), the standard protocol involves preparing monomeric peptide by dissolving solid Aβ(1-42) in cold hexafluoro-2-propanol (HFIP) and incubating at room temperature for at least 1 hour to establish monomerization and structural randomization. HFIP is removed by evaporation, and the resulting peptide film is stored at -20°C or -80°C. The film is dissolved in 5 mM anhydrous DMSO, then diluted to appropriate concentration in buffer (serum- and phenol red-free culture medium). To generate oligomers, the solution is aged at 4-8°C for 48 hours, then centrifuged at 14,000 × g for 10 minutes at 4-8°C; soluble oligomers are recovered in the supernatant and diluted 10-200-fold for experiments. Aggregation state is monitored using Thioflavin T (ThT) fluorescence, transmission electron microscopy (TEM), or MALDI-TOF mass spectrometry. The aggregated form is unstable and should be used immediately . |
| Cell Assay |
Different types of voltage-gated ion currents were recorded in isolated neurons of snail Helix pomatia using the two-microelectrode voltage-clamp technique. Application of amyloid-β peptide (1-42, 1-10 μM) in the bathing solution did not change delayed rectifier K(+)-current and leakage current, but enhanced inactivation of Ca(2+)-current and blocked Ca(2+)-dependent K(+)-current.[1]
Aβ Peptides and MTT Assay [2] Synthetic Aβ peptides were monomerized and solubilized as described. Briefly, monomerized peptides were dissolved to 1 mg/ml in deionized water supplemented with ammonia to a final concentration of 0.13% (measured at pH 9.8). All peptides were used at a concentration of 1 μm. 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay was performed as described previously. Nuclei Preparation and ELISA[2] Nuclei were isolated with the Nuclei EZ Prep nuclei isolation kit according to the manufacturer's instructions with minor modifications. Briefly, pellets containing nuclei were resuspended in PBS, sonicated, incubated at 95 °C, and centrifuged for 10 min at 20,000 × g. Aβ42 ELISAs using the C-terminal specific G2-13 antibody were performed as described. To quantify Aβ38, Aβ40, Aβ42, Aβ42 G33A, and Aβ43, the antibody 4G8 recognizing Aβ residues 17–24 was used. Immunofluorescence [2] SH-SY5Y cells were treated with biotinylated Aβ42 peptide 1 μm. Cells were fixed and permeabilized with 3.3% formaldehyde containing 0.5% Triton X-100 followed by 125 mm glycine in PBS containing magnesium and calcium. Cells were blocked with 5% fetal bovine calf serum followed by the primary antibody. Biotin-Aβ42 was detected with the monoclonal antibody AB or alternatively with Avidin Fluor488 (Sigma). Nuclei were stained with DAPI. Images were obtained using an LSM 510 meta confocal microscope. A typical in vitro protocol for Aβ(1-42) neurotoxicity studies uses SH-SY5Y neuroblastoma cells. Cells are treated with biotinylated Aβ(1-42) peptide at 1-10 μM concentrations. For localization studies, cells are fixed and permeabilized with 3.3% formaldehyde containing 0.5% Triton X-100, then treated with 125 mM glycine in PBS containing magnesium and calcium. Cells are blocked with 5% fetal bovine serum, then incubated with primary antibodies. Biotin-Aβ(1-42) peptide is detected using Avidin Fluor488, and nuclei are stained with DAPI. Images are acquired using confocal microscopy (e.g., LSM 510 meta). For viability assays, cells are treated with 2.5 μM Aβ(1-42) for 24-48 hours, and viability is assessed using MTT or CCK-8 assays. Due to peptide instability, all solutions should be freshly prepared and used immediately . |
| Animal Protocol |
Animals (transgenic APPPS1 mice, 12 months old) were perfused with PBS followed by fixative solution (4% formaldehyde, 0.2% glutaraldehyde in 50 mm sodium cacodylate buffer, pH 7.4). Hippocampi were dissected and post-fixed in the same solution at room temperature. Samples were embedded in LR-Gold resin and polymerized at 4 °C. Ultra-thin sections were incubated with the G2-13 primary antibody labeled with 10 nm colloidal gold. The sections were counterstained with uranyl acetate followed by lead citrate.[2]
