Recombinant Saccharomyces Cerevisiae Actin (ACT1) Protein (His&Myc)

Name: Recombinant Saccharomyces Cerevisiae Actin (ACT1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00177P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Saccharomyces Cerevisiae Actin (ACT1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P60010
Target Symbol	ACT1
Species	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF
Expression Range	1-375aa
Protein Length	Full Length
Mol. Weight	49.1 kDa
Research Area	Others
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	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular Location	Cytoplasm, cytoskeleton.
Protein Families	Actin family
Database References	KEGG: sce:YFL039C STRING: 4932.YFL039C

Gene Functions References

Act1 protein affects tombusvirus recombination in yeast . PMID: 26773384
Using multi-color total internal reflection fluorescence microscopy, the study shows that Crn1 enhances Cof1-mediated severing by accelerating Cof1 binding to actin filament sides. PMID: 26299936
Translation elongation factor 1A mutants with altered actin bundling activity show reduced aminoacyl-tRNA binding and alter initiation via eIF2alpha phosphorylation. PMID: 24936063
Heat shock-induced processing of actin assembly protein Lsb1 is involved in prion inheritance. PMID: 25143386
Data suggest that a glycolytic multi-enzyme complex assembles in cytoplasm of S. cerevisiae in association with F-actin (filamentous actin) but not in association with G-actin (monomeric globular actin). PMID: 23763840
Lsb1 and/or Lsb2 full-length proteins inhibit Las17-mediated actin polymerization PMID: 23577202
data suggest that the R256H actin mutation alters filament conformation resulting in filament instability and misregulation by formin PMID: 22753406
analysis of the molecular mechanism of plasma membrane-actin cytoskeleton coupling mediated by cooperative action of epsin Ent1 and the HIP1R homolog Sla2 in yeast Saccharomyces cerevisiae PMID: 22927393
Data suggest that the region surrounding residue 204 is involved in interactions that change depending on the phosphorylation state of the bound nucleotide that might reflect different conformations of F-actin subunits. PMID: 19935871
Vid24p and Sec28p are present at actin patches during glucose starvation. PMID: 19892709
Two recessive mutations, act1-301 in the actin gene and sla2-82 in a gene involved in cortical actin patch assembly, were identified. PMID: 16547104
An unanticipated role for Aip1 and cofilin in promoting rapid turnover of yeast actin cables was revealed. PMID: 16611742
The stabilization of the actin cytoskeleton caused by deletion of Sla1p or End3p leads to hyperactivation of the Ras signaling pathway. PMID: 16914733
Study found 208 genes that have deleterious complex haploinsufficient (CHI) interactions with actin, including several actin-binding protein genes, and nearly half of the CHI genes have defects in actin organization when deleted. PMID: 17167106
In a single ATP-driven cycle, PLP2-CCT-ACT1 complexes yield 30-fold more native actin than CCT-ACT1 complexes. PMID: 19501098

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.