Recombinant Human DCLK1 Protein

Name: Recombinant Human DCLK1 Protein
Brand: Beta LifeScience
SKU: BLPSN-1550
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	O15075
Synonym	CL1, CLICK1, DCAMKL1, DCDC3A, DCLK
Background	DCAMKL1, also known as DCLK1, is a member of the protein kinase superfamily and the doublecortin family. It contains two N-terminal doublecortin domains, which bind microtubules and regulate microtubule polymerization, a C-terminal serine/threonine protein kinase domain, which shows substantial homology to Ca2+/calmodulin-dependent protein kinase, and a serine/proline-rich domain in between the doublecortin and the protein kinase domains, which mediates multiple protein-protein interactions. DCAMKL1 is involved in several different cellular processes, including neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. Its microtubule-polymerizing activity is independent of its protein kinase activity. DCAMKL1 may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. It may also participate in functions of the mature nervous system.
Description	A DNA sequence encoding the human DCLK1 (- O15075-1) (Met 1-Val 705) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Gly
AA Sequence	Met 1-Val 705
Molecular Weight	The secreted recombinant human DCLK1 consists of 707 a.a. and predicts a molecular mass of 78.5 KDa. The apparent molecular mass of the protein is approximately 64 KDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>80% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, 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.