Recombinant Mouse Vasodilator-stimulated phosphoprotein (Vasp)

Code CSB-YP025797MO
MSDS
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Source Yeast
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Code CSB-EP025797MO-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-BP025797MO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP025797MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Vasp
Uniprot No.
Alternative Names
Vasp; Vasodilator-stimulated phosphoprotein; VASP
Species
Mus musculus (Mouse)
Expression Region
2-375
Target Protein Sequence
SETVICSSRATVMLYDDSNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVV INCAIIRGVKYNQATPIFHQWRDARQVWGLNFGSKEDAIQFATGMANALEALEGGGPPPA PAPPAWSAQNGPSPEELEQQKRQPEHMERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPP PGLPSSGVSGAGHGAGAAPPPAPPLPTAQGPNSGGSGAPGLAAAIAGAKLRKVSKQEEAS GGPLAPKAENSRSTGGGLMEEMNAMLARRRKATQVGEKPPKDESASEESEARLPAQSEPV RRPWEKNSTTLPRMKSSSSVTTSEAHPSTPCSSDDSDLERVKQELLEEVRKELQKMKEEI IEVFVQELRKRGSP
Protein Length
Full Length of Mature Protein
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, pH 8.0
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
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.
Gene References into Functions
  1. Myocardial ischemic preconditioning-induced VASP phosphorylation in platelets is a protective mechanism against the deleterious effects of ischemia. PMID: 29344719
  2. VASP selectively mediate activated T-cell trafficking by promoting the diapedesis step of transendothelial migration in a alpha4 integrin-dependent manner. PMID: 28320969
  3. We identified a phosphorylation-dependent mechanism that regulates selective recruitment of these effectors to Lamellipodin: Abl-mediated Lamellipodin phosphorylation promotes its association with both Scar/WAVE and Ena/VASP, whereas Src-dependent phosphorylation enhances binding to Scar/WAVE but not to Ena/VASP PMID: 26996666
  4. Thus, unlike host proteins characterized in Shigella pathogenesis that promote bacterial spread, VASP and EVL function to limit it. PMID: 26358985
  5. Data show that the hypoxia inducible factor 1 alpha subunit (HIF-1alpha) protein level in lung tissues increased significantly at four hours and eight hours, whereas the vasodilator-stimulated phosphoprotein (VASP) protein level decreased significantly. PMID: 25051011
  6. Collectively, our studies highlighted that the CuB-induced actin aggregation and cofilin-actin rod formation was mediated via the Ga13/RhoA/PKA/VASP pathway. PMID: 24691407
  7. Ena/VASP regulates mDia2-initiated filopodial morphology, dynamics, and function. PMID: 24989797
  8. cancer cells reaching liver sinusoids induced up-regulation of VASP PMID: 24917558
  9. Low VASP activation was associated with high fat diet (HFD). Effects of HFD on aortic inflammation and insulin resistance were recapitulated by VASP knockout, implying a role for VASP to constrain inflammatory signaling and maintain insulin sensitivity. PMID: 25117404
  10. CDC42 activation inhibits this activity and promotes IRSp53-dependent recruitment and clustering of VASP to drive actin assembly. PMID: 24076653
  11. VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation. PMID: 23555988
  12. A VASP to Rac to soluble guanylyl cyclase negative feedback loop limited cGMP production, thereby regulating adipogenesis and energy homeostasis. PMID: 22932701
  13. The results of this study suggested that that PI(3,4)P2, Lpd, and Ena/VASP are involved in the process movement of multipolar migrating cells. PMID: 22915108
  14. study demonstrate that endothelial VASP holds significant importance for endothelial barrier properties during hypoxia PMID: 21607702
  15. studies identified VASP and VASP phosphorylation as crucial target for future hepatoprotective strategies PMID: 22216296
  16. Data indicate that VASP is a critical downstream mediator of the anti-inflammatory effects induced by the NO/cGMP pathway. Targeted deletion of VASP predisposes to Kupffer cell inflammation. PMID: 21911751
  17. phosphorylation of VASP by AMPK occurs at a novel site, serine 322, and phosphorylation at this site alters actin filament binding. PMID: 21945940
  18. VASP binding to actin, elevated Rac activity, and elevated formation of actin free barbed ends, thus restoring normal beta(2) integrin function. PMID: 21795685
  19. Growth of VASP expressing melanomas was retarded in VASP(-/-) versus wild-type animals PMID: 21762694
  20. The phosphorylation of VASP performs a key function for the formation of platelet-neutrophil complexes that is crucially important for the extent of myocardial ischemia-reperfusion injury. PMID: 21606399
