Recombinant Human PTK9 Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3957

Recombinant Human PTK9 Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3957
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Product Overview

Tag His&GST
Host Species Human
Accession Q12792
Synonym A6, MGC23788, MGC41876, PTK9
Background Twinfilin-1, also known as Protein A6, Protein tyrosine kinase 9, TWF1 and PTK9, is a cytoplasm protein which belongs to theactin-binding proteins ADF family and Twinfilin subfamily. Twinfilin-1 (TWF1 / PTK9 ) is a highly conserved actin monomer-binding protein that regulates cytoskeletal dynamics in organisms from yeast to mammals. In addition to the mammalian twinfilin-1, a second protein with approximately 65% sequence identity to twinfilin-1 exists in mouse and humans. TWF1 / PTK9 is expressed at high levels in the colon, testis, ovary, prostate and lung. It is expressed at lower levels in the brain, bladder and heart. It is not detected in liver. TWF1 / PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. TWF1 / PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
Description A DNA sequence encoding the human TWF1 isoform 4 (Q12792-4) (Met 1-Asp 252) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met 1-Asp 252
Molecular Weight The recombinant human TWF1/GST chimera consists of 494 a.a. and has a calculated molecular mass of 57 kDa. It migrates as an approximately 50 kDa band in SDS-PAGE under reducing conditions.
Purity >84% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 50mM Tris, 500mM NaCl, 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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