Recombinant Human Actin-Related Protein 3 (ACTR3) Protein (His&Myc)

Name: Recombinant Human Actin-Related Protein 3 (ACTR3) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01403P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Actin-Related Protein 3 (ACTR3) Protein (His&Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P61158
Target Symbol	ACTR3
Synonyms	Actin-like protein 3
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	AGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDFFIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVKEFNKYDTDGSKWIKQYTGINAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
Expression Range	2-418aa
Protein Length	Full Length of Mature Protein
Mol. Weight	51.1 kDa
Research Area	Immunology
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	ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). Plays a role in ciliogenesis.
Subcellular Location	Cytoplasm, cytoskeleton. Cell projection. Nucleus. Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (PubMed:19109554).
Protein Families	Actin family, ARP3 subfamily
Database References	HGNC: 170 OMIM: 604222 KEGG: hsa:10096 STRING: 9606.ENSP00000263238 UniGene: PMID: 30049513 RARalpha regulates Arp2/3-mediated actin cytoskeletal dynamics through a non-genomic signaling pathway PMID: 26848712 evidence of a direct protein-protein interaction between PKD2 and Arp2/3 PMID: 27559607 miR-24-1/let-7a-ARP2/3 complex-RAC isoforms pathway may represent a novel pathogenic mechanism for Hirschsprung disease. PMID: 26991540 Authors found that ARP3 and profilin1 were 2 binding partners of LMO2, primarily in cytoplasm. LMO2. LMO2 mediated the assembly of a complex including ARP3, profilin1, and actin monomer, increased actin monomer binding to profilin1, and promoted lamellipodia/filopodia formation in basal-type breast cancer cells. PMID: 28170369 Arp2 and Arp3 expression was increased under atherosclerotic conditions both in ApoE-/- mice and in oxidized low-density lipoproteins stimulated human coronary artery endothelial cells (HCAECs). PMID: 27181356 These findings indicate that inhibition of the Rac1WAVE2Arp2/3 signaling pathway may promote radiosensitivity, which may partially result from the downregulation of CFL1 in U251 human glioma cells. PMID: 27052944 Kv3.3 regulates Arp2/3-dependent cortical actin nucleation mediated by Hax-1; resulting cortical actin structures interact with the channel's gating machinery to slow its inactivation rate during sustained membrane depolarizations; a mutation that leads to late-onset spinocerebellar ataxia type 13. PMID: 26997484 demonstrate that the Arp2/3 complex in higher eukaryotes is actually a family of complexes with different properties PMID: 26655834 Platelet actin nodule formation is dependent on WASp and the ARP2/3 complex. PMID: 26028144 Suggest alpha5beta1/Arp2/Arp3/FHOD3 pathway reprograms the actin cytoskeleton to promote invasive migration and local invasion in vivo. PMID: 26370503 The loss of the Arp2/3 complex acts as a stress that initiates cell cycle arrest by triggering p16INK4a/p14Arf transcription. PMID: 25264243 study unveils an ARP2/3:VCA-independent function of nuclear-WASp in TH1 gene activation that is uncoupled from its cytoplasmic role in actin polymerization. PMID: 24872192 Cortactin has a role as a scaffold for Arp2/3 and WAVE2 at the epithelial zonula adherens PMID: 24469447 The Arp2/Arp3 complex has a role in osmotic signaling. PMID: 24344184 Study suggested that positive CFL1 and Arp3 expression are closely related to tumor progression, metastasis, and poor prognosis of gallbladder cancer. PMID: 23320827 We demonstrate that WAVE2-Arp2/3 is a major nucleator of actin assembly at the zonula adherens and likely acts in response to junctional Rac signaling PMID: 23051739 Anthrax edema toxin induced transendothelial cell tunnels are resealed by MIM via Arp2/3-driven actin polymerization. PMID: 22100162 the centrosome transiently recruits Arp2/3 to perform processes such as centrosome separation prior to mitotic entry. PMID: 21108927 The results identify Arp2/3 complex as a key factor in the generation of the dynamic actin cluster during mitosis. PMID: 20974812 key residues at this interface were crucial for actin nucleation and Y-branching, high-affinity F-actin binding, and Y-branch stability, demonstrating that the affinity of Arp2/3 complex for F actin independently modulates branch formation and stability. PMID: 20404198 Loss of Arp2/3 function led to defects in cell adhesion and actin assembly at the junction with the target cell (the lytic synapse) PMID: 19913427 Arp2/3 complex is required for actin polymerization during platelet shape change. PMID: 12036877 Platelets activate Arp2/3 complex, assemble actin, and change shape in the absence of WASp, indicating a more specialized role for WASp in these cells. PMID: 12200375 Results suggest that recruitment of factors by Wiskott-Aldrich Syndrome protein (WASP) and Scar1 stimulates cellular actin-based motility and actin nucleation with the Arp2/3 complex. PMID: 12429845 Arp2/3 complex contribution to actin filament nucleation in platelets and fibroblasts importantly requires free barbed ends generated by severing and uncapping. PMID: 12464680 cortactin links receptor endocytosis to actin polymerization by binding both CD2AP and the Arp2/3 complex, which may facilitate the trafficking of internalized growth factor receptors PMID: 12672817 ARP3-mediated actin polymerization is regulated by phosphorylation of the WASP protein. PMID: 12791263 The interaction between cortactin and Arp2/3 complex plays an important role in S1P-mediated remodeling of endothelial cells. PMID: 15242766 Arp2/3 complex genes have roles in actin organization and possibly in cancer phenotypes PMID: 15279900 existence of an Arp2/3 complex-dependent event during the early phase of the life cycles of both primate lentiviruses and intracellular mature vaccinia virus PMID: 15385624 signalling pathways leading to Arp2/3-dependent actin nucleation play an important role in Salmonella typhimurium invasion, but are not involved in intracellular Salmonella-induced actin assembly PMID: 15469433 T-plastin increases Arp2/3-mediated actin-based movement PMID: 15741236 These results indicate that interaction between the Arp2/3 complex and WASP stimulates actin polymerization and integrin beta-1-mediated adhesion during MCP-1-induced chemotaxis of THP-1 cells. PMID: 16004967 the binding of the C terminus of SPIN90 with both the Arp2/3 complex (actin-related proteins Arp 2 and Arp 3) and G-actin activates the former, leading to actin polymerization PMID: 16253999 in activation of the Arp2/3 complex, the C domain first primes the complex by inducing a necessary conformational change and then initiates nucleus assembly by bringing an actin monomer into proximity of the primed complex PMID: 16403731 signal-induced relief of the autoinhibited fold of IQGAP1 allows activation of N-WASP to stimulate Arp2/3-dependent actin assembly PMID: 17085436 Taken together, our data suggest that Apr3 should play an important role in ATRA signal pathway. PMID: 17524364 p120 depletion led to dramatic loss of cortactin and its partner, Arp3, from the cell leading edges PMID: 17576929 Results suggest that WAVE and the Arp2/3 complex jointly orchestrate different types of actin-based plasma membrane protrusions by promoting ruffling and inhibiting mDia2-induced filopodia. PMID: 18516090 the exchange rate of N-WASP controls the rate of ARP2/3-complex-dependent actin-based motility by regulating the extent of actin polymerization by antagonizing filament capping PMID: 19262673 The Arp2/3 complex, an actin-nucleating factor, is recruited at the ring structure and is important for parasite entry. PMID: 19286135

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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.

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