Recombinant Human Actin, Alpha Skeletal Muscle (ACTA1) Protein (His)

Name: Recombinant Human Actin, Alpha Skeletal Muscle (ACTA1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06756P
Price: 349.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins, Recombinant proteins fall special offers - full-length proteins, Recombinant proteins holiday sale

Price Save $493

Size

100ug

Submit an inquiry or email sales for a custom bulk quote. Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Actin, Alpha Skeletal Muscle (ACTA1) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P68133
Target Symbol	ACTA1
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	C-6His
Target Protein Sequence	DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
Expression Range	3-377aa
Protein Length	Full Length of Mature Protein
Mol. Weight	47.4 kDa
Research Area	Signal Transduction
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	HGNC: 129 OMIM: 102610 KEGG: hsa:58 STRING: 9606.ENSP00000355645 UniGene: Hs.1288
Associated Diseases	Nemaline myopathy 3 (NEM3); Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM); Myopathy, congenital, with fiber-type disproportion (CFTD); Myopathy, scapulohumeroperoneal (SHPM)

Gene Functions References

Our study demonstrates that high ActA level is an independent prognosis factor of survival in cancer patients. More than a basic marker of the severity of the neoplastic disease or of the inflammatory process, ActA seems to influence survival by contributing to the development of cachexia and loss of skeletal muscle mass. PMID: 28712119
The study confirmed ACTA1 mutations in four patients, including one with intranuclear rods, one with large intracytoplasmic aggregates, and two with nemaline intracytoplasmic rods. PMID: 28780987
Study shows that clinically severe ACTA1-related myopathy can present with muscle morphological findings suggestive of cytoplasmic body myopathy in the absence of definite nemaline rods. PMID: 28416349
Shorter than normal thin filament length contributes to the impaired force generation in patients with thin filament myopathy, but only in those who harbor specific mutations in NEB or ACTA1. PMID: 27074222
Over-expression of TNC, SMA, and vimentin were significantly correlated with the lower overall survival in prostate cancer patients. PMID: 28341124
ANA and ASMA evaluation in patients with liver transplantation and no history of autoimmune disease has no clinical relevance, since it varies in time and is not related to any risk factors or liver injury. Routine autoimmunity evaluation should be avoided. PMID: 28337446
Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the vinculin tail helical bundle to mediate actin bundling. PMID: 26493222
This study reported the new information on the frequency and phenotypes of congenital myopathy caused by ACTA1 mutations in subjects >/=5 years of age. PMID: 26172852
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments. PMID: 26295568
Mutations in ACTA1 can cause pathologic features consistent with myofibrillar myopathy. PMID: 25913210
TIMP-1 significantly increased levels of alpha-SMA. PMID: 25895516
novel homozygous recessive missense variant (c.460G>C, P.(Val154Leu)) was found in two brothers with infantile-onset congenital muscular dystrophy with rigid spine. PMID: 25182138
Myopathy associated with zebra bodies is part of the spectrum of myopathies associated with the ACTA1 gene. PMID: 25747004
New scapuloperoneal phenotype associated with an ACTA1 mutation. PMID: 25938801
Antisynthetase syndrome-associated myositis is characterized by distinctive myonuclear actin filament inclusions. PMID: 25746564
The predominant pathway mediated by Australian bat lyssavirus G envelope for internalization into HEK293T cells is clathrin-and actin-dependent also requiring Rab5. PMID: 24576301
Data show that the width and speed of the waves depend counter-intuitively on parameters, negative feedback, and the F-actin time scale. PMID: 23831272
Although most cases of severe infantile form of nemaline myopathy caused by ACTA1 mutations are sporadic and have no family history PMID: 24313005
These findings suggest that the direct contact of Dengue virus 2 E protein with 43 kDa actin protein may have a crucial function in Dengue virus 2 infection of ECV304 cells. PMID: 23376163
Myotonia in adult human skeletal actin transgenic mice may be explained on the basis of a mosaic expression of ClC-1 channels in different fibres and/or on alterations of other conductances. PMID: 23247112
