DMD

  • Official Full Name

    dystrophin

  • Overview

    Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex. Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere.

  • Synonyms

    DMD;dystrophin;BMD;CMD3B;DXS142;DXS164;DXS206;DXS230;DXS239;DXS268;DXS269;DXS270;DXS272;OTTHUMP00000023117;OTTHUMP00000023121;OTTHUMP00000023124;OTTHUMP00000023125;OTTHUMP00000023126;OTTHUMP00000215590;OTTHUMP00000215591;OTTHUMP00000215592;OTTHUMP00000215846;Extracellular Signal-Regulated Kinase-1;ERK-1

Recombinant Proteins

  • Human
  • Mouse
  • Chicken
  • Zebrafish
  • Rat
  • HEK293
  • Wheat Germ
  • Mammalian Cell
  • E.coli
  • In Vitro Cell Free System
  • HEK293T
  • Human cells
  • Yeast
  • Mamanlian cells
  • Myc&DDK
  • Non
  • GST
  • His
  • His&Fc&Avi
  • Flag
  • N-His&C-Myc
Cat.# Product name Source (Host) Species Tag Protein Length Price
DMD-12H Recombinant Human DMD protein, MYC/DDK-tagged HEK293 Human Myc&DDK
DMD-13H Recombinant Human DMD protein, MYC/DDK-tagged HEK293 Human Myc&DDK
DMD-26936TH Recombinant Human DMD Wheat Germ Human Non 635 amino acids
DMD-2704H Recombinant Human DMD Protein, GST-tagged Wheat Germ Human GST
DMD-4644M Recombinant Mouse DMD Protein Mammalian Cell Mouse His
DMD-6851C Recombinant Chicken DMD Mammalian Cell Chicken His
DMD-7053H Recombinant Human DMD protein, His-tagged E.coli Human His Ala3048~Ser3328
Dmd-7054M Recombinant Mouse Dmd protein, His-tagged E.coli Mouse His Ser3059~Ile3314
DMD-9299Z Recombinant Zebrafish DMD Mammalian Cell Zebrafish His
DMD-6899HCL Recombinant Human DMD 293 Cell Lysate HEK293 Human Non
DMD-01H Recombinant Human DMD Protein (Lys3200-Thr3684), N-His tagged E.coli Human His Lys3200-Thr3684
DMD-127HF Recombinant Full Length Human DMD Protein In Vitro Cell Free System Human Full L. 635 amino acids
DMD-1352H Recombinant Human DMD Protein, His-tagged E.coli Human His Ile253-Lys597
DMD-1972H Recombinant Human DMD Protein (Ser3066-Ile3321), N-His tagged E.coli Human His Ser3066-Ile3321
DMD-2410M Recombinant Mouse DMD Protein, His (Fc)-Avi-tagged HEK293 Mouse His&Fc&Avi
DMD-2410M-B Recombinant Mouse DMD Protein Pre-coupled Magnetic Beads HEK293 Mouse
DMD-2735H Recombinant Human DMD Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Human Myc&DDK
DMD-36H Recombinant Human DMD Protein, DYKDDDDK-tagged Human cells Human Flag
DMD-37H Recombinant Human DMD Protein, His-tagged Human cells Human His
DMD-4017HF Recombinant Full Length Human DMD Protein, GST-tagged In Vitro Cell Free System Human GST Full L. 635 amino acids
Dmd-5467R Recombinant Rat Dmd protein, His&Myc-tagged E.coli Rat N-His&C-Myc 1-240aa
Dmd-5632R Recombinant Rat Dmd protein, His-tagged Yeast Rat His 1-240aa
DMD-9354HFL Recombinant Full Length Human DMD protein, Flag-tagged Mamanlian cells Human Flag Full L.

