"Prosci"

Supplier: Prosci

AIF Antibody: Apoptosis is characterized by several morphological nuclear changes including chromatin condensation and nuclear fragmentation. These changes are triggered by the activation of members of caspase family, caspase activated DNase, and several novel proteins. A novel gene, the product of which causes chromatin condensation and DNA fragmentation, was recently identified, cloned, and designated apoptosis inducing factor (AIF). Like the critical molecules, cytochrome c and caspase-9, in apoptosis, AIF localizes in mitochondria. AIF translocates to the nucleus when apoptosis is induced and induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. AIF induces chromatin condensation and DNA fragmentation, which are the hallmarks of apoptosis, of the isolated nucleus and the nucleus in live cells by microinjection. AIF is highly conserved between human and mouse and widely expressed.

Supplier: Prosci

Acinus Antibody: Chromatin condensation and nuclear fragmentation (CCNF) is the hallmark of apoptosis. CCNF is triggered by the activation of members of caspase family, caspase activated DNase (CAD/DFF40), and several novel proteins including AIF and CIDE. A new inducer of chromatin condensation was recently identified and designated Acinus (for apoptotic chromatin condensation inducer in the nucleus). Acinus is cleaved by caspase-3 and an additional unknown protease generating a small active peptide p17, which causes chromatin condensation in vitro when it is added to purified nuclei. Acinus also induces apoptotic chromatin condensation in cells. Acinus is ubiquitously expressed. Three different spliced forms of Acinus have been identified in human and mouse and designated AcinusL, AcinusS and AcinusS'.

Supplier: Prosci

Caspase-13 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death is finally caused by members of the caspase family of proteases and caspase activated DNases. A novel member in the caspase family was recently identified and designated ERICE (for Evolutionarily Related Interleukin-1 beta Converting Enzyme) and caspase-13. Caspase-13 belongs to the ICE subfamily of caspases. Overexpression of caspase-13 induces apoptosis. Caspase-13 was activated by caspase-8, which is a key enzyme in death receptor induced apoptosis. Caspase-13 is expressed in a variety of human tissues and cell lines.

Supplier: Prosci

BACE2 Antibody: Accumulation of the amyloid-beta (Abeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. Abeta peptide is generated by proteolytic cleavage of the beta-amyloid protein precursor (APP) at beta- and gamma-sites by proteases. The long-sought beta-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2). A BACE homolog was recently cloned and designated BACE2, Asp1, DRAP (for Down region aspartic protease), and memapsin 1. BACE2 also cleaves APP at beta-site and at a different site within Abeta. BACE2 locates on chromosome 21q22.3, the so-called ‘Down critical region', suggesting that BACE2 and Abeta may also contribute to the pathogenesis of Down syndrome.

Supplier: Prosci

BACE2 Antibody: Accumulation of the amyloid-beta (Abeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. Abeta peptide is generated by proteolytic cleavage of the beta-amyloid protein precursor (APP) at beta- and gamma-sites by proteases. The long-sought beta-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2). BACE/Asp2 is a novel transmembrane aspartic protease and co-localizes with APP. A BACE homolog was recently cloned and designated BACE2, Asp1, DRAP (for Down region aspartic protease), and memapsin 1. BACE2 also cleaves APP at b-site and at a different site within Abeta. BACE2 locates on chromosome 21q22.3, the so-called ‘Down critical region', suggesting that BACE2 and Abeta may also contribute to the pathogenesis of Down syndrome.

Supplier: Prosci

BACE Antibody: Accumulation of the amyloid-beta (Abeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. Abeta peptide is generated by proteolytic cleavage of the beta-amyloid protein precursor (APP) at beta- and gamma-sites by two proteases. APP is first cleaved by beta-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide, which is deposited in the brains of all suffers of Alzheimer's disease. The long-sought beta-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2). BACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.

Supplier: Prosci

SnoN Antibody: TGF-beta is a ubiquitously expressed cytokine that signals through the Smad protein family to regulate numerous cellular processes such as embryonic development and tumorigenesis. This signaling is negatively regulated by Ski, the mammalian homolog of the transforming protein of an avian retrovirus that induces oncogenic transformation of chicken embryo cells, and the related protein SnoN. Like Ski, SnoN functions by binding to the Smad proteins and preventing their phosphorylation, thereby inhibiting their ability to bind DNA and activate the transcription of downstream genes. SnoN is located primarily in the nucleus in cancer tissues or cells, but in the cytoplasm in normal tissues or primary epithelial cells. There are at least four alternately spliced isoforms of SnoN; SnoN antibody will recognize all isoforms (SnoN, SnoN2, SnoI, and SnoA).

Supplier: Prosci

Ski Antibody: TGF-beta is a ubiquitously expressed cytokine that signals through the Smad protein family to regulate numerous cellular processes such as embryonic development and tumorigenesis. This signaling is negatively regulated by Ski, the mammalian homolog of the transforming protein of an avian retrovirus that induces oncogenic transformation of chicken embryo cells, and the related protein SnoN. Ski functions by binding to the Smad proteins and preventing their phosphorylation, thereby inhibiting their ability to bind DNA and activate the transcription of downstream genes. Ski will also bind to the Smad proteins specific to bone morphogenic proteins (BMPs) and block BMP signaling in mammalian cells.

