Analytical Data
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Gene name
TLN1
- Application
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Alternative Names
TLN1；KIAA1027；TLN；Talin-1
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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
Q9Y490
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Expression Region
92-399aa
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AA Sequence
MLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKEEITGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWNLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDII
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Molecular Weight
62.8 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
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Protein Description
TLN1 (Talin-1) is a cytoskeletal protein integral to the formation of focal adhesions, serving as a crucial link between integrins and the actin cytoskeleton. It plays a pivotal role in cellular processes such as adhesion, migration, and signaling, making it a key player in various physiological and pathological conditions, including cancer metastasis and cardiovascular diseases. Research into TLN1 has expanded its significance beyond cell adhesion to include its involvement in mechanotransduction—the process by which cells sense and respond to mechanical stimuli. Given that TLN1 is essential for the transmission of signals from the extracellular matrix to the cell interior, understanding its structural and functional dynamics is critical. Recent advances in protein engineering and recombinant protein technologies have enabled the production of TLN1 in a laboratory setting, allowing for detailed studies on its biochemical interactions, conformational changes, and role in cell behavior. Investigating TLN1 as a recombinant protein can provide insights into its function and potential as a therapeutic target, particularly in diseases where mechanotransduction pathways are disrupted. Thus, the exploration of TLN1 through recombinant protein studies holds promise for unveiling new therapeutic strategies and understanding cellular mechanics at a deeper level.