Labeling of mAb G2-13 was performed with colloidal gold. After centrifugation (10 min, 6700 × g), the supernatant of colloidal gold was counterstained with uranyl acetate and analyzed by TEM to ensure that the supernatant was free of gold aggregates. An amount of 500 μg of mAb G2-13 was dialyzed with 2 mm sodium tetraborate. Equal volumes of G2-13 and colloidal gold were incubated for 20 min at RT. The stability of the gold/protein ratio was assessed by titration with 10% NaCl. Colloidal gold was adjusted to pH 9 in 100 mm potassium carbonate. The protein/gold solution was incubated in 1% BSA for 20 min. After centrifugation, the pellet was resuspended in 20 mm TBS, 1% BSA, and 0.05% sodium azide, pH 8.2, and the solution was centrifuged for 5 min at 6700 × g. The supernatant contained G2-13 antibodies labeled with 10 nm of gold.[2] A standard in vivo protocol for Aβ(1-42)-induced Alzheimer's disease model: Adult SD rats (or C57BL/6 mice) are anesthetized with 2% pentobarbital sodium (50 mg/kg, i.p.) and placed in a stereotaxic apparatus. The skull is exposed via a midline incision, and a burr hole is drilled at coordinates AP = -3.5 mm, ML = +2.0 mm from bregma for hippocampal injection. A microsyringe is inserted vertically to a depth of 3.0 mm from the brain surface (DV = 3.0 mm). Aβ(1-42) (10 μg in 1 μL sterile PBS) is injected slowly into each hippocampus over 5 minutes. The needle is left in place for 5 minutes to allow diffusion, then withdrawn slowly over 5 minutes. For lateral ventricle injection, coordinates are typically AP = -0.8 mm, ML = ±1.5 mm, DV = -3.5 mm from bregma. Cognitive function is assessed 1-4 weeks post-injection using Morris water maze (escape latency, platform crossings) and neurological severity scores. Brain tissues are collected for histology (Nissl staining, immunohistochemistry for AGER, and Aβ deposition) . |
| ADME/Pharmacokinetics |
Aβ(1-42) itself is not a therapeutic agent but a pathogenic peptide; its pharmacokinetic properties are studied in the context of clearance and metabolism. The peptide undergoes degradation by various proteases in biological matrices, including plasma, whole blood, and liver S9 fractions. Endogenous clearance mechanisms include enzymatic degradation by neprilysin, insulin-degrading enzyme (IDE), and matrix metalloproteinases, as well as receptor-mediated transport across the blood-brain barrier via LRP1 (low-density lipoprotein receptor-related protein 1). Impaired Aβ clearance is a key factor in sporadic AD pathogenesis, with decreased Aβ42/Aβ40 ratio serving as an indicator of reduced amyloid clearance in presymptomatic AD. Studies on Aβ-binding peptides (e.g., D-AIP) show that oral administration can achieve brain penetration with measurable plasma concentrations (AUC values ranging from 261-1928 ng·h/mL at doses of 10-100 mg/kg). The elimination half-life (t½) of Aβ-binding compounds in mouse plasma is approximately 3-5 hours .
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| Toxicity/Toxicokinetics |
Aβ(1-42) exhibits potent neurotoxicity in both in vitro and in vivo settings. In vitro, at 2.5 μM, it reduces SH-SY5Y cell viability to 65% of control levels, with higher concentrations causing greater cytotoxicity. The peptide induces oxidative stress, calcium dysregulation, and mitochondrial dysfunction, leading to apoptosis. In vivo, intracerebral injection of Aβ(1-42) (10 μg/site) causes neuronal loss, neuroinflammation, and cognitive deficits without significant systemic toxicity. The peptide is considered relatively safe for the operator when handled appropriately, as the primary toxicity is directed to neural tissues in model organisms. Human toxicity is associated with AD pathogenesis, where accumulation of Aβ(1-42) oligomers and plaques contributes to progressive neurodegeneration and cognitive decline. No acute systemic toxicity has been reported at the doses used for animal modeling. However, as a disease-associated peptide, its pathogenicity underscores the importance of proper handling and disposal according to institutional biosafety guidelines .
