Arp 2/3 protein complex
(Actin Binding Protein)
| Protein | Arp 2/3 protein complex |
| Origin | Brain, porcine |
| Molecular mass | 224 kDa |
| Protein description |
The seven-subunit protein complex comprises Arp2 and Arp3 and five smaller (Arc) proteins. Both Arp2 and Arp3 possess nucleotide-binding
and divalent cation-binding sites. The complex contains five associated proteins to Arp2 and Arp3, namely p16, p20, p21, p34, and p41
(Synonyms: ARPC-5, -4, -3, -2, and -1).
Arp2/3 is a constitutively inactive complex. Nucleation is efficiently activated in vitro by binding of VCA-domains of members of the Wiskott–Aldrich syndrome family proteins, such as WAVE. For activation, VCA-domain (Cat. #: 8416-01) can be used. |
| Actin interaction | Pointed-end capping protein; branching of actin filaments. Strong nucleation upon activation by VCA-domain (Cat. #: 8416-01). |
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 2 × 500 µg |
| Buffer | 150 mM KCl, 20 mM Trizma pH 7.5, 1 mM DTT, 0.2 mM ATP, 0.5 mM EDTA, 1 mM MgCl2 and 5% disaccharides, when reconstituted with 100 µl ultrapure water to obtain a 1 mg/ml solution. |
| Purity | >98% by scanning densitometry from Coomassie G-250 stained SDS gels. |
| Purification notes | Purified from porcine brain. |
| Protein concentration | Determined at OD280 (0.1% = 1.033). |
| Storage instructions | Store at −70 °C upon arrival; stable in performance for at least 6 months from the date of purchase. Solubilized Arp2/3 complex is kept on ice and should be stored at -20°C in glycerol or CryoProtect (Cat. #: 6011-01). Avoid repeated freeze/thaw cycles. |
| Shipping conditions | At ambient temperature. Upon delivery store at -70°C. |
| Remarks | For research use only. Not for use in human or veterinary diagnostic or therapeutic applications. |
| CAS no. | |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
Reconstitution of contractile actomyosin rings in vesicles.
Litschel T, Kelley CF, Holz D, Adeli Koudehi M, Vogel SK, Burbaum L, Mizuno N, Vavylonis D, Schwille P.
Nat Commun. 2021 Apr 15;12(1):2254. doi: 10.1038/s41467-021-22422-7.
Initiation of DNA replication requires actin dynamics and formin activity.
Parisis N, Krasinska L, Harker B, Urbach S, Rossignol M, Camasses A, Dewar J, Morin N, Fisher D.
EMBO J. 2017 Nov 2;36(21):3212-3231. doi: 10.15252/embj.201796585.
Polarized Exocytosis Induces Compensatory Endocytosis by Sec4p-Regulated Cortical Actin Polymerization.
Johansen J, Alfaro G, Beh CT. PLoS Biol. 2016 Aug 15;14(8):e1002534. doi: 10.1371/journal.pbio.1002534.
Crystal structure of Arp2/3 complex.
Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD.
Science. 2001 Nov 23;294(5547):1679-84.
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.
Nolen BJ, Littlefield RS, Pollard TD.
Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15627-32.
Product DataSheet
Material and Safety Data Sheet
Protein Sequence on NCBI (All chain sequences)
Protein Structures on RCSB
Reconstitution of contractile actomyosin rings in vesicles.
Litschel T, Kelley CF, Holz D, Adeli Koudehi M, Vogel SK, Burbaum L, Mizuno N, Vavylonis D, Schwille P.Nat Commun. 2021 Apr 15;12(1):2254. doi: 10.1038/s41467-021-22422-7.
Parisis N, Krasinska L, Harker B, Urbach S, Rossignol M, Camasses A, Dewar J, Morin N, Fisher D.
EMBO J. 2017 Nov 2;36(21):3212-3231. doi: 10.15252/embj.201796585. Epub 2017 Oct 5.
Polarized Exocytosis Induces Compensatory Endocytosis by Sec4p-Regulated Cortical Actin Polymerization.
Johansen J, Alfaro G, Beh CT.
PLoS Biol. 2016 Aug 15;14(8):e1002534. doi: 10.1371/journal.pbio.1002534. eCollection 2016 Aug.
Robinson RC. Turbedsky K. Kaiser DA. MarchandJB, Higgs HN, Choe S, Pollard TD.
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP.
Nolen BJ, Littlefield RS, Pollard TD.
Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15627-32. Epub 2004 Oct 25.
