Recombinant Human ACTA1 protein, GST-tagged
Cat.No. : | ACTA1-306H |
Product Overview : | Recombinant Human ACTA1 protein(NP_001091.1)(1-377 aa) was fused to GST Tag and expressed in E.coli. |
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Source : | E.coli |
Species : | Human |
Tag : | GST |
Form : | The purified protein was Lyophilized from sterile PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8.). 5 % trehalose and 5 % mannitol are added as protectants before lyophilization. |
Protein length : | 1-377 aa |
AA Sequence : | MCDEDETTALVCDNGSGLVKAGFAG DDAPRAVFPSIVGRPRHQGVMVGMG QKDSYVGDEAQSKRGILTLKYPIEH GIITNWDDMEKIWHHTFYNELRVAP EEHPTLLTEAPLNPKANREKMTQIM FETFNVPAMYVAIQAVLSLYASGRT TGIVLDSGDGVTHNVPIYEGYALPH AIMRLDLAGRDLTDYLMKILTERGY SFVTTAEREIVRDIKEKLCYVALDF ENEMATAASSSSLEKSYELPDGQVI TIGNERFRCPETLFQPSFIGMESAG IHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPS TMKIKIIAPPERKYSVWIGGSILAS LSTFQQMWITKQEYDEAGPSIVHRK CF |
Purity : | 85%, by SDS-PAGE with Coomassie Brilliant Blue staining. |
Stability : | Store for up to 12 months at -20°C to -80°C as lyophilized powder. |
Storage : | Short-term storage: Store at 2-8°C for (1-2 weeks). Long-term storage: Aliquot and store at -20°C to -80°C for up to 3 months, buffer containing 50% glycerol is recommended for reconstitution. Avoid repeat freeze-thaw cycles. |
Reconstitution : | Reconstitute at 0.25 µg/μl in 200 μl sterile water for short-term storage. Reconstitution with 200 μl 50% glycerol solution is recommended for longer term storage (see Stability and Storage for more details). If a different concentration is needed for your purposes please adjust the reconstitution volume as required (please note: the ion concentration of the final solution will vary according to the volume used). Note: Centrifuge vial before opening. When reconstituting, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. |
Gene Name : | ACTA1 actin, alpha 1, skeletal muscle [ Homo sapiens ] |
Official Symbol : | ACTA1 |
Synonyms : | ACTA1; actin, alpha 1, ACTA; ASMA; CFTD; MPFD; NEM1; NEM2; NEM3; CFTD1; CFTDM; |
Gene ID : | 58 |
mRNA Refseq : | NM_001100.3 |
Protein Refseq : | NP_001091.1 |
MIM : | 102610 |
UniProt ID : | P68133 |
Products Types
◆ Recombinant Protein | ||
ACTA1-304H | Recombinant Human ACTA1 Protein (3-377 aa), His-tagged | +Inquiry |
ACTA1-133R | Recombinant Rat ACTA1 Protein, His (Fc)-Avi-tagged | +Inquiry |
ACTA1-281M | Recombinant Mouse ACTA1 Protein, His (Fc)-Avi-tagged | +Inquiry |
ACTA1 -125H | Recombinant Human ACTA1 protein, GST-tagged | +Inquiry |
ACTA1-3090B | Recombinant Bovine ACTA1, His-tagged | +Inquiry |
◆ Native Protein | ||
ACTA1-157R | Native Rabbit skeletal muscle alpha Actin | +Inquiry |
ACTA1-853R | Native Rabbit ACTA1 Protein | +Inquiry |
Acta1-158M | Native Mouse skeletal muscle alpha Actin | +Inquiry |
◆ Lysates | ||
ACTA1-7HCL | Recombinant Human ACTA1 lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (20)
Ask a questionThe Tg(ACTA1)(D286G) mice exhibited decreased activity levels, weaker skeletal muscles, and pathological lesions similar to those observed in human patients. However, unlike the patients, the mice had a normal lifespan.
The ACTA1 protein, also known as skeletal muscle α-actin, plays a crucial role in muscle contraction and the maintenance of muscle structure. It is a key component of the sarcomeres, the structural units of muscle fibers.
