LMO2

  • Official Full Name

    LIM domain only 2 (rhombotin-like 1)
  • Overview

    LMO2 encodes a cysteine-rich, two LIM-domain protein that is required for yolk sac erythropoiesis. The LMO2 protein has a central and crucial role in hematopoietic development and is highly conserved. The LMO2 transcription start site is located approximately 25 kb downstream from the 11p13 T-cell translocation cluster (11p13 ttc), where a number T-cell acute lymphoblastic leukemia-specific translocations occur. Alternative splicing results in multiple transcript variants encoding different isoforms.
  • Synonyms

    LMO2;LIM domain only 2 (rhombotin-like 1);RBTNL1;rhombotin-2;RBTN2;RHOM2;rhombotin like 1;T cell translocation gene 2;TTG2;LMO-2;rhombotin 2;rhombotin-like 1;LIM domain only protein 2;T-cell translocation gene 2;cysteine-rich protein TTG-2;T-cell translocation protein 2

Recombinant Proteins

  • Rhesus macaque
  • Chicken
  • Zebrafish
  • Human
  • Mouse
  • Mammalian Cells
  • HEK293
  • E.coli
  • His
  • Non
  • DDK
  • Myc
  • Avi
  • Fc
Cat.# Product name Source (Host) Species Tag Protein Length Price
LMO2-2534R Recombinant Rhesus monkey LMO2 Protein, His-tagged Mammalian Cells Rhesus macaque His
LMO2-5844C Recombinant Chicken LMO2 Mammalian Cells Chicken His
LMO2-8735Z Recombinant Zebrafish LMO2 Mammalian Cells Zebrafish His
LMO2-4710HCL Recombinant Human LMO2 293 Cell Lysate HEK293 Human Non
Lmo2-1327M Recombinant Mouse Lmo2 Protein, MYC/DDK-tagged HEK293 Mouse DDK&Myc
LMO2-2354R Recombinant Rhesus Macaque LMO2 Protein, His (Fc)-Avi-tagged HEK293 Rhesus macaque Avi&Fc&His
LMO2-2354R-B Recombinant Rhesus Macaque LMO2 Protein Pre-coupled Magnetic Beads HEK293 Rhesus macaque
LMO2-2399H Recombinant Human LMO2 Protein, His-tagged E.coli Human His Met1-Gly156
LMO2-6221H Recombinant Human LMO2 Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293 Human DDK&Myc
LMO2-777H Recombinant Human LMO2 Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293 Human DDK&Myc

    Involved Pathway

    LMO2 involved in several pathways and played different roles in them. We selected most pathways LMO2 participated on our site, such as Transcriptional misregulation in cancer, which may be useful for your reference. Also, other proteins which involved in the same pathway with LMO2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Transcriptional misregulation in cancer IL1R2,GRIA3,SIX1,SS18,Pdgfa&Pdgfb,GZMB,ITGAM,PML,FLT3,PLAU

    Protein Function

    LMO2 has several biochemical functions, for example, E-box binding,RNA polymerase II activating transcription factor binding,RNA polymerase II regulatory region sequence-specific DNA binding. Some of the functions are cooperated with other proteins, some of the functions could acted by LMO2 itself. We selected most functions LMO2 had, and list some proteins which have the same functions with LMO2. You can find most of the proteins on our site.

    Function Related Protein
    cofactor binding TYMS,DDO,PGAM2,ME3,ACLY,C3,TKT,UROS,ACLYA,ASNS
    zinc ion binding RNF24,RNF112,BAZ1B,MARCH6,LNX2A,ADAMTSL1,ESR2,PAM,RNF6,PRKCB
    E-box binding TFAP4,TAL1,ASCL2,MYOG,SREBF2,ATOH8,BHLHE40,NEUROD2,MYC,TCF21
    RNA polymerase II regulatory region sequence-specific DNA binding ZNF549,IRF2,FOXF2,ZFP583,NKX2-1,ZNF256,NME2,RELA,MEF2D,ATF1
    chromatin binding POLE,SHMT2,HDAC3,PRDM13,AAAS,TP63,SMC3,CBX5,DNMT1,JDP2
    protein binding BUB1B,ZNF177,S100A11,TBX2A,RPL7A,C15orf23,VPS18,SFRP4,KCNJ10,SRSF5
    transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding SOHLH2,CREB3L3,ARID3A,MAFF,ELF5,ONECUT3,MYF5,SOX17,EP300,CSRNP1
    RNA polymerase II activating transcription factor binding SIN3A,HEY2,POU1F1,MAD2L2,NFE2L2,TP53BP1,CREB1,EGR2,LDB1,TBX3
    transcriptional activator activity, RNA polymerase II transcription factor binding NKX2,NKX2-5,PITX1,NR1H4,NOTCH1,SOX10,WWP2,PPARA,MIXL1,GBX2

    Interacting Protein

    LMO2 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 LMO2 here. Most of them are supplied by our site. Hope this information will be useful for your research of LMO2.

    MAPRE3;HNRNPM;MAPRE2;LDB1;PHC2

    Resources

    References

    • Zhang, J; Rabbitts, TH; et al. Intracellular antibody capture: A molecular biology approach to inhibitors of protein-protein interactions. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1844:1970-1976(2014).
    • Sewell, H; Tanaka, T; et al. Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex. SCIENTIFIC REPORTS 4:-(2014).

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