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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
  • Cell & Tissue Lysates
  • Protein Pre-coupled Magnetic Beads
  • Human
  • Mouse
  • Rhesus Macaque
  • Zebrafish
  • E.coli
  • HEK293
  • HEK293T
  • Mammalian Cell
  • Mammalian cells
  • Flag
  • GST
  • His
  • His (Fc)
  • Avi
  • Myc
  • DDK
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human SRM-805H Recombinant Human Spermidine Synthase, His-tagged E.coli His
Human SRM-2954H Recombinant Human SRM, GST-tagged E.coli GST 1-302aa
Human SRM-30397TH Recombinant Human SRM, His-tagged E.coli His 302 amino acids
Human SRM-1479HCL Recombinant Human SRM 293 Cell Lysate HEK293 N/A
Human SRM-2735H Recombinant Human SRM Protein, His-tagged E.coli N-His Glu18-Ser302
Human SRM-1642HFL Recombinant Full Length Human SRM Protein, C-Flag-tagged Mammalian cells Flag
Human SRM-5155H Recombinant Human SRM protein, GST-tagged E.coli GST 17-302aa
Human SRM-2098H Recombinant Human SRM Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Human SRM-2098H-B Recombinant Human SRM Protein Pre-coupled Magnetic Beads HEK293
Mouse Srm-6127M Recombinant Mouse Srm Protein, Myc/DDK-tagged HEK293T Myc/DDK
Rhesus Macaque SRM-4466R Recombinant Rhesus monkey SRM Protein, His-tagged Mammalian Cell His
Rhesus Macaque SRM-4282R Recombinant Rhesus Macaque SRM Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Rhesus Macaque SRM-4282R-B Recombinant Rhesus Macaque SRM Protein Pre-coupled Magnetic Beads HEK293
Zebrafish SRM-11266Z Recombinant Zebrafish SRM Mammalian Cell His
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • SRM Related Articles

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
Cysteine and methionine metabolismLDHB;GOT2B;DNMT3A;MDH1AA;DNMT3;AGXT2;MTAP;ADI1;MTR
Arginine and proline metabolismHOGA1;ALDH4A1;GATM;OAT;CNDP1;DAO1;ALDH1B1;SAT2B;CKMT1B
beta-Alanine metabolismALDH3A2;ALDH2.1;SRM;GAD1B;MLYCD;ALDH9A1A.1;CARNS1;SMS;ALDH9A1
Glutathione metabolismGGCTB;GGCTA;GSTM2;G6PD;GGT6;GSTA1;MGST1;GSTM6;GSTT2B
Metabolic pathwaysPLCG1;SGPL1;CS;HADH;PTGS2B;SUCLG2;IDH2;LIPCA;HSD17B10

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 bindingCST3;SH3GLB1;KIAA1274;RPL14;EIF2S1;RBX1;CLEC4G;RBM8A;HTR1B
protein homodimerization activityPEX7;HMGCS1;MTMR2;RQCD1;DPP4;BST2;NR6A1A;NLRC4;BCL2L2
spermidine synthase activity

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

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).
  • Q&As
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