cdk8-in-12

CDK8-IN-12 is a selective, potent and orally active inhibitor of CDK8 (Ki: 14 nM) and is an anti-cancer agent. CDK8-IN-12 inhibits GSK-3α, GSK-3β and PCK-θ with Ki of 13 nM, 4 nM and 109 nM respectively. CDK8-IN-12 showed anti-proliferative activity against MV4-11 cells.

(3ξ,4ξ,5ξ,6ξ,7ξ,11ξ)-3,6-Dihydroxy-8-oxo-9-eremophilene-12-oic acid, a phytotoxin recently identified in Alternaria alternata ssp. tenuissima isolates, is linked to fruit spots on apples.

Drim-8(12)-ene-6β,7α,9α,11-tetraol is a useful organic compound for research related to life sciences and the catalog number is T125326.

8(E),10(E),12(Z)-Octadecatrienoic acid is a conjugated polyunsaturated fatty acid (PUFA) that has been found inC. officinalisseed oil and has anticancer activity.1,2,3It inhibits the growth of Caco-2 cells when used at concentrations ranging from 10 to 50 μM.28(E),10(E),12(Z)-Octadecatrienoic acid (10 μM) induces formation of thiobarbituric acid reactive substances (TBARS) and apoptosis in DLD-1 colorectal adenocarcinoma cells.3It also inhibits prostaglandin biosynthesis in sheep vesicular gland microsomes (IC50= 31 μM).4 1.Crombie, L., and Holloway, S.J.The biosynthesis of calendic acid, octadeca-(8E,10E, 12Z)-trienoic, acid, by developing marigold seeds: origins of (E,E,Z) and (Z,E,Z) conjugated triene acids in higher plantsJ. Chem. Soc. Perk. T. 12425-2434(1985) 2.Yasui, Y., Hosokawa, M., Kohno, H., et al.Growth inhibition and apoptosis induction by all-trans-conjugated linolenic acids on human colon cancer cellsAnticancer Res.26(3A)1855-1860(2006) 3.Shinohara, N., Ito, J., Tsuduki, T., et al.Jacaric acid, a linolenic acid isomer with a conjugated triene system, reduces stearoyl-CoA desaturase expression in liver of miceJ. Oleo Sci.61(8)433-441(2012) 4.Nugteren, D.H., and Christ-Hazelhof, E.Naturally occurring conjugated octadecatrienoic acids are strong inhibitors of prostaglandin biosynthesisProstaglandins33(3)403-417(1987)

β-amyloid (12-28) TFA, a peptide fragment of β-amyloid protein (β1-42), is the major component of senile plaque cores. β-amyloid (12-28) has aggregation properties and the potential for Alzheimer’s disease research.

12-Hydroxy-8(17),13-labdadien-16,15-olide is a natural product for research related to life sciences. The catalog number is TN2598 and the CAS number is 958885-86-4.

8-Oxoeremophil-6-en-12-oic aicd is a useful organic compound for research related to life sciences and the catalog number is T126063.

13,14,15,16-Tetranor-8(17)-labden-12-oic acid is a useful organic compound for research related to life sciences and the catalog number is T128352.

CDK-IN-12 (Example 20), a CDK inhibitor, effectively inhibits CDK4/6, demonstrating IC50 values below 20 nM [1].

15-Nor-14-oxolabda-8(17),12-dien-18-oic acid is a useful organic compound for research related to life sciences and the catalog number is T126495.

CDK8-IN-14 (compound 12) effectively inhibits CDK8, demonstrating an IC50 of 39.2 nM, and exhibits potent anti-AML cell proliferation effects, with a GC50 value of 0.02±0.01μM in MOLM-13 cells and 0.03±0.01μM in MV4-11 cells [1].

CDK8-IN-7 (compound 12) is a potent and selective inhibitor of cyclin-dependent kinase 8 (CDK8), with a Kd of 3.5 nM, and has demonstrated potential for AML-cancer research.

This synthetic peptide consists of amino acids 1 to 17 of beta amyloid protein. This peptide can be employed in beta amyloid solubility studies.

