Analytical Data
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Gene name
TAGLN
- Application
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Alternative Names
TAGLN；SM22；Transgelin
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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
Q01995
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Expression Region
1-201aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMANKGPSYGMSREVQSKIEKKYDEELEERL VEWIIVQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPDGSKPVKVP ENPPSMVFKQMEQVAQFLKAAEDYGVIKTDMFQTVDLFEGKDMAAVQRTL MALGSLAVTKNDGHYRGDPNWFMKKAQEHKREFTESQLQEGKHVIGLQMG SNRGASQAGMTGYGRPRQIIS
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Molecular Weight
25 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
Tropomyosin-1 (TAGLN), a member of the tropomyosin family, is an actin-binding protein that plays a crucial role in various cellular processes, such as cytoskeletal organization, cell migration, and signal transduction. Its expression is predominantly observed in smooth muscle cells and non-muscle cells, and it has been linked to several physiological and pathological processes, including development, cancer progression, and response to injury. Recent studies have highlighted TAGLN's involvement in regulating cell shape and motility, making it a potential target for therapeutic intervention in diseases characterized by abnormal cell behavior. Additionally, the reorganization of TAGLN can influence the remodeling of the extracellular matrix, further emphasizing its significance in cellular dynamics. Investigating the recombinant forms of TAGLN can provide insights into its structural and functional properties, enhancing our understanding of its role in health and disease. This background sets the stage for exploring TAGLN's potential as both a biomarker and a therapeutic target in various clinical contexts.
