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Detail of "99287-08-8"

  • CAS Number:
  • 99287-08-8
  • Name:
  • L-Cysteine,L-alanyl-L-cysteinyl-L-tyrosyl-L-cysteinyl-L-arginyl-L-isoleucyl-L-prolyl-L-alanyl-L-cysteinyl-L-isoleucyl-L-alanylglycyl-L-a-glutamyl-L-arginyl-L-arginyl-L-tyrosylglycyl-L-threonyl-L-cysteinyl-L-isoleucyl-L-tyrosyl-L-glutaminylglycyl-L-arginyl-L-leucyl-L-tryptophyl-L-alanyl-L-phenylalanyl-L-cysteinyl-

  • Molecular Structure:
  • Formula:
  • C150H228 N44 O38 S6
  • Molecular Weight:
  • 3442.03
  • Synonyms:
  • DefensinNP 1 (human reduced); 10: PN: US6545140 SEQID: 47 unclaimed sequence; 11: PN:US20050107325 SEQID: 11 unclaimed sequence; 11: PN: US20050233342 SEQID: 34unclaimed sequence; 11: PN: US20090163705 SEQID: 11 unclaimed sequence; 11: PN:WO2004094345 SEQID: 11 unclaimed sequence; 11: PN: WO2004094595 SEQID: 11unclaimed sequence; 11: PN: WO2007022470 SEQID: 41 unclaimed sequence; 120: PN:WO2008058016 SEQID: 121 claimed protein; 13: PN: WO2007022506 SEQID: 41unclaimed sequence; 17: PN: WO2004090551 SEQID: 17 claimed sequence; 188: PN:US20090238811 SEQID: 75 unclaimed protein; 18: PN: WO2004090108 SEQID: 17unclaimed sequence; 19: PN: WO2008140582 SEQID: 3 unclaimed protein; 1: PN:EP1624074 SEQID: 1 unclaimed sequence; 1: PN: WO2004003195 SEQID: 2 unclaimedsequence; 1: PN: WO2004092332 PAGE: 8 unclaimed sequence; 21: PN: WO2005082399SEQID: 20 unclaimed sequence; 22: PN: WO2009120878 PAGE: 58 unclaimed sequence;22: PN: WO2010006237 PAGE: 18 unclaimed sequence; 25: PN: US20050256069 SEQID:11 unclaimed sequence; 25: PN: WO2009142822 TABLE: 4 unclaimed sequence; 28:PN: WO2008123948 SEQID: 8 unclaimed protein; 2: PN: WO03070176 SEQID: 2 claimedsequence; 2: PN: WO2006084131 SEQID: 1 unclaimed sequence; 2: PN: WO2007000584SEQID: 2 unclaimed sequence; 3476: PN: WO2004091515 SEQID: 6710 unclaimedprotein; 35: PN: US20020035061 TABLE: 1 unclaimed sequence; 38: PN:US20060147442 SEQID: 38 unclaimed sequence; 38: PN: WO2004110143 SEQID: 38unclaimed sequence; 38: PN: WO2007047189 SEQID: 38 unclaimed sequence; 39: PN:WO0209738 SEQID: 38 claimed sequence; 3: PN: CN1810954 PAGE: 8 unclaimedsequence; 3: PN: WO03101394 SEQID: 3 unclaimed sequence; 3: PN: WO2004074807SEQID: 3 unclaimed sequence; 3: PN: WO2006128082 SEQID: 1 unclaimed sequence;40: PN: US20050186591 SEQID: 41 unclaimed sequence; 40: PN: US20070104722SEQID: 38 unclaimed sequence; 417: PN: WO0069900 SEQID: 1103 unclaimedsequence; 41: PN: US20070161595 SEQID: 41 unclaimed sequence; 41: PN:WO2005004794 SEQID: 41 unclaimed sequence;
  • Appearance:
  • White Powder

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CAS No.99287-08-8 HUMAN NEUTROPHIL PEPTIDE-1

storage temp. : ?20°C WGK Germany : 3

Supplier:PEPROTECH [ United States]

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Reference

Direct inactivation of viruses by human granulocyte defensins
Direct inactivation of viruses by human granulocyte defensins. Daher, Kathleen A.; Selsted, Michael E.; Lehrer, Robert I. (Cent.In this study, 99287-07-7 and 99287-08-8 are also used. Health Sci., Univ. California Los Angeles, Los Angeles, CA 90024, USA). J. Virol., 60(3), 1068-74 (English) 1986. CODEN: JOVIAM. ISSN: 0022-538X. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) Human neutrophils contain a family of microbicidal peptides known as defensins. One of these defensins, human neutrophil peptide (HNP)-1, was purified, and its ability to directly inactivate several viruses was extensively tested. Herpes simplex virus (HSV) types 1 and 2, cytomegalovirus, vesicular stomatitis virus, and influenza virus A/WSN were inactivated by incubation with HNP-1. Two nonenveloped viruses, echovirus type 11 and reovirus type 3, were resistant to inactivation. Purified homologous peptides HNP-2 and HNP-3 had HSV-1-neutralizing activities approx. equal to that of HNP-1. Inactivation of HSV-1 by HNP-1 depended on the time, temp., and pH of incubation. Antiviral activity was abrogated by low temp. or prior redn. and alkylation of the defensins. Addn. of serum or serum albumin to the incubation mixts. inhibited neutralization of HSV-1 by HNP-1. D. gradient sedimentation techniques were used to demonstrate that HNP-1 bound to HSV-1 in a temp.-dependent manner. Binding of defensin peptides to certain viruses may impair their ability to infect cells. .
The levels and biologic action of the human neutrophil granule peptide HP-1 in lung tumors
The levels and biologic action of the human neutrophil granule peptide HP-1 in lung tumors. Bateman, Andrew; Singh, Ava; Jothy, Serge; Fraser, Richard; Esch, Fred; Solomon, Samuel (Dep. Med., R. Victoria Hosp., Montreal, PQ H3A 1A1, Can.). Peptides (Fayetteville, N. Y.), 13(1), 133-9 (English) 1992. CODEN: PPTDD5. ISSN: 0196-9781. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) HP-1 is the most abundant human representative of a recently discovered class of neutrophil cystine- and arginine-rich peptides. These peptides have many potentially regulatory activities expressed at nanomolar concns. To establish the levels of HP-1 that can accumulate in human lung tumors and nondiseased lung fragments, tissues were extd. for their peptide content. The exts. were purified on reverse phase HPLC, and HP-1 and related peptides were identified by sequence anal. and their concns. in the tissue quantitated by amino acid anal. Immunohistochem. was performed and strongly suggests that HP-1 is confined to granulocytes under most circumstances, and indicates that the levels of HP-1 measured in the tumors reflect the levels obtained when solid tissue is infiltrated by neutrophils. The max. obsd. levels were 26 nmol per g wet wt. of tissue. Attempts were then made to correlate this level to the cytotoxic potential of HP-1 by performing in vitro cytotoxicity dose-response curves on several cell lines. Most cells were killed at between 1 and 8 mM, and the response depended on the growth conditions of the cells. 99287-08-8 is just another one chemical used in this study. The levels of HP-1 that accumulate in tumors can exceed the in vitro cytolytic concns. The levels are also considerably in excess of those required to exert in vitro regulatory actions. .
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