The presence of ringbinden fibers in the mouse models suggests that patients with ringbinden fibers of unknown genetic origin should be considered for ACTA1 mutation screening, indicating a possible link between these features and ACTA1 mutations.
ACTA1 is inhibited by PAX3-FOXO1 both at the transcriptional level and the protein level. This inhibition occurs through the RhoA-MKL1-SRF signaling pathway.
Researchers employ various techniques to study the ACTA1 protein, such as immunohistochemistry, immunoblotting, and mass spectrometry. These methods help identify the presence, abundance, and localization of ACTA1 in muscle tissues or cells.
Mutations in the ACTA1 gene account for a significant proportion of NM cases. Most of these mutations are missense mutations, which cause autosomal dominant NM by producing an abnormal protein. However, about 10% of ACTA1 gene mutations are associated with autosomal recessive NM, resulting in loss of protein function.
Yes, the ACTA1 protein interacts with other proteins involved in muscle function and structure. For example, it forms complexes with other actin-binding proteins, such as myosin and tropomyosin, to regulate muscle contraction.
Mutations in the skeletal muscle α-actin gene (ACTA1) cause various congenital myopathies, resulting in severe skeletal muscle weakness in most patients.
The majority of ACTA1 gene mutations cause autosomal dominant NM, meaning a single abnormal copy of the gene is sufficient to cause the disorder. In contrast, approximately 10% of ACTA1 gene mutations lead to autosomal recessive NM, requiring two copies of the mutated gene (one from each parent) to manifest the disorder.
The RhoA-MKL1-SRF signaling pathway is involved in mediating the inhibition of ACTA1 by PAX3-FOXO1. It is a signaling cascade that transmits the inhibitory signals from PAX3-FOXO1 to downregulate the expression of ACTA1.
The expression and regulation of the ACTA1 protein in skeletal muscle are tightly controlled by various molecular mechanisms, including transcriptional and post-transcriptional processes. These mechanisms ensure proper levels of ACTA1 for muscle function.
Mass spectrometry analysis revealed that the skeletal muscles of Tg(ACTA1)(D286G) mice contained approximately 25% of the ACTA1(D286G) protein.
CTA1 mutations can disrupt the normal organization of muscle fibers and sarcomeres, leading to structural abnormalities. These abnormalities can include the presence of nemaline bodies, actin accumulations, and widespread sarcomeric disarray.
Mutations in the ACTA1 gene can lead to various congenital myopathies, which are muscle disorders present from birth or early infancy. These mutations can disrupt the normal function and structure of skeletal muscles.
ACTA1 mutations can result in severe skeletal muscle weakness, leading to difficulties in movement and muscle function. In some cases, the severity of the mutations can be life-threatening, causing reduced lifespan and early mortality, as seen in certain dominant ACTA1 mutations.
Yes, there are various types of ACTA1 mutations identified in patients with congenital myopathies. These mutations can have different effects on the structure and function of the ACTA1 protein, leading to a spectrum of clinical presentations and disease severity.
Studies have suggested that altering the ratio of mutant ACTA1 protein to wild-type actin protein in patient muscles may hold promise as a potential therapy for patients with dominant ACTA1 disease
The ACTA1 protein is primarily found in skeletal muscle, which is responsible for voluntary muscle movement in the body.
The inhibition of ACTA1 by PAX3-FOXO1 is believed to play a role in the tumorigenesis and development of alveolar rhabdomyosarcoma (ARMS). It suggests that this regulatory mechanism contributes to the disease progression.
Altering the ratio of mutant ACTA1 protein to wild-type actin in patient muscle may be a potential therapy for patients with dominant ACTA1 disease.
Customer Reviews (5)
Write a reviewI found the protein product to be highly stable, retaining its functionality even after months of storage, which was crucial for my long-term experiments
The protein product's reliable performance and consistent quality reassured me that it would not introduce any confounding factors or jeopardize the integrity of my experiments.
I found the protein product to be compatible with various downstream applications, such as Western blotting and ELISA, broadening its utility in my researc
I appreciated the convenient packaging of the protein product, with individual aliquots that reduced the need for repeated thawing and freezing.
I appreciated the protein product's consistent performance at the specified concentrations, enabling me to achieve accurate dosing in my experiments
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