Tenascin is an extracellular matrix glyoprotein which is found in numerous types of tissues, but most predominately in the nervous system. It has been shown to be upregulated at the edge of healing wounds and in the stroma of many tumors. Three types of tenascin have been identified, tenascin-C, which was the first to be identified, tenascin-R, which is found almost exclusively in the central nervous system, and tenascin-X, a mammalian tenascin found in some connective tissue and around blood vessels.

The protein TCP-1 (t-complex polypeptide 1) is a subunit of the hetero-oligomeric complex CCT (chaperonin containing TCP-1) present in the eukaryotic cytosol. The CCT of eukaryotic cytosol is composed of eight different subunit species that are proposed to have independent functions in folding its in vivo substrates, the Actins and Tubulins. TCP-1 was first identified in the mouse as relevant for tail-less and embryonic lethal phenotypes. Sequences homologous to TCP-1 have been isolated in several other species, and the yeast TCP-1 has been shown to encode a molecular chaperone for Actin and Tubulin. TCP-1 found in mammalian cells and yeast plays an important role in the folding of cytosolic proteins.

TCF 4 (T cell factor 4) is a member of the TCF/LEF (lymphoid enhancer factor) family of transcription factors. Members of this family along with catenin, are involved in mediating Wnt signaling by transactivating downstream genes. TCF 4 generates transcriptionally active complexes with catenin in colon carcinoma cells. Expression of TCF 4 is highest in the CNS and intestinal epithelium where Wnt signaling also plays an essential role in development. Aberrant TCF 4 transcription activity has been implicated in carcinogenesis of intestinal and mammary epithlia.

C-TAK1 (Cdc25C associated protein kinase) is a ubiquitously expressed protein kinase found in human tissues and cell lines and can phosphorylate Cdc25C on serine 216 in vitro. C-TAK1 is distinct from the DNA damage checkpoint kinase Chk1 and may regulate interactions between Cdc25C and 14-3-3 in vivo by phosphorylating Cdc25C at serine 216.

Tumor-necrosis factor- is a proinflammatory cytokine and contributes to a variety of inflammatory disease responses and programmed cell death. TNF- is synthesized as a 26K type II membrane-bound precursor that is cleaved by a convertase to generate secreted 17K mature TNF- . TNF- converting enzyme (TACE) protein was recently purified and the human and mouse TACE cDNAs were cloned by several groups separately (1-3). 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 , the L-selectin adhesion molecule, and alpha-cleavage of amyloid protein precursor (APP) (4,5). 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. (6)

This antibody recognizes the 19 kDa protein, -synuclein, which belongs to a family of small cytoplasmic proteins expressed predominantly in neurons. The epitope maps to amino acid residues 121-125 of human -synuclein. -synuclein may be involved in neuronal plasticity and could act as a molecular chaperone that mediates the transformation of soluble A into insoluble amyloid. The protein is a major component of Lewy bodies, the pathological hallmark of ParkinsonÕs disease, and is also observed in senile plaques of AlzheimerÕs disease patients. Human -synuclein appears to be phosphorylated at two major sites, serine 129 and serine 87, and phosphorylation may play a role in the functional regulation of the protein.

Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. A novel IAP protein was recently identified and designated survivin, apoptosis inhibitor 4 (API4), and TIAP1-3. Survivin/TIAP interacted with the processed form of caspase-3 and inhibited its proteolytic activity. Survivin/TIAP is predominantly expressed in tissues of embryos, transformed cell lines, and many human cancers and lymphomas1,3.

Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. A novel IAP protein was recently identified and designated survivin, apoptosis inhibitor 4 (API4), and TIAP1-3. Survivin/TIAP interacted with the processed form of caspase-3 and inhibited its proteolytic activity. Survivin/TIAP is predominantly expressed in tissues of embryos, transformed cell lines, and many human cancers and lymphomas1,3.

Human Ssu72 is a highly conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. The human Ssu72 is located on Chromosome 1p36 and seems to represent a single gene. It was identified as a pRb binding factor and was also shown to interact with TFIIB and yeast PTA1. Rabbit polyclonal antibodies were raised against SSU72 fusion protein. The ABs recognize a single band of ~30 Kda on immunoblots of various human cell lines but do not work well on mouse tissues.

Stanniocalcin 1 is a secreted disulfide-linked homodimeric glycoprotein belonging to the stanniocalcin family of proteins. It is widely expressed and has endocrine/paracrine/autocrine functions relating to calcium and phosphate homeostasis, reproduction, and development. In the ovary, it has been shown to be a paracrine hormone that regulates granulosa cell function. It also has been known to. stimulate renal phosphate reabsorption, and could therefore prevent hypercalcemia._x000B_

Stanniocalcin 1 is a secreted disulfide-linked homodimeric glycoprotein belonging to the stanniocalcin family of proteins. It is widely expressed and has endocrine/paracrine/autocrine functions relating to calcium and phosphate homeostasis, reproduction, and development. In the ovary, it has been shown to be a paracrine hormone that regulates granulosa cell function. It also has been known to. stimulate renal phosphate reabsorption, and could therefore prevent hypercalcemia._x000B_

SPT16 and SSRP1 are found in all eurkaryotic cells and exists as part of an essential heterodimer complex. Together, SPT16 and SSRP1 are a highly abundant nuclear complex that in mammals has been called FACT, or Facilitates Chromatin Transcription. FACT enhances the processivity of RNA polymerase II through nucleosomes. Evidence also points to a role for FACT in replication, possibly by enhancing DNA polymerase through nucleosomes as well.

