Recombinant Human ACTBL2 Protein, His (Fc)-Avi-tagged
Cat.No. : | ACTBL2-2418H |
Product Overview : | Recombinant Human ACTBL2 with His (Fc)-Avi tag was expressed and purified |
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Source : | HEK293 |
Species : | Human |
Tag : | His (Fc)-Avi |
Endotoxin : | < 1.0 EU per μg of the protein as determined by the LAL method |
Purity : | ≥85% by SDS-PAGE |
Stability : | Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
Storage : | For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles. |
Storage Buffer : | PBS buffer |
Gene Name : | ACTBL2 actin, beta-like 2 [ Homo sapiens ] |
Official Symbol : | ACTBL2 |
Gene ID : | 345651 |
mRNA Refseq : | NM_001017992.3 |
Protein Refseq : | NP_001017992.1 |
MIM : | 614835 |
UniProt ID : | Q562R1 |
Products Types
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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 (21)
Ask a questionActbl2 is postulated to be essential for cell motility based on its functional impact on various cellular processes related to cell movement.
The discovery of ACTBL2 adds to our understanding of the molecular landscape of CRC and holds potential for the development of marker panels for improved early cancer detection.
CR-ACTBL2 cells, with knocked-out ACTBL2, and OE-ACTBL2 cells, overexpressing actbl2, differed from control cells in invasion, focal adhesion formation, actin polymerization ratio, and the formation of lamellipodia and stress fibers.
The findings highlight the negative prognostic impact of ACTBL2 in EOC, suggesting its importance as a potential marker for the disease.
ACTBL2 is identified as a significant pivotal regulator in a dysfunction module associated with thymoma, suggesting its involvement in the molecular dysregulation of the disease.
Knocking out or overexpressing actbl2 in melanoma cells results in differences in invasion, focal adhesion formation, actin polymerization ratio, and the formation of lamellipodia and stress fibers.
Actbl2 is believed to be an important factor for cell motility based on the observed effects on cell behavior, suggesting its involvement in regulating cellular movement.
Yes, siRNA knockdown of NFAT5 led to downregulation of ACTBL2, suggesting a molecular interplay between the two proteins.
Actbl2 is believed to be the seventh actin isoform and plays an essential role in cell motility.
Actbl2 exhibits the largest number of non-conserved amino acid substitutions among all actins.
Yes, ACTBL2 shows potential as a therapeutic target in thymoma, based on its identification as an important component of thymoma molecular dysregulation.
ACTBL2 plays a role in supporting vascular smooth muscle cell (VSMC) migration and is involved in the alignment with stress fibers and dispersion in lamellipodia.
EOC cell lines showed significantly increased mRNA and protein levels of ACTBL2 compared to the benign control.
The divergence of actin groups, including actbl2, started at the beginning of vertebrate evolution.
ACTBL2 is expressed at a low level in several melanoma cell lines, but a small subset of cells shows high ACTBL2 expression.
ACTBL2 has been identified as a novel protein that is upregulated in CRC, potentially serving as a marker for early cancer detection.
Biomechanical stretch acts as a determinant for NFAT5 expression and nuclear translocation, which controls the expression of cytoskeletal protein ACTBL2.
SiRNA knockdown of ACTBL2 resulted in significantly reduced cellular viability, proliferation, and migration in vitro.
ACTBL2 expression is inhibited in cells when NFAT5 is knocked down using siRNA.
The study suggests that ACTBL2 plays a crucial role in ovarian carcinogenesis by modulating cellular motility and proliferation.
Actbl2 has a separate evolutionary history from muscle actins and exhibits the largest number of non-conserved amino acid substitutions among all actins.
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