Supplier: Prosci

SkiP Antibody: TGF-beta and the bone morphogenic proteins (BMPs) are key signaling proteins that regulate numerous cellular processes such as embryonic development and tumorigenesis. Both signal through the Smad protein family and are negatively regulated by Ski and SnoN, two related proto-oncoproteins. Ski functions by binding to the Smad proteins activated by TGF-beta and the (BMPs) and preventing their phosphorylation, inhibiting their ability to bind DNA and activate the transcription of downstream genes. SkiP was originally identified as a Ski-interacting protein and was later found to augment the signals induced by TGF-beta but inhibit transcription induced by BMP-2 in C2C12 cells, suggesting that SkiP is a key player in the signaling cascades inititated by TGF-beta and the BMP protein family.

Supplier: Prosci

Nephrin Antibody: Nephrin is strongly expressed in renal glomeruli and is a member of the immunoglobulin family of cell adhesion molecules. Mutations in the Nephrin gene result in congenital nephrotic syndrome, an autosomal-recessive disorder characterized by massive proteinuria in utero and nephrosis at birth. Renal glomeruli allow normal kidneys to filter plasma so that it is very pure. Nephrin is expressed in the podocyte slit-diaphragm of the renal glomeruli in a manner that suggests that Nephrin molecules homodimerize in an anti-parallel fashion similar to cadherin interactions in adherens junctions. Thus, Nephrin may constitute the entire extracellular structure of the slit-diaphragm.

Supplier: Prosci

AIF Antibody: Apoptosis is characterized by several morphological nuclear changes including chromatin condensation and nuclear fragmentation. These changes are triggered by the activation of members of caspase family, caspase activated DNase, and several novel proteins. A novel gene, the product of which causes chromatin condensation and DNA fragmentation, was recently identified, cloned, and designated apoptosis inducing factor (AIF). Like the critical molecules, cytochrome c and caspase-9, in apoptosis, AIF localizes in mitochondria. AIF translocates to the nucleus when apoptosis is induced and induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. AIF induces chromatin condensation and large scale DNA fragmentation, which are the hallmarks of apoptosis, of the isolated nucleus and the nucleus in live cells by microinjection and apoptosis stimuli. AIF is highly conserved between human and mouse and widely expressed.

Supplier: Prosci

FLASH Antibody: A novel mammalian CED-4 homologous was recently identified and cloned in mouse and human and designated FLASH (for FLICE-associated huge protein). FLASH is involved in Fas induced apoptosis. It is recruited to Fas after the receptor cross-linking. Overexpression of wild type of FLASH facilitates and its dominant negative form inhibits Fas induced apoptosis. FLASH interacts with the DEDs of caspase-8 and FADD through the DED-like domain of FLASH and mediates activation of caspase-8. There are parallels between FLASH and Apaf-1/CED-4 although there are arguments against their structural similarity. FLASH is widely expressed.

Supplier: Prosci

Toso Antibody: Apoptosis is an important process by which normal tissue homeostasis and function are maintained. One of the major signals that regulate this process is mediated by the activation of the Fas receptor by its ligand. This leads to the formation of a Fas-associated death domain (FADD)- containing death-inducing signaling complex and the activation of caspase-8, which in turn activates downstream effector caspases, such as caspase-3 and -7. Recent experiments have shown that overexpression of Toso, a novel regulator of Fas-induced apoptosis in lymphoid cells, in Jurkat cells as well as transgenic mice render these cells resistant to Fas-induced apoptosis but not to TRAIL-induced apoptosis. Furthermore, Toso was found to associate with FADD, suggesting that Toso functions by disrupting the formation of the death-inducing signaling complex.

Supplier: Prosci

F1A alpha Antibody: Fas and tumor necrosis factor receptor 1 (TNFR1) are two prototype members in the death receptor family. A novel protein that associates with the intracellular domains of Fas and TNFR1 was recently identified and designated F1Aalpha and FEM1 beta. F1Aalpha/FEM1 beta is the homologue of C. elegans sex determining protein FEM-1. FEM-1/F1Aalpha is cleaved by CED-3 and caspase. FEM-1/F1Aalpha associates with CED-4 and its mammalian homologue Apaf-1. Overexpression of F1Aalpha induces apoptosis. F1Aalpha is therefore a novel member of the death receptor associated protein that mediates apoptosis. F1Aalpha is expressed in a variety of human and mouse tissues.

Supplier: Prosci

RIP3 Antibody: Certain serine/threonine protein kinases, such as ASK1, RIP, DAP, and ZIP kinases, are mediators of apoptosis. Receptor interacting proteins including RIP and RIP2/RICK mediate apoptosis induced by TNFR1 and Fas, two prototype members in the death receptor family. A novel member in the RIP kinase family was recently identified and designated RIP3. RIP3 contains N-terminal kinase domain but, unlike RIP or RIP2, lacks the C-terminal death or CARD domain. RIP3 binds to RIP and TNFR1, mediates TNFR1 induced apoptosis, and attenuates RIP and TNFR1 induced NF-kappa B activation. Overexpression of RIP3 induces apoptosis and NF-kappa B activation. The messenger RNA of RIP3 is expressed in a subset of adult tissues.

Supplier: Prosci

LFG Antibody: Programmed cell death regulates a number of biological processes such as normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. LFG is a recently identified protein that can inhibit the apoptotic signal transduced by the Fas receptor but not from the related tumor necrosis factor-alpha death signal. In this respect, LFG is functionally similar to the anti-apoptotic proteins FAIM, FLIP and Bcl-xL. LFG, a seven membrane spanning protein, can bind the Fas receptor but does not regulate Fas expression or inhibit binding of FADD to Fas. LFG is widely distributed, but highly expressed in the hippocampus and other neural tissues. LFG was also identified as the neural membrane protein 35 (NMP35) and its expression is known to be regulated by the Phosphatidylinositol 3-kinase-Akt/PKB pathway.