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pp60 c-src (521-533) (phosphorylated)

Inhibits tyrosine kinase activity of pp60c-src and pp60v-src CAS# 149299-77-4

pp60 c-src (521-533) (phosphorylated)

Catalog No. BCC5851----Order now to get a substantial discount!

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Chemical structure

pp60 c-src (521-533) (phosphorylated)

3D structure

Chemical Properties of pp60 c-src (521-533) (phosphorylated)

Cas No. 149299-77-4 SDF Download SDF
PubChem ID 16137939 Appearance Powder
Formula C62H95N16O28P M.Wt 1543.5
Type of Compound N/A Storage Desiccate at -20°C
Solubility Soluble to 1 mg/ml in water
Sequence TSTEPQYQPGENL

(Modifications: Tyr-7 = pTyr)

Chemical Name (2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[2-[[(2S)-1-[(2S)-5-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S,3R)-2-amino-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxybutanoyl]amino]-4-carboxybutanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-(4-phosphonooxyphenyl)propanoyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-4-carboxybutanoyl]amino]-4-oxobutanoyl]amino]-4-methylpentanoic acid
SMILES CC(C)CC(C(=O)O)NC(=O)C(CC(=O)N)NC(=O)C(CCC(=O)O)NC(=O)CNC(=O)C1CCCN1C(=O)C(CCC(=O)N)NC(=O)C(CC2=CC=C(C=C2)OP(=O)(O)O)NC(=O)C(CCC(=O)N)NC(=O)C3CCCN3C(=O)C(CCC(=O)O)NC(=O)C(C(C)O)NC(=O)C(CO)NC(=O)C(C(C)O)N
Standard InChIKey QTTDEIYNMOIHBO-VVTMTNTLSA-N
Standard InChI InChI=1S/C62H95N16O28P/c1-28(2)23-39(62(101)102)74-54(93)38(25-45(65)84)73-51(90)33(15-19-47(86)87)68-46(85)26-67-56(95)41-7-5-21-77(41)60(99)35(14-18-44(64)83)70-53(92)37(24-31-9-11-32(12-10-31)106-107(103,104)105)72-52(91)34(13-17-43(63)82)69-57(96)42-8-6-22-78(42)61(100)36(16-20-48(88)89)71-59(98)50(30(4)81)76-55(94)40(27-79)75-58(97)49(66)29(3)80/h9-12,28-30,33-42,49-50,79-81H,5-8,13-27,66H2,1-4H3,(H2,63,82)(H2,64,83)(H2,65,84)(H,67,95)(H,68,85)(H,69,96)(H,70,92)(H,71,98)(H,72,91)(H,73,90)(H,74,93)(H,75,97)(H,76,94)(H,86,87)(H,88,89)(H,101,102)(H2,103,104,105)/t29-,30-,33+,34+,35+,36+,37+,38+,39+,40+,41+,42+,49+,50+/m1/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 pp60 c-src (521-533) (phosphorylated)

DescriptionPeptide corresponding to the pp60c-src carboxy terminal regulatory domain; phosphorylated at Tyr527. Binds to pp60c-src and pp60v-src at the SH2 domain, suppressing their tyrosine kinase activity and transforming potential.

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References on pp60 c-src (521-533) (phosphorylated)

Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) using synthetic phosphopeptides.[Pubmed:8135747]

Biochem J. 1994 Mar 1;298 ( Pt 2):395-401.

The intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) (44 kDa) was expressed in bacteria, purified using epitope 'tagging' immunoaffinity chromatography, and characterized with respect to kinetic profile, substrate specificity and potential modulators of enzyme activity. A chromogenic assay based on the Malachite Green method was employed for the detection of inorganic phosphate (Pi) released from phosphopeptides by HPTP beta. This assay, modified so as to improve its sensitivity, was adapted to a 96-well microtitre plate format, and provided linear detection between 50 and 1000 pmol of Pi. The cytoplasmic domain of HPTP beta was strongly inhibited by vanadate, molybdate, heparin, poly(Glu, Tyr) (4:1) and zinc ions. In order to explore the substrate preferences of this PTPase, we generated 13-residue synthetic phosphotyrosine-containing peptides that corresponded to sites of physiological tyrosine phosphorylation. HPTP beta demonstrated kcat. values between 76 and 258 s-1 using four different phosphopeptides. The substrate preference of HPTP beta was in the order srcTyr-527 > PDGF-RTyr-740 > ERK1Tyr-204 >> CSF-1RTyr-708 with Km values ranging from 140 microM to greater than 10 mM. The variations in affinity were probably due to differences among the four phosphopeptides compared, particularly with respect to the character of the charged amino acids flanking the phosphotyrosine residue.

Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src.[Pubmed:1720546]

Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10696-700.

Phosphorylation of the carboxyl terminus of pp60c-src, the product of the c-src protooncogene, at Tyr-527 suppresses its tyrosine kinase activity and transforming potential. It has been proposed that the phosphorylated carboxyl terminus of pp60c-src inhibits kinase activity by binding to the SH2 (src homology 2) domain. We have synthesized peptides corresponding to the carboxyl-terminal 13 residues of pp60c-src phosphorylated and nonphosphorylated at Tyr-527. A highly transforming mutant, pp60c-src(F527), in which Tyr-527 is mutated to Phe, bound to the phosphorylated peptide immobilized to Affi-Gel 10. Binding of the phosphorylated peptide was abolished by deletion of residues 144-175 in the SH2 domain but not by deletion of residues 93-143, which removes most of the SH3 domain. The phosphorylated peptide also bound to pp60v-src, the transforming protein of Rous sarcoma virus. Only traces of pp60v-src and pp60c-src(F527) bound to the corresponding nonphosphorylated c-src peptide. Normal pp60c-src bound much less efficiently to the phosphorylated peptide than did pp60c-src(F527). A phosphorylated peptide corresponding to the carboxyl terminus of the c-fgr protein also bound to pp60c-src(F527), but with weaker affinity. Furthermore, the phosphorylated synthetic carboxyl-terminal pp60c-src peptide markedly inhibited phosphorylation of pp60c-src(F527) during cytoskeletal kinase assays. These results provide direct evidence for models in which the phosphorylated carboxyl terminus of pp60c-src binds intramolecularly or intermolecularly to the SH2 domain of the c-src protein.

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