Recombinant humaan vitamine D-bindeiwit/VDB/Gc-globuline (C-6His)

Source: Human Cells. MW :52.3kD. Recombinant Human Vitamin D-Binding Protein is produced by our Mammalian expression system and the target gene encoding Leu17-Leu474 is expressed with a 6His tag at the C-terminus. Vitamin D-Binding Protein (DBP) is a member of the ALB/AFP/VDB family. DBP is a secreted protein and contains three albumin domains. The primary structure contains 28 cysteine residues forming multiple disulfide bonds. DBP acts as a multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid, and urine and on the surface of many cell types. DBP binds to vitamin D and its plasma metabolites and transports them to target tissues. DBP associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes.

GC

2638

P02774

Lyophilized from a 0.2 μm filtered solution of 20mM PB,150mM NaCl, pH7.2.

The product is shipped at ambient temperature.

Lyophilized protein should be stored at -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at -20°C for 3 months.

Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. Endotoxin : Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test.

LERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKRSDFASNCCSINSPPLYCDSEIDAELKNILVDHHHHHH