CALP1

CAS# 145224-99-3

CALP1

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Chemical structure

CALP1

3D structure

Chemical Properties of CALP1

Cas No. 145224-99-3 SDF Download SDF
PubChem ID 10440555 Appearance Powder
Formula C40H75N9O10 M.Wt 842.09
Type of Compound N/A Storage Desiccate at -20°C
Solubility Soluble to 1 mg/ml in sterile water
Chemical Name (2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]propanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-3-methylbutanoyl]amino]hexanoic acid
SMILES CCC(C)C(C(=O)NC(C(C)O)C(=O)NC(C(C)C)C(=O)NC(CC(C)C)C(=O)NC(C(C)C)C(=O)NC(CCCCN)C(=O)O)NC(=O)C(C)NC(=O)C(C(C)C)N
Standard InChIKey HTOHLCKNMRKYLK-KVZSNLRASA-N
Standard InChI InChI=1S/C40H75N9O10/c1-13-23(10)31(48-33(51)24(11)43-35(53)28(42)20(4)5)38(56)49-32(25(12)50)39(57)47-30(22(8)9)37(55)45-27(18-19(2)3)34(52)46-29(21(6)7)36(54)44-26(40(58)59)16-14-15-17-41/h19-32,50H,13-18,41-42H2,1-12H3,(H,43,53)(H,44,54)(H,45,55)(H,46,52)(H,47,57)(H,48,51)(H,49,56)(H,58,59)/t23-,24-,25+,26-,27-,28-,29-,30-,31-,32-/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.
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.
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.

Biological Activity of CALP1

DescriptionCell-permeable calmodulin (CaM) agonist that binds to the EF-hand/Ca2+-binding site; produces CaM-dependent activation of phosphodiesterase. Also binds to cytoplasmic sites on other Ca2+ channels, including NMDA and HIV-1 gp120-activated channels, inhibiting Ca2+-mediated cytotoxicity and apoptosis (IC50 = 52 μM). Shown to protect pancreatic acinar cells from gossypol (Cat.No. 1964) induced necrosis. Inhibits VLA-5-mediated adhesion of mast cells to fibronectin in vitro and attenuates inflammatory cell influx in guinea pig lung in vivo.

CALP1 Dilution Calculator

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Preparing Stock Solutions of CALP1

1 mg 5 mg 10 mg 20 mg 25 mg
1 mM 1.1875 mL 5.9376 mL 11.8752 mL 23.7504 mL 29.688 mL
5 mM 0.2375 mL 1.1875 mL 2.375 mL 4.7501 mL 5.9376 mL
10 mM 0.1188 mL 0.5938 mL 1.1875 mL 2.375 mL 2.9688 mL
50 mM 0.0238 mL 0.1188 mL 0.2375 mL 0.475 mL 0.5938 mL
100 mM 0.0119 mL 0.0594 mL 0.1188 mL 0.2375 mL 0.2969 mL
* Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations.

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References on CALP1

The Ca(v)3.1 T-type calcium channel is required for neointimal formation in response to vascular injury in mice.[Pubmed:22886848]

Cardiovasc Res. 2012 Dec 1;96(3):533-42.

AIMS: Restenosis is an undesirable consequence following percutaneous vascular interventions. However, the current strategy for preventing restenosis is inadequate. The aim of this study was to investigate the role of low-voltage gated T-type calcium channels in regulating vascular smooth muscle cell (VSMC) proliferation during neointimal formation. METHODS AND RESULTS: Wire injury of mice carotid arteries resulted in neointimal formation in the wild-type and Ca(v)3.2(-/-) but not Ca(v)3.1(-/-) mice, indicating a critical role of Ca(v)3.1 in neointimal formation. In addition, we found a significant increase of Ca(v)3.1 mRNA and protein in injured arteries. Ca(v)3.1 knockout or knockdown (shCa(v)3.1) reduced VSMC proliferation. Since T-channels are expressed predominantly in the G(1) and S phases in VSMCs, we examined whether an abnormal G(1)/S transition was the cause of the reduced cell proliferation in shCa(v)3.1 VSMCs. We found a disrupted expression of cyclin E in shCa(v)3.1 VSMCs, and calmodulin agonist CALP1 partially rescued the defective cell proliferation. Furthermore, we demonstrated that infusion of NNC55-0396, a selective T-channel blocker, inhibited neointimal formation in wild-type mice. CONCLUSION: Ca(v)3.1 is required for VSMC proliferation during neointimal formation, and blocking of Ca(v)3.1 may be beneficial for preventing restenosis.

Functional characterization of the calcipressin 1 motif that suppresses calcineurin-mediated NFAT-dependent cytokine gene expression in human T cells.[Pubmed:16406492]

Cell Signal. 2006 Sep;18(9):1430-8.

