H-Phe-Asp-OH
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H-Phe-Asp-OH

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Category
Others
Catalog number
BAT-015439
CAS number
22828-05-3
Molecular Formula
C13H16N2O5
Molecular Weight
280.28
H-Phe-Asp-OH
IUPAC Name
(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]butanedioic acid
Synonyms
Phenylalanyl-aspartic acid; L-phenylalanyl-L-aspartic acid; FD dipeptide; L-Phe-L-Asp
Purity
95%
Density
1.371±0.06 g/cm3
Melting Point
227-229°C
Boiling Point
552.0±50.0 °C at 760 mmHg
Sequence
H-Phe-Asp-OH
Storage
Store at -20°C
InChI
InChI=1S/C13H16N2O5/c14-9(6-8-4-2-1-3-5-8)12(18)15-10(13(19)20)7-11(16)17/h1-5,9-10H,6-7,14H2,(H,15,18)(H,16,17)(H,19,20)/t9-,10-/m0/s1
InChI Key
HWMGTNOVUDIKRE-UWVGGRQHSA-N
Canonical SMILES
C1=CC=C(C=C1)CC(C(=O)NC(CC(=O)O)C(=O)O)N
1. Amino acid sequence of bovine brain derived class 1 heparin-binding growth factor
D J Strydom, J W Harper, R R Lobb Biochemistry. 1986 Mar 11;25(5):945-51. doi: 10.1021/bi00353a001.
The major class 1 heparin-binding growth factor from bovine brain is a single-chain polypeptide of 140 amino acids with a molecular weight of 15 877. It has the amino acid sequence Phe1-Asn-Leu-Pro-Leu-Gly-Asn-Tyr-Lys-Lys-Pro-Lys-Leu-Leu- Tyr15-Cys-Ser- Asn-Gly-Gly-Tyr-Phe-Leu-Arg-Ile-Leu-Pro-Asp-Gly-Thr30-Val-Asp-Gly- Thr-Lys-Asp-Arg- Ser-Asp-Gln-His-Ile-Gln-Leu-Gln45-Leu-Cys-Ala-Glu-Ser-Ile-Gly- Glu-Val-Tyr-Ile- Lys-Ser-Thr-Glu60-Thr-Gly-Gln-Phe-Leu-Ala-Met-Asp-Thr-Asp-Gly- Leu-Leu-Tyr-Gly75- Ser-Gln-Thr-Pro-Asn-Glu-Glu-Cys-Leu-Phe-Leu-Glu-Arg-Leu- Glu90-Glu-Asn-His-Tyr- Asn-Thr-Tyr-Ile-Ser-Lys-Lys-His-Ala-Glu-Lys105-His-Trp-Phe-Val -Gly-Leu-Lys-Lys- Asn-Gly-Arg-Ser-Lys-Leu-Gly120-Pro-Arg-Thr-His-Phe-Gly-Gln-Lys -Ala-Ile-Leu-Phe-Leu-Pro-Leu135-Pro-Val-Ser-Ser-Asp140-OH. The mitogen is homologous to the class 2 heparin-binding growth factor pituitary fibroblast growth factor with about 50% of the amino acids being identical between the two mitogens.
2. Amino acid sequence of human tumor derived angiogenin
D J Strydom, J W Fett, R R Lobb, E M Alderman, J L Bethune, J F Riordan, B L Vallee Biochemistry. 1985 Sep 24;24(20):5486-94. doi: 10.1021/bi00341a031.
