[Ala107]-MBP (104-118)Protein kinase C inhibitor CAS# 99026-77-4 |
![[Ala107]-MBP (104-118)](/media/images/struct/BCC5835.png "[Ala107]-MBP (104-118)")
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Quality Control & MSDS
Number of papers citing our products
Chemical structure
3D structure
| Cas No. | 99026-77-4 | SDF | Download SDF |
| PubChem ID | 71312080 | Appearance | Powder |
| Formula | C67H104N20O19 | M.Wt | 1493.68 |
| Type of Compound | N/A | Storage | Desiccate at -20°C |
| Synonyms | [Ala<sup>107</sup>]-Myelin Basic Protein (104-118) | ||
| Solubility | Soluble to 1 mg/ml in 10% acetonitrile | ||
| Sequence | GKGAGLSLSRFSWGA | ||
| Chemical Name | (2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[2-[[(2S)-6-amino-2-[(2-aminoacetyl)amino]hexanoyl]amino]acetyl]amino]propanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]acetyl]amino]propanoic acid | ||
| SMILES | CC(C)CC(C(=O)NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CO)C(=O)NC(CCCN=C(N)N)C(=O)NC(CC1=CC=CC=C1)C(=O)NC(CO)C(=O)NC(CC2=CNC3=CC=CC=C32)C(=O)NCC(=O)NC(C)C(=O)O)NC(=O)CNC(=O)C(C)NC(=O)CNC(=O)C(CCCCN)NC(=O)CN | ||
| Standard InChIKey | PKKMMDDHSZRJTF-NBRSAOMZSA-N | ||
| Standard InChI | InChI=1S/C67H104N20O19/c1-35(2)23-45(80-55(94)31-74-56(95)37(5)77-53(92)29-75-57(96)43(19-12-13-21-68)79-52(91)27-69)60(99)85-50(33-89)64(103)82-46(24-36(3)4)61(100)86-49(32-88)63(102)81-44(20-14-22-72-67(70)71)59(98)83-47(25-39-15-8-7-9-16-39)62(101)87-51(34-90)65(104)84-48(26-40-28-73-42-18-11-10-17-41(40)42)58(97)76-30-54(93)78-38(6)66(105)106/h7-11,15-18,28,35-38,43-51,73,88-90H,12-14,19-27,29-34,68-69H2,1-6H3,(H,74,95)(H,75,96)(H,76,97)(H,77,92)(H,78,93)(H,79,91)(H,80,94)(H,81,102)(H,82,103)(H,83,98)(H,84,104)(H,85,99)(H,86,100)(H,87,101)(H,105,106)(H4,70,71,72)/t37-,38-,43-,44-,45-,46-,47-,48-,49-,50-,51-/m0/s1 | ||
| General tips | For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months. We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months. Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it. |
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| About Packaging | 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial. 2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial. 3. Try to avoid loss or contamination during the experiment. |
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| Shipping Condition | Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request. | ||
| Description | Synthetic peptide analog of bovine myelin basic protein (MBP). Non-competitive inhibitor of PKC (IC50 = 46 - 145 mM). |
[Ala107]-MBP (104-118) Dilution Calculator
[Ala107]-MBP (104-118) Molarity Calculator
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Synthetic myelin basic protein peptide analogs are specific inhibitors of phospholipid/calcium-dependent protein kinase (protein kinase C).[Pubmed:2418828]
Biochem Biophys Res Commun. 1986 Jan 14;134(1):78-84.
Synthetic peptide analogs of the bovine myelin basic protein (MBP) corresponding to residues 104-118 were found to specifically inhibit phospholipid/ Ca2+-dependent protein kinase (protein kinase C). The peptides [Ala107]MBP (104-118) and [Ala113]MBP (104-118) inhibited protein phosphorylation of intact MBP, histone H1 and peptide phosphorylation with MBP(104-123), MBP(104-118) or [Ala105]MBP (104-118) as substrates. The inhibitor peptides [Ala107]MBP(104-118) and [Ala113]MBP (104-118), containing alanine in place of the arginine recognition sites, apparently inhibited the enzyme noncompetitively with respect to substrates, with IC50 values ranging from 46-145 and 28-62 microM, respectively. These peptide analogs did not inhibit cyclic AMP-dependent protein kinase or myosin light chain kinase but inhibited phospholipid/Ca2+-dependent phosphorylation of endogenous proteins in the total, solubilized fraction of rat brain.
Substrate specificity of phospholipid/Ca2+-dependent protein kinase as probed with synthetic peptide fragments of the bovine myelin basic protein.[Pubmed:2413012]
J Biol Chem. 1985 Sep 25;260(21):11503-7.
The substrate specificity of phospholipid/Ca2+-dependent protein kinase (protein kinase C) was studied using synthetic peptides, in particular those corresponding to the amino acid sequence around serine 115 in bovine myelin basic protein (MBP). It was found that MBP (104-118) and MBP (104-123) were substrates for the enzyme, with apparent Km values of 14 and 10 microM, respectively. Neither MBP (111-118) nor MBP (111-123) were phosphorylated, indicating that an additional segment of sequence extending toward the N terminus, but not toward the C terminus, was essential for the substrate activity of the peptides. Of the alanine-substituted analogs examined, [Ala 105] MBP (104-118) was comparable to the parent peptide, whereas [Ala 107] MBP (104-118) and [Ala 113] MBP-(104-118) were much poorer substrates. These findings indicated that lysine 105 was not essential, but both arginine 107 and arginine 113 were important specificity determinants. Initial studies revealed that [Ala 113] MBP (104-118) inhibited phosphorylation by the enzyme of the parent peptide and, to a lesser extent, the intact MBP(1-170). Serine 115 was the only site phosphorylated in the analog peptides [Ala 105] MBP (104-118) and [Ala 107]MBP (104-118). In the parent peptide, serine 115 was the initial site of phosphorylation but after prolonged phosphorylation other sites became phosphorylated (serine 110 and/or serine 112), further supporting the concept that arginine residues act as essential substrate specificity determinants for phospholipid/Ca2+-dependent protein kinase.
