Recombinant Human Beta-Actin Protein (C-6His)

Name: Recombinant Human Beta-Actin Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1467NP
Availability: InStock

BL-1467NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Beta-Actin is produced by our E.coli expression system and the target gene encoding Asp2-Phe375 is expressed with a 6His tag at the C-terminus.
Accession	P60709
Synonym	Actin Cytoplasmic 1; Beta-Actin; ACTB
Gene Background	Actins are ubiquitous globular and highly conserved proteins that are involved in various types of cell motility, structure, and integrity. Three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. ACTB is a major constituent of the contractile apparatus and one of the two nonmuscle cytoskeletal actins. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.
Molecular Mass	42.8 KDa
Apmol Mass	43 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 10mM Tris-HCl, 0.1% TritonX-100, 2mM DTT, 10% Glycerol, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA.
Subcellular Location	Cytoplasm, cytoskeleton. Nucleus.
Protein Families	Actin family
Database References	HGNC: 132 OMIM: 102630 KEGG: hsa:60 STRING: 9606.ENSP00000349960 UniGene: PMID: 28194011 Haploinsufficiency of ACTB is the main cause of the clinical phenotype observed in the patients with 7p22.1 microdeletions. PMID: 29274487 Baraitser-Winter cerebrofrontofacial syndrome is caused by missense mutations in the cytoplasmic beta- and gamma-actin genes ACTB and ACTG1. We provide an overview of the clinical characteristics (including some novel findings in four recently diagnosed patients), diagnosis, management, mutation spectrum and genetic counselling. PMID: 27625340 The authors describe heterozygous ACTB deletions and nonsense and frameshift mutations in 33 individuals with developmental delay, apparent intellectual disability, increased frequency of internal organ malformations (including those of the heart and the renal tract), growth retardation, and a recognizable facial gestalt. PMID: 29220674 Data indicate AIM1 (absent in melanoma 1) as an actin binding protein and show that it regulates cytoskeletal remodeling and cell migration in prostate epithelial cells. PMID: 28747635 Case Report: gastric pericytoma harboring the exceptionally rare translocation t(7;12) resulting in ACTB-GLI1 gene fusion. PMID: 26980027 Data suggest that, in T-lymphocytes, nitric oxide generated by eNOS S-nitrosylates Cys374 on ACTB and thus regulates activation/recruitment of PRKCQ at immune synapse; S-nitrosylation of beta-actin impairs actin binding to PFN1 and regulates protein transport in lamellipodia. (eNOS = nitric oxide synthase 3; ACTB = beta-actin; PRKCQ = protein kinase C-theta; PFN1 = profilin-1) PMID: 28394935 Data indicate that the IQGAP1 N-terminal fragment spanning residues 1-191 (CHDF) binds to both F-actin and Ca(2+)/calmodulin. PMID: 27798963 Based on present and published dup7p22.1 patients we suggest that renal abnormalities might be an additional feature of the 7p22.1 microduplication syndrome.We also pinpoint the ACTB gene as the key gene affecting the 7p22.1 duplication syndrome phenotype. PMID: 27866048 We suggest that haploinsufficiency of ACTB may be responsible for the clinical features of patients with 7p22.1 microdeletions PMID: 27633570 crucial role of Glu270 in ADP-ribosylation of actin by Ia PMID: 26713879 Studies indicate that the process of megakaryocyte maturation and the formation of proplatelets are essential steps in the production of mature platelets and both depend heavily on the actin and microtubule cytoskeletons. PMID: 26210823 Data show that tripartite motif-containing 28 protein (TRIM28) and beta-actin were up-regulated in the glioblastoma multiforme (GBM) stem-like cells compared to the controls. PMID: 25419715 Data suggest that by binding to both clathrin and F-actin, mammalian actin-binding protein 1 (mAbp1; HIP-55 or SH3P7) is specifically recruited at a late stage of clathrin-coated pits (CCPs) formation, which subsequently recruits dynamin to CCPs. PMID: 25690657 The results indicate that the disease-related human beta-actin mutations p.R183W and p.E364K affect interdomain mobility and nucleotide interactions as a basis for the formation of disease phenotypes in patients. PMID: 25255767 Data indicate the WASp-interacting protein (WIP)-Wiskott-Aldrich syndrome protein (WASp) interaction in the regulation of actin-dependent processes. PMID: 24962707 Mutations in ACTB cause a distinctly more severe phenotype than ACTG1 mutations in Baraitser-Winter syndrome. PMID: 23756437 TIA proteins can function as long-term regulators of the ACTB mRNA metabolism in mouse and human cells. PMID: 24766723 Downregulation of the HuR gene results in decreased beta-actin gene expression, which in turn results in decreased motility and proliferation of corneal fibroblasts. PMID: 24826067 Thus, the