caspase-1

Expression system: E. coli
Length: 1-91, Partial
Activity: Not Tested

Expression system: E. coli
Length: 220-480, Partial
Activity: Not Tested

Caspase 14 is a member of the caspase family. Caspases are a kind of cysteine proteinase consisting of a prodomain plus large and small catalytic subunits, that play a central role in cell apoptosis. Caspase 14 possesses an unusually short prodomain and is highly expressed in embryonic tissues but absent from most of the adult tissues except for the skin, which suggests a role in ontogenesis and skin physiology. Unlike the other short prodomain caspases(caspase-3, caspase-6, and caspase-7), Caspase 14 was not processed by multiple death stimuli including activation of members of the tumor necrosis factor receptor family and expression of proapaptotic members of the bcl-2 family. Caspase 14 has been described to be processed and activated by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may take part in keratinocyte terminal differentiation, which is essential for the skin barrier.

DR5, also called TRAIL R2, TRICK 2, TNFRSF10B, and MK is a type 1 TNF R superfamily, membrane protein which is a receptor for TRAIL (APO2 ligand). DR5 is a receptor for the cytotoxic ligand TNFSF10 TRAIL. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis.

AIM2, Absent In Melanoma 2 is a member of the interferon-inducible HIN-200 protein family that contains an amino-terminal pyrin domain and a carboxy-terminal oligonucleotide oligosaccharide-binding domain, senses cytoplasmic DNA by means of its oligonucleotide oligosaccharide-binding domain and interacts with ASC (apoptosis-associated speck-like protein containing a CARD) through its pyrin domain to activate caspase-1. In response to foreign cytoplasmic DNA, AIM2 forms an inflammasome, resulting in caspase activation in inflammatory cells. It had been pointed to a role of AIM2 function in both inflammation and cancer. AIM-2 antigen is expressed in a wide variety of tumor types, including neuroectodermal tumors, as well as breast, ovarian and colon carcinomas. AIM-2 could be used as a tumor antigen target for monitoring vaccine trials or to develop antigen specific active immunotherapy for glioma patients.

Granzyme B(GZMB) contains 1 peptidase S1 domain and belongs to the peptidase S1 family. This enzyme is necessary for target cell lysis in cell-mediated immune responses. It cleaves after Asp and seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. The protein cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis.

Expression system: E. coli
Length: 1-199, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-195, Full Length
Activity: Not Tested

Interleukin-1 beta (IL-1β) is induced by inflammatory signals in a broad number of immune cell types. IL-1β (and IL-18) are the only cytokines which are processed by caspase-1 after inflammasome-mediated activation. IL-1 signaling activates innate immune cells including antigen presenting cells, and drives polarization of CD4 T cells towards T helper type (Th) 1 and Th17 cells. IL-1 beta IL-1F2 Protein, Cynomolgus, Recombinant (His) is expressed in E. coli expression system with C-His tag. The predicted molecular weight is 18.33 kDa and the accession number is A0A2K5VDC7.

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.

Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.

Expression system: E. coli
Length: 1-275, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-193, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-363, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-247, Full Length
Activity: Enzyme activity

Expression system: HEK293 Cells
Length: 1-363, Partial
Activity: Not Tested

DR5, also called TRAIL R2, TRICK 2, TNFRSF10B, and MK is a type 1 TNF R superfamily, membrane protein which is a receptor for TRAIL (APO2 ligand). DR5 is a receptor for the cytotoxic ligand TNFSF10 TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis.

Expression system: E. coli
Length: 117-269, Full Length of Mature Protein
Activity: ELISA、SPR

Expression system: E. coli
Length: 1-195, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 29-175, Partial
Activity: Not Tested

Expression system: E. coli
Length: 2-105, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-199, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-233, Full Length
Activity: Not Tested

Mouse Apoptosis-mediating surface antigen FAS (Fas) belongs to the death receptor subfamily of the TNF receptor superfamily and is designated TNFRSF6. Mouse Fas contains 1 death domain and 3 TNFR-Cys repeats. It detected in various tissues including thymus, liver, lung, heart, and adult ovary. As a receptor for TNFSF6 FASLG, The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both.