Recombinant Human CSNK1G1 Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-1460

Recombinant Human CSNK1G1 Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-1460
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Product Overview

Tag His&GST
Host Species Human
Accession NP_071331.2
Synonym CK1gamma1
Background Casein kinase I isoform gamma-1, also known as CSNK1G1, is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family and casein kinase I subfamily. Thecasein kinase I family of protein kinases are serine / threonine-selective enzymes that function as regulators ofsignal transductionpathways in most eukaryotic cell types. Casein has been used as a substrate since the earliest days of research on protein phosphorylation. Casein kinase activity associated with the endoplasmic reticulum of mammary glands was first characterized in 1974 and its activity was shown to not depend on cyclic AMP. The CKI family of monomeric serine-threonine protein kinases is found in eukaryotic organisms from yeast to human. Mammals have seven family members: alpha, beta 1, gamma 1, gamma 2, gamma 3, delta, and epsilon. The family members have the highest homology in their kinase domains (53%-98% identical) and differ from most other protein kinases by the presence of the sequence S-I-N instead of A-P-E in kinase domain VIII. The CKI family members appear to have similar substrate specificity and substrate selection is thought to be regulated via subcellular localization and docking sites in specific substrates.
Description A DNA sequence encoding full length of human CSNK1G1 (NP_071331.2) (Met 1-Lys 422) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Met 1-Lys 422
Molecular Weight The recombinant human CSNK1G1/GST chimera consists of 659 a.a. and has a calculated molecular mass of 76.3 kDa. It migrates as an approximately 66 kDa band in SDS-PAGE under reducing conditions.
Purity >94% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity The specific activity was determined to be 4 nmol/min/mg using casein as substrate.
Formulation Supplied as sterile 20mM Tris, 500mM NaCl, 10% gly, pH 7.4.
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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