    Involved Pathway

    DMD involved in several pathways and played different roles in them. We selected most pathways DMD participated on our site, such as Arrhythmogenic right ventricular cardiomyopathy,Arrhythmogenic right ventricular cardiomyopathy (ARVC),Dilated cardiomyopathy, which may be useful for your reference. Also, other proteins which involved in the same pathway with DMD were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Non-integrin membrane-ECM interactions DDR2,TTR,DDR1,TRAPPC4,LAMC3
    Arrhythmogenic right ventricular cardiomyopathy DES,JUP,CDH2,CTNNA1,DSP,CACNG2,DAG1,CTNNA2,DSG2,DSC2
    Striated Muscle Contraction SMYHC3,TNNI2A.3,TNNI1,MYBPC2,TNNT3B,TNNT1,TNNI2B.1,MYBPC3,TNNI2A.4,DESMB
    Hypertrophic cardiomyopathy (HCM) TGFB3,CACNA2D3,TTN,MYH7,TNNI3,ITGB3,ACTC1,ITGB7,EMD,TNNC1
    Muscle contraction MYL1,TMOD2,TNNI1B,MYL6B,MYBPC2A,DESMB,TMOD3,TMOD1,TNNI2A.1,DESMA
    Dilated cardiomyopathy TGFB3,ITGB3,ATP2A2,CACNG2,PLN,ITGAV,CACNB3,TTN,TGFB1,ITGB8
    Arrhythmogenic right ventricular cardiomyopathy (ARVC) ITGB3,CACNG1,SGCG,CACNA2D4,ITGB1,CACNA2D1,DAG1,ITGA2B,ITGA9,ITGA2
    Extracellular matrix organization COL2A1,COL5A3B,PCOLCEA,MFAP1B,DAG1,MFAP5,ADAM9,LEPREL1,MMP20,MFAP1

    Protein Function

    DMD has several biochemical functions, for example, actin binding,dystroglycan binding,myosin binding. Some of the functions are cooperated with other proteins, some of the functions could acted by DMD itself. We selected most functions DMD had, and list some proteins which have the same functions with DMD. You can find most of the proteins on our site.

    Function Related Protein
    myosin binding RHOA,STX4A,SLC6A4,CALM,CALD1,NPHS1,ARFGEF2,TRIM32,KIRREL,VETZ
    actin binding MYOT,KLHL1,CAPZB,DBNL,MYOZ2,PDLIM5,FMN2,HOOK1,FKBP15,CAPZA2
    zinc ion binding GATAD2B,BRCA1,ZNF259,DNAJC21,ZDHHC5,ZZEF1,GATA2A,TRIM37,TRIM54,TRIM35-22
    dystroglycan binding AGRN,DAG1,VCL,CLASP1,AGR3,AGR2,MAP2,GYLTL1B
    structural constituent of muscle TTN,OBSCN,COX4I2,MYL2,SMTN,NEBL,ACTN3,MYL1,SORBS2,MYL6B
    structural constituent of cytoskeleton TUBB4B,CTNNA2,TUBD1,KRT17,BICD1,TUBA2,ATXN1,NEFL,VIM,EPB41L3
    protein binding EXOC1,IMPA2,ZBTB48,DNAJB1,FEZ1,ATCAY,BAI2,SNCA,NKX3,KCNS2
    nitric-oxide synthase binding DNM2,SNTA1,SLC14A2,SCN5A,CAMK2D,CALM2,CD74,ACTB,DNM3,CAV3
    vinculin binding ACTN1,CTNNA1,NRAP,TLN1,DAG1,C22orf28,SYNM,SORBS3,PXN

    Interacting Protein

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

    DTNB;DTNA;SNTB1;HAUS1;CTNNAL1;KRT19

    Resources

    References

    • Santacatterina, F; Chamorro, M; et al. Quantitative analysis of proteins of metabolism by reverse phase protein microarrays identifies potential biomarkers of rare neuromuscular diseases. JOURNAL OF TRANSLATIONAL MEDICINE 13:-(2015).
    • Dalakas, MC; Loscher, WN; et al. 7th International Immunoglobulin Conference: Interlaken Leadership Awards. CLINICAL AND EXPERIMENTAL IMMUNOLOGY 178:124-126(2014).

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