protein

Recombinant Human Dermcidin

MBS952054

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Dermcidin

Dermcidin

Preproteolysin

dermcidin isoform 2 preproprotein; Dermcidin; dermcidin; dermcidin; Preproteolysin

DCD

DCD; DCD; PIF; AIDD; DSEP; HCAP; DCD-1; AIDD; DSEP

DCD_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

20-110, Full length.

110

YDPEAASAPGSGNPCHEASAAQKENAGEDPGLARQAPKP
RKQRSSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKG
AVHDVKDVLDSVL

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Signal Transduction

DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E Coli, E. faecalis, S. aureus and C. albicans. Optimal pH and salt concentration resble the conditions in sweat. Also exhibits proteolytic activity. Survival-promoting peptide promotes survival of neurons and displays phosphatase activity. It may bind IgG.

Dermcidin a novel human antibiotic peptide secreted by sweat glands.Schittek B., Hipfel R., Sauer B., Bauer J., Kalbacher H., Stevanovic S., Schirle M., Schroeder K., Blin N., Meier F., Rassner G., Garbe C.Nat. Immunol. 2:1133-1137(2001) Overexpression of new survival/evasion peptide (DSEP) attenuates retinoic acid responses and protects cells.Cunningham T.J., Jing H., Akerblom I., Morgan R., Fisher T.S., Neveu M.Genomic structure and chromosomal mapping of human preproteolysin gene.Tang X.D., Daggett H., Hoshi T.Structural and functional homologies of human proteolysis inducing factor.Lowrie A.G., Wigmore S.J., Deans D.A.C., Fearon K.C.H., Waddell I., Ross J.A.Identification of dermcidin in human gestational tissue and characterization of its proteolytic activity.Lee Motoyama J.P., Kim-Motoyama H., Kim P., Nakagama H., Miyagawa K., Suzuki K.Biochem. Biophys. Res. Commun. 357:828-833(2007) The finished DNA sequence of human chromosome 12.Baylor College of Medicine Human Genome Sequencing Center Sequence Production TeamScherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Identification of a survival-promoting peptide in medium conditioned by oxidatively stressed cell lines of nervous system origin.Cunningham T.J., Hodge L., Speicher D., Reim D., Tyler-Polsz C., Levitt P., Eagleson K., Kennedy S., Wang Y.J. Neurosci. 18:7047-7060(1998) Signal peptide prediction based on analysis of experimentally verified cleavage sites.Zhang Z., Henzel W.J.Protein Sci. 13:2819-2824(2004) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles.Jung H.H., Yang S.T., Sim J.Y., Lee S., Lee J.Y., Kim H.H., Shin S.Y., Kim J.I.BMB Rep. 43:362-368(2010)

665505971

NP_001287783.1

NM_001300854.1

P81605

36.7kD

This antimicrobial gene encodes a secreted protein that is subsequently processed into mature peptides of distinct biological activities. The C-terminal peptide is constitutively expressed in sweat and has antibacterial and antifungal activities. The N-terminal peptide, also known as diffusible survival evasion peptide, promotes neural cell survival under conditions of severe oxidative stress. A glycosylated form of the N-terminal peptide may be associated with cachexia (muscle wasting) in cancer patients. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2014]

DCD: DCD-1 displays antimicrobial activity thereby limiting skin infection by potential pathogens in the first few hours after bacterial colonization. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Secreted; Secreted, signal peptide; EC 3.4.-.-. Chromosomal Location of Human Ortholog: 12q13.1. Cellular Component: extracellular region; extracellular space. Molecular Function: peptidase activity; protein binding. Biological Process: defense response to bacterium; defense response to fungus; killing of cells of another organism; proteolysis

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750