Analytical Data
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Gene name
TAGLN2
- Application
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Alternative Names
Epididymis tissue protein Li 7e; SM22-alpha homolog
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P37802
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Expression Region
Ala2~Leu199
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Molecular Weight
15&26kDa
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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
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Protein Description
TAGLN2 (Transgelin-2) is a member of the transgelin family, known for its role in smooth muscle contraction and cellular processes such as migration and adhesion. Research into TAGLN2 has gained attention due to its involvement in various physiological and pathological conditions, including cancer progression, cardiovascular diseases, and tissue remodeling. Studies have demonstrated that TAGLN2 plays a crucial role in regulating the cytoskeletal organization by binding to actin filaments, thereby influencing cell shape and motility. Moreover, alterations in TAGLN2 expression have been linked to the metastatic potential of tumors, highlighting its significance as a potential biomarker and therapeutic target. Reconstructions of the TAGLN2 protein through recombinant expression systems enable detailed investigations into its structure-function relationships and interactions with other cellular components. By producing TAGLN2 as a recombinant protein, researchers can study its biochemical properties, explore its regulatory mechanisms, and assess its involvement in various signaling pathways. This research avenue not only enhances our understanding of TAGLN2's biological functions but also paves the way for developing novel strategies in disease treatment and management. The characterization of TAGLN2 and its signaling roles in disease contexts may ultimately lead to innovations in targeted therapies, thereby improving patient outcomes in conditions where TAGLN2 is implicated.
