Analytical Data
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Gene name
ABRA
- Application
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Alternative Names
ABRAActin-binding Rho-activating Protein; Striated muscle activator of Rho-dependent signaling; STARS
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N0Z2
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Expression Region
1-381aa
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AA Sequence
MAPGEKESGE GPAKSALRKI RTATLVISLA RGWQQWANEN SIRQAQEPTG WLPGGTQDSP QAPKPITPPT SHQKAQSAPK SPPRLPEGHG DGQSSEKAPE VSHIKKKEVS KTVVSKTYER GGDVSHLSHR YERDAGVLEP GQPENDIDRI LHSHGSPTRR RKCANLVSEL TKGWRVMEQE EPTWRSDSVD TEDSGYGGEA EERPEQDGVQ VAVVRIKRPL PSQVNRFTEK LNCKAQQKYS PVGNLKGRWQ QWADEHIQSQ KLNPFSEEFD YELAMSTRLH KGDEGYGRPK EGTKTAERAK RAEEHIYREM MDMCFIICTM ARHRRDGKIQ VTFGDLFDRY VRISDKVVGI LMRARKHGLV DFEGEMLWQG RDDHVVITLL K
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Molecular Weight
43.1 KDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ABRA (Alpha-Actinin-Binding Protein) is a crucial member of the spectrin-repeat protein family, primarily involved in the regulation of actin cytoskeleton dynamics in various cellular contexts. Its significance lies in its ability to interact with alpha-actinin, a key actin-binding protein, thereby influencing muscle contraction, cellular motility, and the integrity of the cytoskeleton. Research has unveiled that ABRA plays an essential role in several physiological processes, including muscle development and repair, as well as the formation of specialized cellular structures. Additionally, aberrant ABRA function has been associated with various pathologies, including cancer, where it may contribute to tumor metastasis through its effects on cell migration and invasion. Recent advances in proteomics and molecular biology have facilitated a deeper understanding of ABRA’s structural characteristics and regulatory mechanisms, making it a focal point for studies aimed at unraveling its multifaceted roles in cell biology. The exploration of ABRA's function and interaction with other cellular components holds promise for the development of therapeutic strategies targeting diseases related to cytoskeletal dysregulation. This research not only helps decipher ABRA's involvement in fundamental cellular processes but also opens avenues for novel interventions in conditions where ABRA is implicated, highlighting its potential as a biomarker or therapeutic target in cancer and other disorders.