The amino acid sequence and disulfide bond pairing of human tumor derived angiogenin, the first tumor angiogenesis factor to be isolated in pure form from human sources, have been determined by conventional sequencing techniques adapted and applied to nanomole and subnanomole levels of material. Angiogenin, obtained from conditioned media of a human colonic adenocarcinoma cell line, is a single-chain protein consisting of 123 amino acids with the following sequences: less than Glu1-Asp-Asn-Ser-Arg-Tyr-Thr-His- Phe-Leu-Thr-Gln-His-Tyr-Asp15-Ala-Lys-Pro-Gln-Gly-Arg-Asp-Asp- Arg-Tyr-Cys-Glu-Ser-Ile-Met30- Arg-Arg-Arg-Gly-Leu-Thr-Ser-Pro-Cys-Lys-Asp-Ile-Asn-Thr- Phe45-Ile-His-Gly-Asn-Lys-Arg-Ser -Ile-Lys-Ala-Ile-Cys-Glu-Asn-Lys60-Asn-Gly-Asn-Pro-His-Arg-Glu-Asn -Leu-Arg-Ile -Ser-Lys-Ser-Ser75 -Phe-Gln-Val-Thr-Thr-Cys-Lys-Leu-His-Gly-Gly-Ser-Pro-Trp-Pro90-Pro -Cys-Gln-Tyr -Arg-Ala-Thr-Ala -Gly-Phe-Arg-Asn-Val-Val-Val105-Ala-Cys-Glu-Asn-Gly-Leu-Pro-Val- His-Leu-Asp-Gln-Ser-Ile-Phe120-Arg-Arg-Pro123-OH. Three disulfide bonds link the half-cystinyl residues 26-81, 39-92, and 57-107. The sequence is homologous to that of the pancreatic ribonucleases with 35% identity and many of the remaining residues conservatively replaced. Similarities are especially apparent around the major active-site residues His-12, Lys-41, and His-119 of ribonuclease which are conserved as are three of the four disulfide bonds.(ABSTRACT TRUNCATED AT 250 WORDS)
3. Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases
W Ardelt, S M Mikulski, K Shogen J Biol Chem. 1991 Jan 5;266(1):245-51.
Rana pipiens oocytes and early embryos contain large amounts of a basic protein with antiproliferative/cytotoxic activity against several tumor cell lines in vitro (Darzynkiewicz, Z., Carter, S. P., Mikulski, S. M., Ardelt, W., and Shogen, K. (1988) Cell Tissue Kinet. 21, 169-182; Mikulski, S.M., Viera, A., Ardelt, W., Menduke, H., and Shogen, K. (1990) Cell Tissue Kinet. 23, 237-246), as well as antitumor activity in vivo (Mikulski, S. M., Ardelt, W., Shogen, K., Bernstein, E. H., and Menduke, H. (1990) J. Natl. Cancer Inst. 82, 151-153). The protein, provisionally named P-30 Protein, was purified to homogeneity from early embryos and characterized. It is a single-chain protein consisting of 104 amino acid residues in the following sequence: less than Glu1-Asp-Trp-Leu-Thr-Phe-Gln-Lys-Lys-His-Ile-Thr-Asn-Thr- Arg15-Asp-Val-Asp-Cys-Asp-Ans-Ile-Met-Ser-Thr-Asn-Leu-Phe-His-C ys30-Lys-Asp-Lys - Asn-Thr-Phe-Ile-Tyr-Ser-Arg-Pro-Glu-Pro-Val-Lys45-Ala-Ile-Cys-Lys- Gly-Ile-Ile- Ala-Ser-Lys-Asn-Val-Leu-Thr-Thr60-Ser-Glu-Phe-Tyr-Leu-Ser-Asp -Cys-Asn-Val-Thr-Ser-Arg-Por-Cys75-Lys-Tyr-Lys-Leu-Lys-Lys-Ser-Thr -Asn-Lys-Phe- Cys-Val-Thr-Cys90-Glu-Asn-Gln-Ala-Pro-Val-His-Phe-Val-Gly-Val-Gly- Ser-Cys104-OH . Its molecular weight calculated from the sequence is 11,819. The sequence homology clearly indicates that the protein belongs to the superfamily of pancreatic ribonuclease. It is also demonstrated that it indeed exhibits a ribonucleolytic activity against highly polymerized RNA and that this activity seems to be essential for its antiproliferative/cytotoxic effects.
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