  21. VASP is the critical regulator of BBB maintenance during acute ischemic stroke PMID: 21151938
  22. VASP deficiency leads to a more profound endothelial barrier disruption and delayed recovery after activation of thrombin PAR-1 receptor. PMID: 20945373
  23. A link is proposed between vimentin, VASP phosphorylation and actin dynamics that delivers an explanation for the important role of vimentin in controlling endothelial cell morphogenesis. PMID: 20382123
  24. Data demonstrate a novel mechanism by which alphavbeta3 integrin acts to locally suppress beta1 integrin activation and regulate VASP and RIAM to control cell adhesion and migration. PMID: 20404115
  25. VASP-deficient platelets display normal filopodia extension PMID: 19806269
  26. Results suggest that VASP phosphorylation by PKA plays an important role in membrane ruffle formation and chemotaxis via the regulation of focal adhesion formation/maturation. PMID: 19733667
  27. IRAK-1 forms a close complex with PKCepsilon as well as VASP, and participates in phorbol 12-myristate 13-acetate-induced phosphorylation of VASP. PMID: 20044140
  28. VASP phosphorylation controls remodeling of the actin cytoskeleton. PMID: 19825941
  29. These results identify tissue-specific VASP as a central protein in the control of the alveolar-capillary barrier properties during acute lung injury. PMID: 19690214
  30. Results reveal a vasodilator-stimulated phosphoprotein (VASP)-dependent modulation of the Rac/PAK pathway and Rac/PAK-regulated processes, like cell motility and polarization. PMID: 12055190
  31. function as a cellular regulator of actin dynamics perhaps via initializing actin polymerization PMID: 12372613
  32. Ena-VASP proteins may play an important role in intercalated disk function at the interface between cardiac myocytes. PMID: 12933343
  33. VASP is involved in down-regulation of platelet adhesion to the vascular wall under both physiologic and pathophysiologic conditions. PMID: 12933589
  34. findings indicate that Ena/VASP proteins contribute to the persistence of both speed and directionality of L. monocytogenes movement PMID: 12940993
  35. Mena & VASP are needed for viability & the formation of neural-derived organs. Neural tube, craniofacial, spinal nerve, & anterior commissure defects are seen in double but not single M-/- & V-/- mutants, showing both are needed for the above structures. PMID: 15371503
  36. Despite an enhanced injury response early on, VASP -/- mice are protected from long-term progression of nephrotoxic nephritis, which is associated with improved renal endothelial cell preservation and regeneration. PMID: 15743999
  37. delayed hearing development in VASP-/- mice is supposed to be caused by a delayed formation of actin filaments in the outer pillar head plate indicating the importance of appropriate pillar cell stiffness in cochlear mechanics PMID: 17361081
  38. Both recruitment of SH2-Bbeta to Listeria and SH2-Bbeta stimulation of actin-based propulsion require the vasodilator-stimulated phosphoprotein (VASP), which binds ActA at the surfaces of Listeria cells and enhances bacterial actin-based motility. PMID: 17452473
  39. VASP has a role during neonatal development of the mammalian cochlea PMID: 17920567
  40. Loss of murine Ena/VASP protein, an actin regulatory protein, causes neuronal ectopias, alters intralayer positioning in the cortical plate, and, surprisingly, blocks axon fiber tract formation during corticogenesis. PMID: 17988629
  41. VASP at least in part stabilizes endothelial barrier functions by regulating Rac1 activity. PMID: 17989211
  42. VASP is involved in cAMP-mediated Rac 1 activation in microvascular endothelial cells. PMID: 19118163
  43. Data indicate that VASP is required for integrin alpha5beta1-mediated adhesion which stabilizes endothelial barrier properties at least in part by facilitating Rac 1 activation. PMID: 19347869
  44. Regulation of VASP phosphorylation in cardiac myocytes: differential regulation by cyclic nucleotides and modulation of protein expression in diabetic and hypertrophic heart. PMID: 19734360
  45. VASP phosphorylation at serine239 regulates cytoskeleton remodeling. PMID: 19798690

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Subcellular Location
Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane.
Protein Families
Ena/VASP family
Tissue Specificity
Highly expressed in thymus and spleen. Lower levels in lung, ovary, placenta and fat.
Database Links
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