Respiratory muscles from an animal model of nemaline myopathy with an ACTA1 mutation show distinct muscle fiber weakness compared to limb muscles. PMID: 23656990
The objective was to evaluate the presence and distribution of the lubricating and anti-adhesion glycoprotein lubricin and cells containing the contractile isoform smooth muscle alpha-actin (SMA) in pseudomembranes around loose hip prostheses. PMID: 23174700
analysis of the pattern of of evolutionarily conserved basic and acidic residues that constitutes the binding interface of actin-tropomyosin PMID: 23420843
Data show that GnRHR activation affected several cellular markers of locomotion, including actin organization and polymerization as well as active RhoA-GTP levels. PMID: 23176180
Data indicate that actin nucleation on Chlamydia inclusions exhibited moderate depolymerization dynamics. PMID: 23071671
The organization of actin and cytokeratin cytoskeleton and the expression of TCTP, p53,cyclin A, RhoA and actin in HIO180 non-transformed ovarian epithelial cells, and OVCAR3 and SKOV3 ovarian epithelial cancer cells, was studied. PMID: 23042265
Data show that the urinary messenger RNA (mRNA) levels of alpha-smooth muscle actin (alpha-SMA), fibronectin, and matrix metalloproteinase-9 (MMP-9) were significantly higher in the diabetic nephropathy (DN) group, and mRNA levels increased with DN progression. PMID: 21824169
High alpha-actin is associated with colorectal carcinogenesis. PMID: 21912905
Over-expression of Nkx2.5 and/or cardiac alpha-actin inhibit the contraction ability of adipose tissue-derived stromal cells-derived cardiomyocytes. PMID: 21691712
Platelets gal-1 forms an intracellular complex with monomeric actin. PMID: 22081313
Herpesviruses exploit actin and actin-associated myosin motors for viral entry and virion egress. [review] PMID: 21994736
CK2 regulates vaccinia virus dissemination and actin tail formation. PMID: 22209233
Actin playes differential roles in trafficking of Epstein-Barr virus in B cells and epithelial cells. PMID: 22031939
a link between extramuscular expression of alpha-skeletal muscle actin and clinical symptoms in non-skeletal muscle tissues of patients with ACTA1 mutations, and probably a functional role of alpha-skeletal muscle actin during fetal development PMID: 21514153
The filopodium: a stable structure with highly regulated repetitive cycles of elongation and persistence depending on the actin cross-linker fascin PMID: 21975552
Actin accumulates throughout the activated immunological synapse. PMID: 21931536
Actin-EGFP and ezrin-EGFP accumulated below pilus-coated beads when force was applied. PMID: 21340023
Data show that concurrent phosphorylation of cortactin by ERK1/2 and tyrosine kinases enables cells with the ability to regulate actin dynamics. PMID: 21079800
BCL2 interaction with actin in vitro may inhibit cell motility by enhancing actin polymerization PMID: 20716950
Results suggest that actin polymerization and bundling by VASP are critical for spine formation, expansion, and modulating synaptic strength. PMID: 20826790
Centrosomal actin was detected with the anti-actin antibody 1C7 that recognizes antiparallel ("lower dimer") actin dimers. PMID: 21108927
These findings demonstrated that PI3K-mediated actin rearrangements are required for Cronobacter sakazakii invasion of human brain microvascular endothelial cells. PMID: 20809254
Results confirm that DNaseI-binding loop (D-loop) is involved in stabilization of skeletal muscle actin structure, both as monomers and filaments; actin is stabilized by ligands (by phalloidin, aluminum fluoride, & ATP [and to lesser extent by ADP]). PMID: 20718862
Simultaneous tracking of both TCR clusters and GFP-actin speckles reveals their dynamic association and individual flow patterns. Actin retrograde flow directs the inward transport of TCR clusters PMID: 20686692
We conclude that the Drosophila indirect flight muscles provide a good model system for studying ACTA1 mutations PMID: 20452215
Data demonstrate for the first time that L-plastin contributes to the fine-tuning of actin turn-over, an activity which is regulated by Ser5 phosphorylation promoting its high affinity binding to the cytoskeleton. PMID: 20169155
Podocyte BK(Ca) channels are regulated by synaptopodin, Rho, and actin microfilaments. PMID: 20630939
these data identify NHS as a new regulator of actin remodelling. PMID: 20332100
ACTA1 mutations are involved in fiber size disproportion in congenital myotonic dystrophy PMID: 20179953
First insights of S100A10 function as a regulator of the filamentous actin network. PMID: 20100475

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.