Recombinant Human PTC2 (PRKAR1A-RET) Protein

Name: Recombinant Human PTC2 (PRKAR1A-RET) Protein
Brand: Beta LifeScience
SKU: BL-0631SG
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_002734NM_020630
Synonym	PRKAR1A: CAR; CNC; CNC1; PKR1; PPNAD1; PRKAR1; TSE1RET: CDHF12, RET51, PTC, RET-ELE1; RET/PTC2
Background	RET/PTC2 is fused of the tyrosine-kinase domain of proto-RET with the regulatory subunit R/A of c-AMP-dependent protein kinase A, by transforming a chromosomal translocation at t(10;17)(q11.2;q23) (1). The RET/PTC oncoproteins display constitutive TK activity and tyrosine phosphorylation. The RET/PTC2 Tyr-539 is an essential docking site for activating the SH2-containing transducer phospholipase PLCgamma (2). The RET/PTC2 activation may play crucial roles in papillary thyroid tumorigenesis and neoplastic oncogene.
Description	Recombinant human RET/PTC2, the fusion protein [PRKAR1A (1-236)-RET (713-end)], was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	713a.a.-end
Molecular Weight	~105 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human PTC2 (PRKAR1A-RET) Protein should be stored should be stored at < -70°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.