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| References |
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| Additional Infomation |
Using dual microelectrode voltage clamp technique, different types of voltage-gated ion currents were recorded in isolated neurons from snails (Helix pomatia). The addition of amyloid-β peptide (1-42, 1-10 μM) to the bath did not change the delayed rectified potassium ion current and leakage current, but enhanced the inactivation of calcium ion current and blocked calcium-dependent potassium ion current. [1]
Although the soluble amyloid-β peptide Aβ42 is associated with the symptoms of Alzheimer's disease, little is known about the biological activity of amyloid-β peptide (Aβ). In this paper, we found that Aβ peptides of 38 to 43 amino acids in length could be internalized in cultured neuroblastoma cells and were present in the cell nucleus. We confirmed the direct detection of nuclear Aβ42 using three independent methods: (i) biochemical analysis of nuclear components; (ii) detection of biotin-labeled Aβ in live cells using confocal laser scanning microscopy; and (iii) observation of Aβ in cultured cells and brain tissue from wild-type and transgenic APPPS1 mice (overexpressing amyloid precursor protein with Swedish and L166P mutations, respectively) using transmission electron microscopy. Furthermore, this study elucidated a novel function of Aβ42 in nuclear signaling, distinct from the intracellular domain of amyloid precursor protein. Chromatin immunoprecipitation experiments demonstrated that Aβ42 specifically interacts as a gene transcription repressor with the LRP1 and KAI1 promoters. Quantitative RT-PCR confirmed that the mRNA levels of the candidate genes detected were reduced only by the potentially neurotoxic wild-type Aβ42 peptide. Shorter peptides (Aβ38 or Aβ40) and other longer peptides (non-toxic Aβ42 G33A substitution or Aβ43) had no effect on mRNA levels. Overall, our data suggest that nuclear translocation of Aβ42 affects gene regulation, and the detrimental role of Aβ42 in the pathogenesis of Alzheimer's disease may be influenced by alterations in the expression profile of disease-modifying genes. [2] |
| Molecular Formula |
C₂₀₃H₃₁₁N₅₅O₆₀S
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|---|---|
| Molecular Weight |
4514.04
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| Exact Mass |
4511.27
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| CAS # |
107761-42-2
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| PubChem CID |
57339251
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| Sequence |
Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala
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| SequenceShortening |
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
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| Appearance |
White to off-white solid powder
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| LogP |
1.351
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| SMILES |
CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)O)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@H](CC2=CC=CC=C2)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CC3=CNC=N3)NC(=O)[C@H](CC4=CNC=N4)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC5=CC=C(C=C5)O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC6=CNC=N6)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC7=CC=CC=C7)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)O)N
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| InChi Key |
DZHSAHHDTRWUTF-SIQRNXPUSA-N
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| InChi Code |
InChI=1S/C203H311N55O60S/c1-28-106(20)164(195(310)220-91-149(267)228-130(71-98(4)5)181(296)238-129(66-70-319-27)179(294)251-158(100(8)9)193(308)218-87-146(264)215-88-151(269)250-160(102(12)13)198(313)255-163(105(18)19)199(314)258-165(107(21)29-2)200(315)227-112(26)202(317)318)257-201(316)166(108(22)30-3)256-169(284)109(23)224-147(265)89-216-171(286)122(51-40-42-67-204)233-188(303)139(81-145(208)263)244-192(307)143(94-260)230-150(268)92-219-194(309)159(101(10)11)252-191(306)141(83-157(280)281)245-177(292)127(60-64-153(272)273)232-168(283)111(25)226-180(295)133(73-113-45-34-31-35-46-113)241-184(299)135(75-115-49-38-33-39-50-115)247-196(311)162(104(16)17)254-190(305)131(72-99(6)7)239-173(288)123(52-41-43-68-205)234-175(290)125(58-62-144(207)262)236-185(300)136(77-117-84-211-95-221-117)243-187(302)138(79-119-86-213-97-223-119)248-197(312)161(103(14)15)253-178(293)128(61-65-154(274)275)237-182(