Spermidine synthase Recombinant Protein | SRM recombinant protein

Recombinant Human Spermidine synthase

Cat. Num. AAA717224

• Gene Names: SRM; PAPT; SPS1; SPDSY; SRML1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Spermidine synthase; Recombinant Human Spermidine synthase; Putrescine aminopropyltransferase; SRM recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 17-302aa; Partial
• Sequence: REGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALNDVS
• Sequence Length: 302

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for SRM recombinant protein

Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extrely low activity towards spermidine.

Product Categories/Family for SRM recombinant protein

Metabolism

References

Human spermidine synthase cloning and primary structure.Wahlfors J., Alhonen L., Kauppinen L., Hyvoenen T., Jaenne J., Eloranta T.DNA Cell Biol. 9:103-110(1990) Human spermidine synthase gene structure and chromosomal localization.Myoehaenen S., Kauppinen L., Wahlfors J., Alhonen L., Jaenne J.DNA Cell Biol. 10:467-474(1991) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 63253298
• NCBI GeneID: 6723
• NCBI Accession #: NP_003123.2
• NCBI GenBank Nucleotide #: NM_003132.2
• UniProt Accession #: P19623; Q15511; B1AKP9
• Molecular Weight: 59.4 kDa
• NCBI Official Full Name: spermidine synthase
• NCBI Official Synonym Full Names: spermidine synthase
• NCBI Official Symbol: SRM
• NCBI Official Synonym Symbols: PAPT; SPS1; SPDSY; SRML1
• NCBI Protein Information: spermidine synthase
• UniProt Protein Name: Spermidine synthase
• Protein Family: Spermidine synthase
• UniProt Gene Name: SRM
• UniProt Synonym Gene Names: SPS1; SRML1; SPDSY
• UniProt Entry Name: SPEE_HUMAN

NCBI Description

The polyamines putrescine, spermine, and spermidine are ubiquitous polycationic mediators of cell growth and differentiation. Spermidine synthase is one of four enzymes in the polyamine-biosynthetic pathway and carries out the final step of spermidine biosynthesis. This enzyme catalyzes the conversion of putrescine to spermidine using decarboxylated S-adenosylmethionine as the cofactor. [provided by RefSeq, Jul 2008]

Uniprot Description

SRM: Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine. Belongs to the spermidine/spermine synthase family.

Protein type: Amino Acid Metabolism - cysteine and methionine; EC 2.5.1.16; Transferase; Amino Acid Metabolism - arginine and proline; Other Amino Acids Metabolism - glutathione; Other Amino Acids Metabolism - beta-alanine

Chromosomal Location of Human Ortholog: 1p36-p22

Cellular Component: cytosol

Molecular Function: protein binding; protein homodimerization activity; spermidine synthase activity

Biological Process: polyamine metabolic process; spermidine biosynthetic process