β-Amyloid (33-40) is a peptide composed of amino acids 33 to 40 from the beta-amyloid protein.

β-Amyloid (35-42), a peptide derived from the beta-amyloid protein, encompasses amino acids 35 through 42.

β-amyloid (15-21) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.

β-Amyloid (11-22) is a peptide fragment of β-Amyloid. β-Amyloid peptide (Abeta), the primary component of amyloid plaques in the brains of Alzheimer’s patients, is believed to be the cause of Alzheimer’s Disease (AD), the most common neurodegenerative disease, affecting approximately 10% of the population over 60.

Intracerebroventricular administration of synthetic peptides Beta-amyloid (12-20), (12-28), and (18-28) causes amnesia in mice. These peptides have only amino acid residues VFF at position 18 to 20 in common, suggesting the amnestic effect of the triad.

Amyloid β1-40 is one of the fragments generated after cleavage of the amyloid peptide precursor protein by β and γ secretases.

This synthetic peptide consists of amino acids 1 to 20 of beta amyloid protein.

This is an N-terminal fragment of beta amyloid. It consists of amino acid residues 1 to 9. Truncated beta amyloid peptide (10-40) still forms amyloid fibrils and shows fibril polymorphism.

Amyloid β-peptide fragment; minimum section required to bind to brain proteins. Binds with high affinity to α7-nicotinic ACh receptors, and impairs memory retention following central administration in mice in vivo.

This synthetic peptide consists of amino acids 22 to 40 of beta amyloid protein. This peptide sequence is often used in beta amyloid structure and aggregation studies.

β-Amyloid 15-21 acetate (Beta-Amyloid (15-21) acetate) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.

This is a fragment of beta-amyloid peptide. It has amino acids 1 through 34.

β-Amyloid (31-35) (β-Amyloid 31-35) is the shortest sequence of native Amyloid-β peptide.

β-Amyloid (1-15) (Amyloid β-Protein (1-15)) is a fragment of β-amyloid protein used in the study of Alzheimer's disease.

Anionic interaction of Beta-amyloid (1-11) with Factor XII is suspected to cause massive activation of the C4 (complement 4) system in the cerebrospinal fluid of Alzheimer’s disease patients.

β-Amyloid (1-37) (human) is potentially associated with mental status in Alzheimer's disease.

The amyloid β-protein is a 39- to 43-amino acid polypeptide that is the primary constituent of senile plaques and cerebrovascular deposits in Alzheimer's disease and Down's syndrome. Additionally it acts as an inhibitor of the ubiquitin-dependent protein degradation in vitro.

β-Amyloid (13-27) is a synthetic peptide comprising amino acids 26 to 40 of the beta amyloid protein. It is utilized to study the kinetics of beta amyloid formation.

β-Amyloid (1-28), a fragment of the β-Amyloid protein, is involved in metal binding.

β-Amyloid (12-20) is a peptide fragment of β-Amyloid containing the amino acid residues VFF at positions (18-20), suggesting amnestic effects for this triad.

β-Amyloid (25-35) (Aβ25-35) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide. Which has shown neurotoxic activities in cultured cells.

Rat form of the beta-Amyloid (1-40) peptide

Antibodies corresponding to beta-amyloid (4-10) are effective in vivo inhibitors of cytotoxicity, amyloid plaque formation and special memory disturbances in mice. This peptide does not elicit an inflammatory response.

β-Amyloid (1-16) is an amyloidogenic protein fragment derived from the β-amyloid sequence, known for its ability to bind metal ions, indicating its role in metal-binding processes. β-Amyloid, a peptide, is responsible for forming amyloid plaques in the brains of people with Alzheimer's disease (AD).

β-Amyloid (22-35) is a 14-aa peptide, shows aggregates and induces neurotoxicity in the hippocampal cells. Beta amyloid (22-35) is a synthetic truncated fragment of beta-amyloid peptide.

β-Amyloid (29-40) is a fragment of Amyloid-β peptide. Alzheimer's beta amyloid peptide (29-40 42) C-terminal fragments exhibit physical and chemical properties similar to fusion peptides of viral proteins, inducing liposome fusion in vitro.

Amyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) re