SRM

  • Official Full Name

    spermidine synthase
  • Overview

    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.
  • Synonyms

    SRM;spermidine synthase;SRML1;SPS1;OTTHUMP00000002170;PAPT;Putrescine aminopropyltransferase;SPDSY;SPEE_HUMAN;Spermidine synthase 1;spermidine synthase-1

Recombinant Proteins

  • Human
  • Zebrafish
  • Rhesus macaque
  • Mouse
  • E.coli
  • Mammalian Cells
  • HEK293
  • GST
  • His
  • Non
  • Flag
  • Avi&Fc&His
  • DDK&Myc
Cat.# Product name Source (Host) Species Tag Protein Length Price
SRM-2954H Recombinant Human SRM, GST-tagged E.coli Human GST 1-302aa
SRM-11266Z Recombinant Zebrafish SRM Mammalian Cells Zebrafish His
SRM-30397TH Recombinant Human SRM, His-tagged E.coli Human His 302 amino acids
SRM-4466R Recombinant Rhesus monkey SRM Protein, His-tagged Mammalian Cells Rhesus macaque His
SRM-805H Recombinant Human Spermidine Synthase, His-tagged E.coli Human His
SRM-1479HCL Recombinant Human SRM 293 Cell Lysate HEK293 Human Non
SRM-1642HFL Recombinant Full Length Human SRM Protein, C-Flag-tagged Mammalian Cells Human Flag Full L.
SRM-2098H Recombinant Human SRM Protein, His (Fc)-Avi-tagged HEK293 Human Avi&Fc&His
SRM-2098H-B Recombinant Human SRM Protein Pre-coupled Magnetic Beads HEK293 Human
SRM-2735H Recombinant Human SRM Protein, His-tagged E.coli Human His Glu18-Ser302
SRM-4282R Recombinant Rhesus Macaque SRM Protein, His (Fc)-Avi-tagged HEK293 Rhesus macaque Avi&Fc&His
SRM-4282R-B Recombinant Rhesus Macaque SRM Protein Pre-coupled Magnetic Beads HEK293 Rhesus macaque
SRM-5155H Recombinant Human SRM protein, GST-tagged E.coli Human GST 17-302aa
Srm-6127M Recombinant Mouse Srm Protein, Myc/DDK-tagged HEK293 Mouse DDK&Myc

    Involved Pathway

    SRM involved in several pathways and played different roles in them. We selected most pathways SRM participated on our site, such as Cysteine and methionine metabolism,Arginine and proline metabolism,beta-Alanine metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with SRM were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Arginine and proline metabolism ALDH18A1,ALDH2.2,DHDPSL,PRODH2,CKMT1A,GATM,LAP3,ADC,ALDH9A1,ALDH9A1B
    Metabolic pathways ATP6V1AA,GPI,NDUFA12,UCK2B,SYNJ2,GBGT1,CYP2C55,COX6B2,INPP5K,GCDHA
    beta-Alanine metabolism ALDH2.2,ALDH3A2A,ALDH3B1,MLYCD,AOC3,HADHAB,ALDH9A1A.1,ALDH7A1,GAD2,HADHA
    Glutathione metabolism GPX5,GGCTB,GGCTA,OPLAH,GSTT1B,GSTAL,LAP3,GPX4A,GPX2,G6PD
    Cysteine and methionine metabolism CTH,TAT,GOT1,MAT2AL,AMD1,AGXT2,TST,MAT2AA,DNMT3B,AHCYL2

    Protein Function

    SRM has several biochemical functions, for example, protein binding,protein homodimerization activity,spermidine synthase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by SRM itself. We selected most functions SRM had, and list some proteins which have the same functions with SRM. You can find most of the proteins on our site.

    Function Related Protein
    protein homodimerization activity ADRA2A,CSF1,MBL1,IDE,S100A13,PLD6,GYS2,DARS2,P2RX7,WHRN
    protein binding AGAP2,INTS3,ING2,PSMA6,SMUG1,PXMP4,EPAS1,SEPT6,ACLY,SH2D3C

    Interacting Protein

    SRM has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SRM here. Most of them are supplied by our site. Hope this information will be useful for your research of SRM.

    VCAM1;TERF1;DMWD;IKBKE;DDA1;SOX12

    Resources

    References

    • Such-Sanmartin, G; Bache, N; et al. Detection and differentiation of 22 kDa and 20 kDa Growth Hormone proteoforms in human plasma by LC-MS/MS. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1854:284-290(2015).
    • Porta, T; Lesur, A; et al. Quantification in MALDI-MS imaging: what can we learn from MALDI-selected reaction monitoring and what can we expect for imaging?. ANALYTICAL AND BIOANALYTICAL CHEMISTRY 407:2177-2187(2015).

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