Recombinant Rat Dystrophin (DMD) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00526P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Rat Dystrophin (DMD) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00526P
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Product Overview

Description Recombinant Rat Dystrophin (DMD) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P11530
Target Symbol DMD
Species Rattus norvegicus (Rat)
Expression System Yeast
Tag C-6His
Target Protein Sequence MLWWEEVEDCYEREDVQKKTFTKWINAQFSKFGKQHIDNLFSDLQDGKRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALQVLQKNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKTIMAGLQQTNSEKILLSWVRESTRNYPQVNVLNFTSSWSDGLALNALIHSHRPDLFDWNSVVSQQSATQRLEHAFNIAKCQLGIEKLLDPEDVATTYPDKKSILMYITSLFQVLP
Expression Range 1-240aa
Protein Length Partial
Mol. Weight 29.1 kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission.
Subcellular Location Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell junction, synapse, postsynaptic cell membrane.
Database References

STRING: 10116.ENSRNOP00000029969

UniGene: PMID: 29267303

  • results show that dystrophin 71d, dystrophin 71f and dystrophin-associated protein integrate protein complexes, and both complexes were associated to nuclear speckles structures. PMID: 26378780
  • Dp40 can interact with beta-dystroglycan as observed by co-localization assays and the co-localization was reduced with Dp40 mutants. PMID: 26004254
  • Hypoxia-induced muscle damage is not accompanied by the loss of dystrophin and desmin. PMID: 20717635
  • Dp71 is a component of the mitotic spindle and cytokinesis multi-protein apparatuses that might modulate the cell division cycle by affecting lamin B1 and beta-dystroglycan levels. PMID: 21886794
  • This study found that cells stably expressing Dp71Delta(78-79) (PC12-C11) differentiate more efficiently than non-transfected cells. PMID: 21668890
  • we established by immunoprecipitation assays that Dp71 and the dystrophin-associated proteins form a dystrophin-associated protein complex in the cell nucleus. PMID: 19784870
  • dysfunction of dystrophin may result in endothelial and astroglial damage leading to vasogenic edema that is involved in pathogenesis of epileptogenesis PMID: 21029730
  • SAP97 and dystrophin macromolecular complexes determine two pools of cardiac sodium channels Nav1.5 in cardiomyocytes. PMID: 21164104
  • results reveal a crucial role of MMP-mediated beta-DG cleavage in autoimmune neuritis, such as Guillain-Barre' syndrome, and bring insights into therapeutic strategies for autoimmune diseases. PMID: 20097170
  • Components of dystrophin-dystroglycan complex were also distributed along the blood vessels of the pineal gland PMID: 19924636
  • the distribution of dystrophin in series-fibred muscles suggests they are involved in transmission of tension from PMID: 12037582
  • expression of dystrophin during skeletal muscle regeneration PMID: 12086334
  • During a cycle of regeneration in tibialis anterior muscle following myonecrosis, dystrophin is found to be weakly labeled at the sarcolemma on day 5 and moderately stained on day 7. PMID: 12416719
  • Loss of sarcolemmal dystrophin may be involved in the mechanism of contractile force-induced reperfusion injury. PMID: 12890920
  • Results present immunocytochemical localization of beta-dystroglycan, the central member of the dystrophin glycoprotein complex, and show that beta-dystroglycan and utrophin are colocalized in clusters in all parts of Muller cells. PMID: 14711029
  • Cardioprotection conferred by ischemic preconditioning may be enhanced by temporary blockade of contractile activity until restoration of membrane dystrophin during reperfusion. PMID: 15001448
  • Dmd deficient PC12 cells generated by addition of antisense-Dp71 cells exhibited a marked suppression of neurite outgrowth. Early responses were normal, late responses were disturbed. PMID: 15149856
  • Dp71 protein contributes to the proper functioning of the cerebrospinal fluid and blood-brain barriers PMID: 15501597
  • These data support the notion of a physiological role of Dp71f distinct from other dystrophin isoforms present in the central nervous system. PMID: 16841465
  • evaluation of the effect of repeated bouts of exercise on on skeletal muscle titin, desmin & dystrophin; desmin and dystrophin mRNA levels were increased after the first and fifth sessions PMID: 17436058
  • Dp71f modulates GSK3-beta recruitment to the beta1-integrin adhesion complex. PMID: 18677563
  • Dp71d is a dynamic component of nuclear matrix that might participate in the nuclear modeling occurring during neuronal differentiation. PMID: 18687308
  • Findings demonstrate the interdependence between laminin binding to dystroglycan and GM1-containing lipid raft reorganization and provide novel insight into the dystrophin complex regulation of AQP4 polarization in astrocytes. PMID: 19451651
  • dystrophin Dp71f is important for the function that the beta1-integrin complex has during neurite outgrowth PMID: 19681445
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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