Recombinant Human CTH Protein

Beta LifeScience SKU/CAT #: BL-2059NP
BL-2059NP: Greater than 85% as determined by reducing SDS-PAGE. (QC verified)
BL-2059NP: Greater than 85% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human CTH Protein

Beta LifeScience SKU/CAT #: BL-2059NP
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

Description Recombinant Human Cystathionine Gamma-Lyase is produced by our E.coli expression system and the target gene encoding Met1-Ser405 is expressed.
Accession P32929
Synonym Cystathionine Gamma-Lyase; Cysteine-Protein Sulfhydrase; Gamma-Cystathionase; CTH
Gene Background Cystathionine Gamma-Lyase (CTH) belongs to the trans-sulfuration enzymes family. CTH exists as a homotetramer and interacts with CALM in a calcium-dependent manner. CTH breaks down cystathionine into cysteine, ammonia and 2-oxobutanoate. CTH catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine and has broad substrate specificity. Defects in CTH will lead to cystathioninuria, which is an autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine.
Molecular Mass 44.7 KDa
Apmol Mass 38-50 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 8% Sucrose, 0.05% Tween 80, pH8.0.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 85% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

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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