Inhibition of the calcineurin-NFAT signalling pathway is one of the main challenges for immunosuppression therapy to avoid the severe side effects of the current anticalcineurinic drugs, cyclosporin A and FK506. The members of the calcipressin family are endogenous inhibitors of calcineurin. We describe for the first time that two independent motifs within human calcipressin 1, the ELHA and the PxIxxT motifs, interact with calcineurin in an independent functional manner. However, the main finding here is that the ELHA-containing calcineurin-inhibitor CALP1 (CIC) motif is the responsible for the in vivo inhibition of calcineurin-mediated NFAT-dependent cytokine gene expression in human T cells. We believe that the identification of the CIC motif could be used as a starting point for the development of new immunosuppressive drugs for use in transplantation and autoimmune diseases.

Ca2+ sensors modulate asthmatic symptoms in an allergic model for asthma.[Pubmed:12969760]

Eur J Pharmacol. 2003 Aug 22;476(1-2):151-7.

We previously described two novel peptides, Ca2+-like peptide (CALP) 1 and CALP2, which interact with Ca2+-binding EF hand motifs, and therefore have the characteristics to define the role of the Ca2+-sensing regulatory protein calmodulin in asthma. In the present study, the effects of the calcium-like peptides were investigated in an animal model for allergic asthma. For that purpose, sensitized guinea pigs were intratracheally pretreated with CALP1 or CALP2. Thirty minutes later, the animals were challenged with aerosolized ovalbumin. Acute bronchoconstriction was measured as well as characteristic features of asthma 6 and 24 hours (h) after challenge. Neither CALP1 nor CALP2 prevented the anaphylactic response elicited by ovalbumin challenge. However, CALP1 pretreatment attenuated the influx of inflammatory cells in the lungs 6 h after challenge. Furthermore, radical production by these cells was diminished both 6 and 24 h after challenge. Moreover, CALP1 completely inhibited airway hyperresponsiveness in vitro 24 h after challenge. We conclude that CALP1, as a selective calmodulin agonist, inhibits the development of asthmatic features probably via the attenuation of mast cell degranulation and radical production. Specific modulation of calmodulin activity might therefore be a potential new target for the treatment of allergic asthma.

Cloning, localization, and axonemal function of Tetrahymena centrin.[Pubmed:12529441]

Mol Biol Cell. 2003 Jan;14(1):251-61.

Centrin, an EF hand Ca(2+) binding protein, has been cloned in Tetrahymena thermophila. It is a 167 amino acid protein of 19.4 kDa with a unique N-terminal region, coded by a single gene containing an 85-base pair intron. It has > 80% homology to other centrins and high homology to Tetrahymena EF hand proteins calmodulin, TCBP23, and TCBP25. Specific cellular localizations of the closely related Tetrahymena EF hand proteins are different from centrin. Centrin is localized to basal bodies, cortical fibers in oral apparatus and ciliary rootlets, the apical filament ring and to inner arm (14S) dynein (IAD) along the ciliary axoneme. The function of centrin in Ca(2+) control of IAD activity was explored using in vitro microtubule (MT) motility assays. Ca(2+) or the Ca(2+)-mimicking peptide CALP1, which binds EF hand proteins in the absence of Ca(2+), increased MT sliding velocity. Antibodies to centrin abrogated this increase. This is the first demonstration of a specific centrin function associated with axonemal dynein. It suggests that centrin is a key regulatory protein for Tetrahymena axonemal Ca(2+) responses, including ciliary reversal or chemotaxis.

Attenuation of very late antigen-5-mediated adhesion of bone marrow-derived mast cells to fibronectin by peptides with inverted hydropathy to EF-hands.[Pubmed:11145661]

J Immunol. 2001 Jan 15;166(2):861-7.

Release of allergic mediators from mast cells is enhanced by very late Ag (VLA)-5-mediated interaction of these cells with fibronectin. In this report, we show that VLA-5-mediated adhesion of bone marrow-derived mast cells to fibronectin can be induced by two different pathways: first, FcepsilonRI clustering, which depends on calmodulin activation and extracellular Ca(2+), and, second, by Mn(2+) stimulation, which is independent of calmodulin activation and antagonized by Ca(2+). Previous studies have shown the presence of several cation-binding domains in VLA-5 that are homologous to the calcium-binding EF-hands of calmodulin. To show a role for EF-hands of different proteins in VLA-5-mediated adhesion, we used calcium-like peptides (CALP), CALP1 and CALP2, designed to bind to EF-hands based on inverted hydropathy. CALP1 and, more potently, CALP2 inhibited FcepsilonRI-induced adhesion to fibronectin via different mechanisms. The target for the effects of CALP1 and 2 on FcepsilonRI-induced adhesion and degranulation was intracellular and likely involved calmodulin. Interestingly only CALP2 was able to inhibit Mn(2+)-induced calmodulin-independent adhesion by interfering with an extracellular target, which is probably VLA-5. We conclude that CALP1 and 2 can inhibit VLA-5-mediated adhesion of mast cells to fibronectin through binding to EF-hands of multiple proteins, and that these peptides can be used as lead compounds for the development of future therapy against allergy.

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