85-5961-05　［受注停止］SERPINC1, Recombinant, Human, aa33-464, His-Tag (SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III) 20ug　470254

特徴

• SERPINC1, also known as antithrombin-III, is a member of the Serpin superfamily of the serine protease inhibitors. It is the principal plasma Serpin of blood clotting proteases and inhibits thrombin as well as several factors such as Xa. It is one of the most important coagulation inhibitors and is the basic enzyme for the therapeutic action of heparin. In common with SerpinA5 and D1, the inhibitory activity of SerpinC1 dramatically increases the presence of heparin and other glycosaminoglycans. It mediates the promotion of prostaglandin release, inhibitors of leukocyte activation and down-regulation of many inflammatory cytokines. This protein has anti-inflammatory properties besides anticoagulant.
• Recombinant protein corresponding to aa33-464 from human SERPINC1, fused to His-Tag at C-terminal, expressed in Insect Cell.
• Molecular Weight:~50.1kD (441aa)~50-70kD (SDS-PAGE under reducing conditions)
• Biological Activity:Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 1nM.
• Amino Acid Sequence:ADPHGSPVDI CTAKPRDIPM NPMCIYRSPE KKATEDEGSE QKIPEATNRR VWELSKANSR FATTFYQHLA DSKNDNDNIF LSPLSISTAF AMTKLGACND TLQQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SKLVSANRLF GDKSLTFNET YQDISELVYG AKLQPLDFKE NAEQSRAAIN KWVSNKTEGR ITDVIPSEAI NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SASMMYQEGK FRYRRVAEGT QVLELPFKGD DITMVLILPK PEKSLAKVEK ELTPEVLQEW LDELEEMMLV VHMPRFRIED GFSLKEQLQD MGLVDLFSPE KSKLPGIVAE GRDDLYVSDA FHKAFLEVNE EGSEAAASTA VVIAGRSLNP NRVTFKANRP FLVFIREVPL NTIIFMGRVA NPCVKHHHHH H
• Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 6 months after receipt at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.