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VCA domain of WASP (GST fusion)

VCA domain of WASP (GST fusion)

ArtNr	VCG03-A
Hersteller	Cytoskeleton
Menge	1 x 500 ug
Kategorie	Oncology Peptides & Proteins Recombinant Proteins Cell Biology Cytoskeleton Microfilaments By Organ Breast Cancer
Typ	Proteins
Specific against	other
Purity	Purity is determined by scanning densitometry of proteins on SDS-PAGE gels. Samples are >95% pure (Figure 1).
Citations	van der Gucht, J., Paluch, E., Plastino, J. and Sykes, C. (2005). Stress release drives symmetry breaking for actin-based movement. Proc. Natl. Acad. Sci. U. S. A. 102, 7847-7852.
ECLASS 10.1	32160409
ECLASS 11.0	32160409
UNSPSC	12352202
Alias	Actin, Actin Protein, VCA, WASP, WASP protein, WASP-VCA domain, WASP VCA, WASP VCA domain
Similar products	Actin, WASP, VCA, Actin Protein, WASP protein, WASP-VCA domain, WASP VCA, WASP VCA domain
Versandbedingung	Raumtemperatur
Lieferbar
Shipping Temperature	AT
Storage Conditions	On Arrival: 4°C
Delivery Time	1-2 Weeks
FAQs	Question 1: By itself, what is the effect of VCA-domain WASP protein on actin polymerization? Answer 1: By itself, the VCA-domain WASP protein ((Cat. #VCG03) partial inhibits actin polymerization. When combined with Arp2/3 (RP01), actin polymerization is greatly enhanced. See the associated datasheets for details. Question 2: What is the optimal concentration of Arp2/3 and VCA-domain WASP protein to modify actin polymerization? Answer 2: We recommend thatpyrene actin is present at a final concentration of 0.8 &mu, M, Arp2/3 complex at 10 nM (RP01) and the VCA domain of WASP at 400 nM ((Cat. #VCG03). The critical factor here is the actin concentration which must be 0.80 +/-0.2 µ, M in the final reaction. This concentration is just below the critical concentration for assembly and hence will not polymerize on it&rsquo, s own.
Weight (grams)	8
Product Uses	Stimulating Arp2/3 complex activity Isolating Arp2/3 complex from cell or tissue extract
Material	The VCA (Verprolin, cofilin, acidic) domain of human WASP protein has been expressed in a bacterial expression system as a GST-tagged fusion protein. The protein has been purified by glutathione affinity chromatography and is supplied as a lyophilized powder.When reconstituted with distilled water, the complex is in the following buffer: 20 mM Tris pH 7.5, 25 mM KCl, 1 mM MgCl₂ 0.5 mM EDTA, 0.2% dextran, 2% sucrose. The molecular weight of the GST-VCA domain protein is approximately43 kDa.
Biological Activity	VCG03 was tested in an actin polymerization assay (Cat. # BK003). In conjunction with Arp2/3 (Cat. # RP01>) it was shown to stimulate actin polymerization 20-fold compared to the control without VCG03. This indicates VCA domain specificity for stimulating the actin nucleating activity of Arp2/3.<
Figure 1 Legend	Figure 1. Purity determination of GST-WASP VCA domain. 20 ug of VCG03 was run on an SDS-PAGE gel and visualized by coomassie blue staining. Protein quantitation was performed using the Precision Red Protein Assay Reagent (Cat.# ADV02 ).
Figure 2 Legend	Figure 2: Actin polymerization stimulated by Arp2/3 complex and the VCA domain of WASP. Actin polymerization was measured using kit BK003 . The addition of Arp2/3 complex or the VCA domain alone to actin has minimal effects on actin polymerization, while the combination of Arp2/3 and the VCA domain strongly stimulates the rate of actin polymerization.

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VCG03-A.pdf

VCG03-A-datasheet.pdf

VCG03-A-safety-datasheet.pdf