nucleocapsid domain in HIV-1 Gag does not appear to have a role in actin recruitment or actin incorporation into HIV-1 particles. PMID: 24789788 Taken together, these findings indicate that actin filament dynamics are dispensable for HIV-1 Gag assembly at the plasma membrane of HeLa cells. PMID: 24789789 Results indicate that actin cytoskeleton is one of the upstream regulators of Hippo signaling. PMID: 24040060 PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism. PMID: 24415753 chorein interacts with beta-adducin and beta-actin. PMID: 24129186 Data indicate that monomeric actin probes concentrate in nuclear speckles. PMID: 23447706 the roles of ACTB in tumors PMID: 23266771 Data suggest that P-glycoprotein associate with the F-actin cytoskeleton through ezrin/radixin/moesin (ERM) in CCR9/CCL25 induced multidrug resistance of acute T-lymphocytic leukemia (T-ALL) cells. PMID: 23326330 Two variants of beta-actin, beta1 and beta2 were found in the Enterovirus 71-susceptible rhabdomyosarcoma cells, compared to Enterovirus 71-resistant cells that contains only one variant beta1. PMID: 23535377 Studies indicate that cofilin binds actin stoichiometrically - one cofilin molecule per actin filament subunit. PMID: 23395798 Studies indicate that that vinculin not only bundles actin filaments but can also cap these filaments and promote actin polymerization. PMID: 23466368 Cofilin nuclear shuttling is critical for the cofilin-actin rod stress response. PMID: 22623727 These results indicate that F-actin in association with the M protein alters the interaction between the M and H proteins, thereby modulating measles virus cell-cell fusion and assembly. PMID: 23221571 Data indicate beta-cytoplasmic (beta-CYA) and gamma-cytoplasmic (gamma-CYA) actins differential localization and dynamics at epithelial junctions. PMID: 22855531 roles for undetected ACtB in liver cancer progression PMID: 22961449 Data show that ENOA, PARK7 and Beta-actin are proper reference standards in obesity studies based on omental fat. PMID: 22272336 identified de novo missense changes in the cytoplasmic actin-encoding genes ACTB and ACTG1 in one and two probands, respectively; suggest that Baraitser-Winter syndrome is the predominant phenotype associated with mutation of these two genes PMID: 22366783 Recombinant human actin is constantly shuttled into the murine nucleus by importin 9 and out by exportin 6. Nuclear actin is required for maximal transcription. PMID: 22323606 Antioxidant supplementation was noted to increase G6PDH in the pentose phosphate cycle and 18S rRNA in the ribosome. There were no significant changes in the gene expression levels of beta-ACT PMID: 22285204 non-muscle alpha-ACTN4, HSPA5 and cytoplasmic ACTB, should be targeted in idiopathic premature ovarian failure cases PMID: 21890413 Data indicate taht candidate genes ACTB, BZW, OCM, MACC1, NXPH1, PRPS1L1, RAC1 and RPA3, which lie within the DFNB90 region, were sequenced and no potentially causal variants were identified. PMID: 21734401 ACTB showed high expression in forensic skin and body-fluid samples, providing a suitable marker for skin identification PMID: 21221983 Nuclear beta-actin controls growth arrest of epithelial cells. PMID: 21172822 Data suggest that the existence of a common epitope on the molecules of phosducin and beta-actin may reflect a topological similarity of a small region of their surfaces. PMID: 20804785 Findings indicate that activation of the cofilin-F-actin pathway contributes to tumor cell migration and metastasis enhanced by Aur-A, revealing a novel function for mitotic Aur-A kinase in tumor progression. PMID: 21045147 The actin network plays a role in nuclear ERalpha actions in breast cancer cells. PMID: 20308691 Immunoblot analysis revealed profoundly decreased beta-actin levels during Ectromelia virus infection replicative cycle in the infected cells 24 hrs post infection. PMID: 20201613 This protein has been found differentially expressed in the anterior cingulate cortex from patients with schizophrenia PMID: 20381070 Data show that inducible Hox genes are selectively sensitive to the inhibition of actin polymerization and that actin polymerization is required for the assembly of a transcription complex on the regulatory region of the Hox genes. PMID: 19477923 Results suggest a novel mechanism by which cofilin is regulated by v-Src through tyrosine phosphorylation that triggers the degradation of cofilin through ubiquitination-proteosome pathway and reducing cellular F-actin contents and cell spreading. PMID: 19802004 region responsible for down-regulation of the gamma-actin gene during differentiation is not in the 3' end of the gene in contrast to that for beta-actin. PMID: 11787062

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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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