Recombinant Mouse Protein diaphanous homolog 1 (Diaph1), partial

Code CSB-YP006890MO
MSDS
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Source Yeast
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Code CSB-EP006890MO
MSDS
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Source E.coli
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Code CSB-EP006890MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP006890MO
MSDS
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Source Baculovirus
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Code CSB-MP006890MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Diaph1; Diap1Protein diaphanous homolog 1; Diaphanous-related formin-1; DRF1; p140mDIA; mDIA1
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity.
Gene References into Functions
  1. We studied the interactions between actin and the FH2 domains of formins Cdc12, Bni1 and mDia1 to understand the factors underlying their different rates of polymerization. All-atom molecular dynamics simulations revealed two factors that influence actin filament elongation and correlate with the rates of elongation PMID: 30035712
  2. The aim of this study was to investigate the role of DIAPH1 in the physiological response to experimental myocardial I/R in mice. After subjecting wild-type mice to experimental I/R, myocardial DIAPH1 expression was increased, an effect that was echoed following hypoxia/reoxygenation (H/R) in H9C2 and AC16 cells PMID: 29239839
  3. mDia induces circumferential actin filaments around the edge of the synaptic cleft, which contract the presynaptic terminals in a ROCK-dependent manner. PMID: 27880913
  4. these results uncover a novel role for mDia1 in Abeta-mediated synaptotoxicity and demonstrate that inhibition of MT dynamics and accumulation of PTMs are driving factors for the induction of tau-mediated neuronal damage. PMID: 28877993
  5. Small Molecule Inhibition of Ligand-Stimulated RAGE-DIAPH1 Signal Transduction. PMID: 26936329
  6. Diaphanous-related formin signaling plays a role in heart and vascular development and the maintenance of SMC phenotype. PMID: 26381868
  7. Liprin-alpha3 uses an alpha-helical region to bind to mDia1, counteracting mouse Dia1 activation by RhoA. PMID: 25911102
  8. Depleting FMNL1, another Formin family member, resulted in reduced mDia1 expression, while RhoA inhibition did not alter mDia1 expression, which indicated that there was a FMNL1-mDia1-Profilin1 signaling pathway in mouse oocytes. PMID: 25447542
  9. Mammalian diaphanous-related formin 1 regulates GSK3beta-dependent microtubule dynamics required for T cell migratory polarization. PMID: 24260404
  10. study examined how mDia functions in axon guidance in vivo and in vitro; findings show mDia plays multiple roles in the proper formation of the neural network PMID: 23890216
  11. mDia1 can efficiently put actin filaments under mechanical tension. PMID: 23695677
  12. The active form of mDia1 localized to the apical membrane in exocrine pancreas cells; introduction of an active form of mDia1 leads to a marked increase in actin bundle density along the secretory vesicle lumen perimeter. PMID: 23754409
  13. Dia1 and Dia2 are dynamic components of meiotic spindle and pole complex during meiotic maturation of oocytes. PMID: 20971793
  14. Full-length mouse mDia1 (mDia1-FL) forms tightly autoinhibited dimers that can only be partially activated by RhoA. PMID: 22605659
  15. mDia1 integrates oxidative and signal transduction pathways triggered, at least in part, by receptor for advanced glycation endproducts ligands, thereby regulating pathological neointimal expansion. PMID: 22511750
  16. mDia1 and WAVE2 are important Src homology 3 domain partners of IRSp53 in forming filopodia. PMID: 22179776
  17. The results of this study suggested that Rho signaling via mDia and ROCK critically regulates nuclear translocation through F-actin dynamics in tangential migration, whereas this mechanism is dispensable in radial migration. PMID: 22246438
  18. Microtubules modestly inhibit actin polymerization by mDia1. PMID: 21998204
  19. actin cytoskeleton regulated by Rho-mDia pathway is critical for the integrity of the adherens junctions and the polarity of neuroepithelial cells PMID: 21980468
  20. Activity and localization of mouse formin mDia1 can be regulated through interactions with phospholipids in the carboxyl-terminus, which functions as a switch for transient inactivation. PMID: 20619927
  21. Loss of mDia1 is associated with impaired T-cell interaction and T-cell stimulation in lymph nodes. PMID: 20881208
  22. Autoinhibition in the native Dia1 dimer involves steric hindrance with the actin filament. PMID: 20927343
  23. study showed helical rotation of mDia1 by single-molecule fluorescence polarization (FL(P)); FL(P) of labeled F-actin, both elongating and depolymerizing from immobilized mDia1, oscillated with a periodicity corresponding to F-actin long-pitch helix PMID: 21148346
