Analytical Data
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Gene name
TAGLN2
- Application
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Alternative Names
TAGLN2；KIAA0120；Transgelin-2
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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
P37802
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Expression Region
2-199aa
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AA Sequence
ANRGPAYGL SREVQQKIEK QYDADLEQIL IQWITTQCRK DVGRPQPGRE NFQNWLKDGT VLCELINALY PEGQAPVKKI QASTMAFKQM EQISQFLQAA ERYGINTTDI FQTVDLWEGK NMACVQRTLM NLGGLAVARD DGLFSGDPNW FPKKSKENPR NFSDNQLQEG KNVIGLQMGT NRGASQAGMT GYGMPRQIL
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Molecular Weight
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
Related Products
Protein Description
TAGLN2 (Transgelin-2) is a member of the calponin family of actin-binding proteins, primarily involved in the regulation of smooth muscle contraction and cellular signaling pathways. It plays a crucial role in cytoskeletal dynamics and cellular processes such as cell migration, proliferation, and differentiation. Recent studies have highlighted the significance of TAGLN2 in various physiological and pathological conditions, including cancer metastasis, cardiovascular diseases, and fibrotic disorders. The expression levels of TAGLN2 have been correlated with tumor progression and patient prognosis in certain cancers, making it a potential biomarker and therapeutic target. To better understand its biological functions and implications in disease, researchers have focused on the production and characterization of recombinant TAGLN2 protein. By generating this protein through recombinant DNA technology, scientists aim to elucidate its structural properties, interaction with other cellular components, and its regulatory mechanisms. This research also facilitates the development of targeted therapies aimed at modulating TAGLN2 activity in disease contexts. Overall, the study of TAGLN2 recombinant protein is vital for advancing our understanding of its functions in health and disease, and it holds promise for the development of innovative therapeutic strategies.
