Daxx peptide Reference: GTX27879 Daxx is a death domain containing important intermediate in the Fasmediatedapoptosis. It binds to death domain of Fas to enhance theapoptotic pathway and activate JNK pathway. It is widely expressed inhuman and mouse issue.
MDC (CCL22), rat, recombinant Reference: E-67910 Recombinant Rat Macrophage Derived Chemokine (CCL22)
DcR1 peptide Reference: GTX27880 Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors. TRAIL/Apo2L is a new member of the TNF family and induces apoptosis of a variety of tumor cell lines. DR4 and DR5 are the recently identified functional receptors for TRAIL. Two decoy receptors for TRAIL have been identified and designated DcR1/TRID/TRAILR3/ LIT and DcR2/TRAIL-R4/TRUNDD. DcR1 has extracellular TRAIL-binding domain but lacks intracellular signaling domain. It is a glycophospholipid anchored cell surface protein. DcR1 transcripts were expressed in many normal human tissues but not in most cancer cell lines. Overexpression of DcR1 did not induce apoptosis, but attenuated TRAIL-induced apoptosis.
MEC (CCL28), rat, recombinant Reference: E-67940 Recombinant Rat Mucosae-Associated Epithelial Chemokine (CCL28)
ADAM17 peptide Reference: GTX27881 TNF alpha is a pro-inflammatory cytokine and contributes to a variety of inflammatory disease responses and programmed cell death. It is synthesized as a 26K type II membrane-bound precursor that is cleaved by aconvertase to generate secreted 17K mature TNF alpha. TNF alpha converting enzyme (TACE) protein was recently purified and the human and mouse TACE cDNAs were cloned by several groups separately. TACE is a membrane-bound metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease). TACE also processes other cell surface proteins, including TNF receptor, TGF alpha, the L-selectin adhesion molecule, and alpha-cleavage of amyloid protein precursor (APP). TACE mRNA is expressed in a variety of human and murine tissues. TACE was selected as one of the few targets in cytokine activation by the Eighth International Conference of the Inflammation Research Association.
MyD88 peptide Reference: GTX27882 Myeloid differentiation Marker 88 (MyD88) is an adaptor molecule for the Toll/IL-1R and is involved in the inflammatory response induced by IL-1, IL-18 and LPS. MyD88 recruits IRAK to IL-1 receptor complex in response to IL-1. This pathway further leads to activation of NF-kB. MyD88 has a wide tissue distribution.
BACE1 peptide Reference: GTX27883 Amyloid beta peptide is the major constituent of amyloid plaques in the brains of individuals afflicted with Alzheimers disease. This peptide is generated from the beta-amyloid precursor protein (beta APP) in a two-step process. The first step involves cleavage of the extracellular, amino-terminal domain of beta APP. Protein cleavage is performed by an aspartyl protease termed beta-secretase (BACE), of which there are two isoforms, BACE1 and 2. This enzyme is synthesized as a propeptide that must be modified to the mature and active form by the prohormone convertase, furin. Beta APP cleavage by the mature form of BACE results in the cellular secretion of a segment of beta APP and a membrane-bound remnant. This remnant is then processed by another protease termed gamma-secretase. Gamma-secretase cleaves an intra-membrane site in the carboxyl-terminal domain of beta APP, thus generating the amyloid beta peptide. Gamma-secretase is believed to be a multi-subunit complex containing presenilin-1 and 2 as central components. Found associated with the presenilins is the transmembrane glycoprotein nicastrin. Nicastrin has been found to bind to the carboxyl-terminus of beta APP and helps to modulate the production of the amyloid beta peptide. Also found in the neurofibrillary lesions associated with Alzheimers disease is a protein termed Tau. Tau is a neuronal microtubule-associated protein found predominantly on axons. Tau functions to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major constituent of paired helical filaments (PHF), which are the building block of neurofibrillary lesions found in brain tissue of Alzheimers diseased patients.
Caspase 9 peptide Reference: GTX27885 Caspases are cysteine proteases, expressed as inactive precursors, that mediate apoptosis by proteolysis of specific substrates. Caspases have the ability to cleave after aspartic acid residues. There are two classes of caspases involved in apoptosis; initiators (activation by receptor cluster) and effectors (activation by mitochondrial permeability transition). Proapoptotic signals autocatalytically activate initiator caspases, such as Caspase-8 and Caspase-9. Activated initiator caspases then process effector caspases, such as Caspase-3 and Caspase-7, which in turn cause cell collapse.