Recombinant Human TLK2 Protein (aa 397-772)

Beta LifeScience SKU/CAT #: BLPSN-4543

Recombinant Human TLK2 Protein (aa 397-772)

Beta LifeScience SKU/CAT #: BLPSN-4543
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Product Overview

Tag aa 397-772
Host Species Human
Accession Q86UE8
Synonym HsHPK, PKU-ALPHA
Background Serine / threonine-protein kinase tousled-like 2, also known as PKU-alpha, Tousled-like kinase 2 and TLK2, is a nucleus protein which belongs to theprotein kinase superfamily and Ser/Thr protein kinase family. The tousled-like kinases are an evolutionarily conserved family of proteins implicated in DNA repair, DNA replication and mitosis in metazoans and plants. Their absence from the yeasts and other eukaryotic 'microbes' suggests a specific role for them in the development of multicellular organisms. Tousled-like kinase 2 / TLK2 is widely expressed. It is present in fetal placenta, liver, kidney, pancreas, heart and skeletal muscle. It is also found in adult cell lines. Tousled-like kinase 2 / TLK2 contains oneprotein kinase domain. Tousled-like kinase 2 / TLK2 is rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly.
Description A DNA sequence encoding the human TLK2 (Q86UE8-1) (Leu397-Asn772) was fused with two additional amino acids (Gly & Pro) at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Gly
AA Sequence Leu397-Asn772
Molecular Weight The recombinant human TLK2 consists of 378 a.a. and has a calculated molecular mass of 43.6 kDa. The recombinant protein migrates as an approximately 44 kDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Supplied as sterile 20mM Tris, 500mM NaCl, 3mM DTT, 10% glycerol, pH 8.0..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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