Recombinant Human kynureninase Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3104

Recombinant Human kynureninase Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3104
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Product Overview

Tag His
Host Species Human
Accession Q16719
Synonym KYNUU
Background Genetic studies in mouse and human suggest that kynureninase activity may influence blood pressure and renal function. The gene coding kynureninase (KYNU) is also located on chromosome band 2q14-q23, where a linkage peak for essential hypertension was previously detected in the Chinese Han population.The results show that the rare KYNU variant Arg188Gln affects kynureninase activity and are consistent with the hypothesis that this mutation can predispose to essential hypertension.
Description The recombinant human KYNU consists of 475 amino acids and predicts a molecular mass of 53.7 kDa. The apparent molecular mass of rhKYNU is approximately 47 kDa in SDS-PAGE under reducing conditions.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
Molecular Weight The recombinant human KYNU consists of 475 a.a. and predicts a molecular mass of 53.7 kDa. The apparent molecular mass of rhKYNU is approximately 47 kDa in SDS-PAGE under reducing conditions.
Purity >92% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to oxidize 3-hydroxykynurenine.The specific activity is > 200 pmoles/min/ug.
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.0, 25% gly.
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.

Target Details

Target Function Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
Subcellular Location Cytoplasm, cytosol.
Protein Families Kynureninase family
Database References
Associated Diseases Hydroxykynureninuria (HYXKY); Vertebral, cardiac, renal, and limb defects syndrome 2 (VCRL2)
Tissue Specificity Expressed in all tissues tested (heart, brain placenta, lung, liver, skeletal muscle, kidney and pancreas). Highest levels found in placenta, liver and lung. Expressed in all brain regions.

Gene Functions References

  1. Our results suggest that tryptophan metabolism might dichotomously modulate immune responses, with KYNU as a switch between immunosuppressive versus inflammatory outcomes. PMID: 26725996
  2. A rare variant at the KYNU gene is associated with essential hypertension in the Han Chinese population. PMID: 22012986
  3. The Lys412Glu polymorphism of the KYNU gene in a hypertensive candidate chromosomal region is associated with essential hypertension in Han Chinese. PMID: 16080802

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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