Analytical Data
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Gene name
ITK
- Application
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Alternative Names
PSCTK2; EMT; LYK; T-cell-specific kinase; Tyrosine-protein kinase Lyk
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q03526
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Expression Region
Leu368~Leu625
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Molecular Weight
59kDa
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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
Recombinant proteins, particularly those produced using the Intein-Mediated Protein Ligation (ITK) method, have garnered significant attention in the fields of biotechnology and molecular biology. The development of recombinant proteins is pivotal for various applications, including drug discovery, vaccine development, and the production of therapeutic enzymes. ITK offers a unique advantage by allowing the precise manipulation of protein sequences through the use of inteins, which are self-splicing proteins. This process enables the seamless joining of protein fragments, facilitating the generation of functional proteins with desired modifications or tags. The ability to produce these proteins in a cost-effective and efficient manner has expanded opportunities for research, as well as for the development of novel therapeutics. Recent advancements in gene editing technologies and expression systems have further enhanced the yield and purity of recombinant proteins, making ITK a powerful tool for protein engineering. Researchers are continually exploring new intein variants and optimizing conditions for their use, which has led to a growing body of literature on ITK-derived proteins in diverse biological and medical contexts. With the increasing demand for personalized medicine and innovative protein therapies, the study of ITK recombinant proteins is poised to make significant contributions to both fundamental research and applied sciences.