297)132(76-116-54-56-120(261)57-55-116)229-148(266)90-217-172(287)142(93-259)249-189(304)140(82-156(278)279)246-186(301)137(78-118-85-212-96-222-118)242-174(289)124(53-44-69-214-203(209)210)235-183(298)134(74-114-47-36-32-37-48-114)240-176(291)126(59-63-152(270)271)231-167(282)110(24)225-170(285)121(206)80-155(276)277/h31-39,45-50,54-57,84-86,95-112,121-143,158-166,259-261H,28-30,40-44,51-53,58-83,87-94,204-206H2,1-27H3,(H2,207,262)(H2,208,263)(H,211,221)(H,212,222)(H,213,223)(H,215,264)(H,216,286)(H,217,287)(H,218,308)(H,219,309)(H,220,310)(H,224,265)(H,225,285)(H,226,295)(H,227,315)(H,228,267)(H,229,266)(H,230,268)(H,231,282)(H,232,283)(H,233,303)(H,234,290)(H,235,298)(H,236,300)(H,237,297)(H,238,296)(H,239,288)(H,240,291)(H,241,299)(H,242,289)(H,243,302)(H,244,307)(H,245,292)(H,246,301)(H,247,311)(H,248,312)(H,249,304)(H,250,269)(H,251,294)(H,252,306)(H,253,293)(H,254,305)(H,255,313)(H,256,284)(H,257,316)(H,258,314)(H,270,271)(H,272,273)(H,274,275)(H,276,277)(H,278,279)(H,280,281)(H,317,318)(H4,209,210,214)/t106-,107-,108-,109-,110-,111-,112-,121-,122-,123-,124-,125-,126-,127-,128-,129-,130-,131-,132-,133-,134-,135-,136-,137-,138-,139-,140-,141-,142-,143-,158-,159-,160-,161-,162-,163-,164-,165-,166-/m0/s1
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| Chemical Name |
(4S)-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-6-amino-1-[[2-[[(2S)-1-[[(2S,3S)-1-[[(2S,3S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[2-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(1S)-1-carboxyethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1-oxohexan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-4-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]propanoyl]amino]-5-oxopentanoic acid
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| Synonyms |
β-Amyloid (1-42, human); Abeta1-42; Abeta42; Amyloid beta 1-42; Abeta 1-42;
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month Note: (1). This product is not stable in solution, please use freshly prepared working solution for optimal results. (2). Please store this product in a sealed and protected environment, avoid exposure to moisture. |
| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
DMSO : ~33.33 mg/mL (~7.20 mM)
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|---|---|
| Solubility (In Vivo) |
Solubility in Formulation 1: ≥ 2.5 mg/mL (0.54 mM) (saturation unknown) in 10% DMSO + 40% PEG300 + 5% Tween80 + 45% Saline (add these co-solvents sequentially from left to right, and one by one), clear solution.
For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 400 μL PEG300 and mix evenly; then add 50 μL Tween-80 to the above solution and mix evenly; then add 450 μL normal saline to adjust the volume to 1 mL. Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH₂ O to obtain a clear solution. Solubility in Formulation 2: 2.5 mg/mL (0.54 mM) in 10% DMSO + 90% (20% SBE-β-CD in Saline) (add these co-solvents sequentially from left to right, and one by one), suspension solution; with ultrasonication. For example, if 1 mL of working solution is to be prepared, you can add 100 μL of 25.0 mg/mL clear DMSO stock solution to 900 μL of 20% SBE-β-CD physiological saline solution and mix evenly. Preparation of 20% SBE-β-CD in Saline (4°C，1 week): Dissolve 2 g SBE-β-CD in 10 mL saline to obtain a clear solution. View More
Solubility in Formulation 3: ≥ 2.5 mg/mL (0.54 mM) (saturation unknown) in 10% DMSO + 90% Corn Oil (add these co-solvents sequentially from left to right, and one by one), clear solution. |
| Preparing Stock Solutions | 1 mg | 5 mg | 10 mg | |
| 1 mM | 0.2215 mL | 1.1077 mL | 2.2153 mL | |
| 5 mM | 0.0443 mL | 0.2215 mL | 0.4431 mL | |
| 10 mM | 0.0222 mL | 0.1108 mL | 0.2215 mL |
*Note: Please select an appropriate solvent for the preparation of stock solution based on your experiment needs. For most products, DMSO can be used for preparing stock solutions (e.g. 5 mM, 10 mM, or 20 mM concentration); some products with high aqueous solubility may be dissolved in water directly. Solubility information is available at the above Solubility Data section. Once the stock solution is prepared, aliquot it to routine usage volumes and store at -20°C or -80°C. Avoid repeated freeze and thaw cycles.
Calculation results
Working concentration： mg/mL；
Method for preparing DMSO stock solution： mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation:：Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O，mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.
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