Recombinant Mouse Vasodilator-Stimulated Phosphoprotein (VASP) Protein (His)

Name: Recombinant Mouse Vasodilator-Stimulated Phosphoprotein (VASP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07052P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Vasodilator-Stimulated Phosphoprotein (VASP) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P70460
Target Symbol	VASP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SETVICSSRATVMLYDDSNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIIRGVKYNQATPIFHQWRDARQVWGLNFGSKEDAIQFATGMANALEALEGGGPPPAPAPPAWSAQNGPSPEELEQQKRQPEHMERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPSSGVSGAGHGAGAAPPPAPPLPTAQGPNSGGSGAPGLAAAIAGAKLRKVSKQEEASGGPLAPKAENSRSTGGGLMEEMNAMLARRRKATQVGEKPPKDESASEESEARLPAQSEPVRRPWEKNSTTLPRMKSSSSVTTSEAHPSTPCSSDDSDLERVKQELLEEVRKELQKMKEEIIEVFVQELRKRGSP
Expression Range	2-375aa
Protein Length	Full Length of Mature Protein
Mol. Weight	45.5 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	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.
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
Database References	KEGG: mmu:22323 STRING: 10090.ENSMUSP00000032561 UniGene: PMID: 29344719 VASP selectively mediate activated T-cell trafficking by promoting the diapedesis step of transendothelial migration in a alpha4 integrin-dependent manner. PMID: 28320969 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 Thus, unlike host proteins characterized in Shigella pathogenesis that promote bacterial spread, VASP and EVL function to limit it. PMID: 26358985 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 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 Ena/VASP regulates mDia2-initiated filopodial morphology, dynamics, and function. PMID: 24989797 cancer cells reaching liver sinusoids induced up-regulation of VASP PMID: 24917558 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 CDC42 activation inhibits this activity and promotes IRSp53-dependent recruitment and clustering of VASP to drive actin assembly. PMID: 24076653 VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation. PMID: 23555988 A VASP to Rac to soluble guanylyl cyclase negative feedback loop limited cGMP production, thereby regulating adipogenesis and energy homeostasis. PMID: 22932701 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 study demonstrate that endothelial VASP holds significant importance for endothelial barrier properties during hypoxia PMID: 21607702 studies identified VASP and VASP phosphorylation as crucial target for future hepatoprotective strategies PMID: 22216296 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 phosphorylation of VASP by AMPK occurs at a novel site, serine 322, and phosphorylation at this site alters actin filament binding. PMID: 21945940 VASP binding to actin, elevated Rac activity, and elevated formation of actin free barbed ends, thus restoring normal beta(2) integrin function. PMID: 21795685 Growth of VASP expressing melanomas was retarded in VASP(-/-) versus wild-type animals PMID: 21762694 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 VASP is the critical regulator of BBB maintenance during acute ischemic stroke PMID: 21151938 VASP deficiency leads to a more profound endothelial barrier disruption and delayed recovery after activation of thrombin PAR-1 receptor. PMID: 20945373 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 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 VASP-deficient platelets display normal filopodia extension PMID: 19806269 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 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 VASP phosphorylation controls remodeling of the actin cytoskeleton. PMID: 19825941 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 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 function as a cellular regulator of actin dynamics perhaps via initializing actin polymerization PMID: 12372613 Ena-VASP proteins may play an important role in intercalated disk function at the interface between cardiac myocytes. PMID: 12933343 VASP is involved in down-regulation of platelet adhesion to the vascular wall under both physiologic and pathophysiologic conditions. PMID: 12933589 findings indicate that Ena/VASP proteins contribute to the persistence of both speed and directionality of L. monocytogenes movement PMID: 12940993 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 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 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 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 VASP has a role during neonatal development of the mammalian cochlea PMID: 17920567 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 VASP at least in part stabilizes endothelial barrier functions by regulating Rac1 activity. PMID: 17989211 VASP is involved in cAMP-mediated Rac 1 activation in microvascular endothelial cells. PMID: 19118163 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 Regulation of VASP phosphorylation in cardiac myocytes: differential regulation by cyclic nucleotides and modulation of protein expression in diabetic and hypertrophic heart. PMID: 19734360 VASP phosphorylation at serine239 regulates cytoskeleton remodeling. PMID: 19798690

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.