  24. Findings suggest that Rho-mDia1 signaling facilitates malignant transformation and invasion by manipulating the actin cytoskeleton and targeting Src to the cell periphery. PMID: 20679479
  25. Results show that DIP/WISH binds to mammalian diaphanous and N-WASP, and functions as a scaffold protein by binding to Nck protein. PMID: 19778379
  26. ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts. PMID: 12021256
  27. mDia influences Pax6-induced transcriptional activity and axonal pathfinding in a way opposite from ROCK (Rho kinase) and that it may act via Pax6 to modulate early neuronal development PMID: 12324464
  28. These results identify novel functional elements of mDia1 and show that it regulates serum response factor activity by inducing depletion of the cellular pool of G-actin. PMID: 12429848
  29. single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells; in vitro, mDia1 FH1-FH2 associated persistently with the growing actin barbed end PMID: 15044801
  30. results show an evolutionarily conserved pathway for microtubule capture, and suggest that mDia functions as a scaffold protein for EB1 and APC to stabilize microtubules and promote cell migration. PMID: 15311282
  31. Data report the crystal structure of the dimeric regulatory domain of the Diaphanous-related formin, mDia1. PMID: 15866170
  32. Interaction of carboxy-terminal Diaphanous-autoregulatory domain with the regulatory N-terminus of Dia1 and its release by Rho*GTP are described PMID: 16292343
  33. mDia1 is recruited early during CR3-mediated phagocytosis and colocalizes with polymerized actin in the phagocytic cup in macrophages. PMID: 16303559
  34. The crystal structure of the Diaphanous autoinhibitory domain of mDia1 in complex with the N-terminal Diaphanous inhibitory domain suggests a mechanism for regulating mDia1 activation. PMID: 16472745
  35. mDia1-FH2 has an effect on the conformation of actin filaments PMID: 16490788
  36. HAN11 and mDia1 repressed DYRK1A-dependent GLI1 transcriptional activity PMID: 16887337
  37. These results identify a new activity for the formin mDia in regulating GSK3beta through novel PKCs and implicate novel PKCs as new factors in the MT stabilization pathway. PMID: 16987962
  38. These results indicate that RhoA-dependent signaling through mDia1/2 and the MRTFs is important for SMC-specific gene expression in smooth muscle cells. PMID: 17170370
  39. p140mDia1 has a central role in vivo in dynamic cytoskeletal remodeling events driving normal T cell responses PMID: 17595162
  40. These results suggest that mDia1 plays a distinct role in chemotaxis in T lymphocyte trafficking. PMID: 17682067
  41. Results suggest that a balance between two pathways downstream of mDia, one involving SRF, regulates MyoD expression and cell cycle progression. PMID: 17684061
  42. the DD/CC region is required for the Rho-independent membrane targeting of the isolated N terminus of mDia1 and mDia2 PMID: 17716977
  43. mDia may be important for Rho-dependent survival of oncogenically transformed cells, perhaps driven by AKAP13/Lbc PMID: 17786040
  44. Galpha(12/13) proteins exert essential functions linking extracellular signals to microtubule dynamics and cell polarity via RhoGEF and formin activity. PMID: 17959834
  45. The binding of POPX2 (PPM1F) to mDia1 or to an mDia-containing complex greatly decreases the ability of mDia1 to activate transcription from the serum response element (SRE). PMID: 18230650
  46. G-actin regulates rapid induction of actin nucleation by mDia1 to restore cellular actin polymers. PMID: 18827014
  47. In vitro rheologic assays were used to deconvolve the dynamic cross-linking activity from the bundling activity of formin FRL1 and the closely related mDia1 and mDia2. PMID: 18835565
  48. Hck functions in neutrophils to be realized, at least in part, via its interaction with mDia1 and WASp, and identifies the mDia1/Hck/WASp axis as a cytoskeletal signaling interface. PMID: 19234535
  49. Mammalian diaphanous-related formin 1 (mDia1)plays an essential role in neutrophil chemotaxis; mDia1 and Wiskott-Aldrich syndrome protein (WASp) colocalize at the leading edge of polarized neutrophils. PMID: 19265163
  50. the effect of mDia1-FH2 formin fragments on the dynamic and conformational properties of actin filaments PMID: 19348771

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Subcellular Location
Cell membrane. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm. Nucleus.
Protein Families
Formin homology family, Diaphanous subfamily
Tissue Specificity
Widely expressed. In the organ of Corti, it is expressed at the outer and inner hair cell layers. Expression at the inner hair cell layer is restricted to inner pillar cells. Detected in cochlear spiral ganglion neurons.
Database Links
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