HEK293 cells.
Corticosteroid-binding globulin, CBG, Serpin A6, Transcortin, Serpina6.
Greater than 95.0% as determined by SDS-PAGE.
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SERPINA6 Human Recombinant is a single, glycosylated polypeptide chain containing 389 amino acids (23-405a.a) and having a molecular mass of 43.5kDa (calculated). SERPINA6 is fused to a 6 a.a His tag at C-terminal.
Belonging to the serpin superfamily, SERPINA6 (Serpin Peptidase Inhibitor, Clade A Member 6) is produced and released by liver hepatocytes, and is present in cells responsive to glucocorticoids. SERPINA6 levels are modulated by estrogens. As the primary carrier for progestins and glucocorticoids in the bloodstream, SERPINA6 plays a crucial role in regulating their bioavailability, metabolic breakdown, cellular uptake, and protection from chemical and enzymatic degradation. SERPINA6 possesses a single steroid binding site with a strong affinity for cortisol and progesterone. It binds to approximately 80-90% of circulating cortisol, rendering it biologically inactive. Conversely, unbound cortisol represents the biologically active form. Consequently, the concentration of SERPINA6 directly influences the active fraction of plasma cortisol. Genetic defects in SERPINA6 can lead to corticosteroid-binding globulin deficiency (CBG deficiency), a rare disorder characterized by decreased CBG production, resulting in hypo/hypertension and muscle fatigue.
Human Recombinant SERPINA6 is a single, glycosylated polypeptide chain consisting of 389 amino acids (23-405a.a). With a molecular weight of 43.5kDa (calculated), it features a 6 a.a His tag at the C-terminal.
The product is prepared by subjecting SERPINA6 to a 0.4 μm filtration process, followed by lyophilization from a 0.5mg/ml solution in PBS at pH 7.5.
To create a working solution with an approximate concentration of 0.5mg/ml, add deionized water to the lyophilized pellet and allow it to fully dissolve.
Store the lyophilized protein at -20°C. To prevent repeated freeze-thaw cycles, aliquot the product after reconstitution. The reconstituted protein exhibits stability at 4°C for a limited duration, showing no noticeable changes over a two-week period at this temperature.
The purity of the protein is determined to be greater than 95.0% based on SDS-PAGE analysis.
Corticosteroid-binding globulin, CBG, Serpin A6, Transcortin, Serpina6.
HEK293 cells.
MDPNAAYVNM SNHHRGLASA NVDFAFSLYK HLVALSPKKN IFISPVSISM ALAMLSLGTC GHTRAQLLQG LGFNLTERSE TEIHQGFQHL HQLFAKSDTS LEMTMGNALF LDGSLELLES FSADIKHYYE SEVLAMNFQD WATASRQINS YVKNKTQGKI VDLFSGLDSP AILVLVNYIF FKGTWTQPFD LASTREENFY VDETTVVKVP MMLQSSTISY LHDSELPCQL VQMNYVGNGT VFFILPDKGK MNTVIAALSR DTINRWSAGL TSSQVDLYIP KVTISGVYDL GDVLEEMGIA DLFTNQANFS RITQDAQLKS SKVVHKAVLQ LNEEGVDTAG STGVTLNLTS KPIILRFNQP FIIMIFDHFT WSSLFLARVM NPVHHHHHH
SERPINA6 plays a crucial role as the major transport protein for glucocorticoids and progestins in the blood of most vertebrates . It binds to corticosteroids with high affinity, thereby regulating their bioavailability and activity. This binding helps maintain homeostasis and modulates the body’s response to stress .
Serpins, including SERPINA6, inhibit their target proteases through an irreversible mechanism. They undergo a significant conformational change that disrupts the active site of the target protease, effectively inhibiting its activity . This mechanism is distinct from the more common competitive inhibition, where inhibitors bind to and block access to the protease active site .
Mutations in the SERPINA6 gene can lead to Corticosteroid-Binding Globulin Deficiency, a condition characterized by reduced levels of CBG in the blood. This deficiency can result in altered cortisol levels and an impaired stress response . Additionally, SERPINA6 has been associated with Vitamin D Hydroxylation-Deficient Rickets, Type 1B, highlighting its importance in various metabolic pathways .