SPT16 and SSRP1 are found in all eurkaryotic cells and exists as part of an essential heterodimer complex. Together, SPT16 and SSRP1 are a highly abundant nuclear complex that in mammals has been called FACT, or Facilitates Chromatin Transcription. FACT enhances the processivity of RNA polymerase II through nucleosomes. Evidence also points to a role for FACT in replication, possibly by enhancing DNA polymerase through nucleosomes as well.

SPT16 and SSRP1 are found in all eurkaryotic cells and exists as part of an essential heterodimer complex. Together, SPT16 and SSRP1 are a highly abundant nuclear complex that in mammals has been called FACT, or Facilitates Chromatin Transcription. FACT enhances the processivity of RNA polymerase II through nucleosomes. Evidence also points to a role for FACT in replication, possibly by enhancing DNA polymerase through nucleosomes as well.

SPT16 and SSRP1 are found in all eurkaryotic cells and exists as part of an essential heterodimer complex. Together, SPT16 and SSRP1 are a highly abundant nuclear complex that in mammals has been called FACT, or Facilitates Chromatin Transcription. FACT enhances the processivity of RNA polymerase II through nucleosomes. Evidence also points to a role for FACT in replication, possibly by enhancing DNA polymerase through nucleosomes as well.

Rat sphingosine kinase 1 catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (spp)(sphingosine + ATP = sphingosine 1-phosphate + ADP), a lipid mediator with both intra- and extracellular functions. also acts on d-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as d,l-threo-dihydrosphingosine, n,n-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol. The long form of sphingosine kinase 1, an N-terminal extension, is responsible for FceRI-mediated calcium mobilization and may play a role in other ligand mediated signaling events.

The long form of sphingosine kinase 2 (Sphk2-L) is a species-specific isoform of the Sphk2 enzyme expressed in human but not in mouse. It is an N-terminal extended form of Sphk2, extended by 36 amino acids. It functions as expected, catalyzing the formation of sphingosine 1-phosphate from sphingosine, however it appears to have a decreased ability to inhibit DNA synthesis as compared to Sphk2-S (short form of Sphk2). Under normal cellular conditions, Sphk2-L does not appear to inhibit DNA synthesis, but under serum deprivation, SphK2-L translocates to the nucleus and accumlates. This accumlation may be involved in the cessation of cell proliferation or apoptosis depending on the cell type.

Sphingosine Kinase 2 (Sphk2) catalyzes the phosphorylation of sphingosine to sphingosine 1-phosphate (S1P), an important signaling molecule with intra- and extracellular functions. Inside the cell S1P acts as a signaling molecule like other sphingolipid metabolites like ceramide and sphingosine. S1P has been implicated in regulating cell differentiation, calcium mobilization from intracellular stores, and apoptosis. The cell surface receptors for S1P are the EDG family of G protein-coupled receptors (S1P Receptors). These receptors couple to multiple G proteins (e.g. S1P1 couples to Gi whereas S1P2 and S1P3 couple to Gq, G13 in addition to Gi) and regulate a extremely wide range of cellular events including cell motility, survival, apoptosis, migration and cell-cell interaction. Important roles for S1P have also been reported in regulation of cardiogenesis, vascular maturation, oocyte survival, immune cell trafficking, cells of the neuronal system and bone cells. S1P levels are regulated by the activity of Sphk (Sphk1 and Sphk2).

Sphingosine Kinase 1 (Sphk1) catalyzes the phosphorylation of sphingosine to sphingosine 1-phosphate (S1P), an important signaling molecule with intra- and extracellular functions. Inside the cell S1P acts as a signaling molecule like other sphingolipid metabolites like ceramide and sphingosine. S1P has been implicated in regulating cell differentiation, calcium mobilization from intracellular stores, and apoptosis. The cell surface receptors for S1P are the EDG family of G protein-coupled receptors (S1P Receptors). These receptors couple to multiple G proteins (e.g. S1P1 couples to Gi whereas S1P2 and S1P3 couple to Gq, G13 in addition to Gi) and regulate a extremely wide range of cellular events including cell motility, survival, apoptosis, migration and cell-cell interaction. Important roles for S1P have also been reported in regulation of cardiogenesis, vascular maturation, oocyte survival, immune cell trafficking, cells of the neuronal system and bone cells. S1P levels are regulated by the activity of Sphk (Sphk1 and Sphk2).

Sphingosine 1-phosphate (S1P) is a highly bioactive lipid that has a myriad of biological effects both intracellularly as a second messenger and extracellularly by binding to the S1P(1-5)/G-protein-coupled receptors of the endothelial differentiation gene family. Intracellularly, at least two enzymes, sphingosine kinase (1 and 2) and S1P phosphatase, regulate the activity of S1P by governing the phosphorylation of S1P. SPPase2 is localized to the endoplasmic reticulum. The enzymatic activity and localization of SPPase2 are similar to SPPase1. The tissue expression of SPPase2 was different from that of SPPase1. SPPase2 is an important member of the SPPase family which play a role in attenuating intracellular S1P signaling.