api 2

Major allergen Api g 1, isoallergen 2 Protein, Apium graveolens, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 23.1 kDa and the accession number is P92918.

Alpha 2 Antiplasmin SerpinF2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 53.2 kDa and the accession number is P08697-1.

PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Large-pool solvent detergent (SD) plasma for transfusion exhibits reduced alpha 2-antiplasmin (alpha2-AP; SERPINF2) functional activity. The reason for the loss of alpha2-AP has not been described and could be due to the SD incubation itself and or to the processing steps implemented to remove the solvent and the detergent.

XIAP Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 14.3 kDa and the accession number is P98170.

XIAP Protein, Human, Recombinant (Avi) is expressed in E. coli expression system with AVI tag. The predicted molecular weight is 29.1 kDa and the accession number is P98170.

The cellular inhibitor of apoptosis protein-1 (cIAP1) is a member of the Inhibitor of Apoptosis family proteins are (IAP) whose members are characterized by a novel domain of about 70 amino acids termed baculoviral IAP repeats (BIRs). The BIR domains of cIAP1 and cIAP2 bind to caspases, the key effector proteases of apoptosis. The IAP protein family which can enhance cell survival are crucial regulators of programmed cell death. Both cIAP1 and cIAP2 are the E3 ubiquitin protein isopeptide ligases for Smac, taking part in promoting cancer survival through functioning as E3 ubiquitin ligases. Removal of cIAP1 by genetic deletion may result in NF-κB signaling activation that induces TNFα production and in killing sensitive tumor cells through enhanced TNF-R1 death-receptor signaling and caspase 8 activation. The substrate-dependent E3 activity of cIAPs is mediated by their RING domains and is dependent on the specific interactions between cIAPs and Smac. cIAP1 and cIAP2 are also reported to be regulators of NF-kB activation upon TNFαtreatment.