Analytical Data
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Gene name
TLN2
- Application
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Alternative Names
TLN2；KIAA0320；Talin-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
Q9Y4G6
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Expression Region
88-406aa
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AA Sequence
RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGAEKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQISQLIAGYIDIILKKK
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Molecular Weight
39.1kDa
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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
TLN2 (talin 2) is a cytoskeletal protein that plays a crucial role in linking integrins to the actin cytoskeleton, thus facilitating cellular adhesion and signaling processes. Research into TLN2 has gained significant attention due to its involvement in various physiological and pathological conditions, including cell migration, tissue repair, and cancer metastasis. The significance of TLN2 is underscored by its differential expression patterns in various tissues and its potential as a biomarker for certain diseases. The reconstitution and study of TLN2 as a recombinant protein allow for detailed investigations into its structural and functional properties, enabling researchers to better understand its mechanisms of action within cells. Furthermore, recombinant TLN2 provides a valuable tool for elucidating the protein's role in cell adhesion dynamics and its interaction with integrin and other cytoskeletal components. This research area holds promise for therapeutic applications, particularly in targeting metastatic pathways in cancer or enhancing wound healing processes. Thus, the exploration of TLN2's functional dynamics through recombinant protein studies not only enhances our understanding of fundamental cellular processes but also opens avenues for innovative clinical strategies.
