Human SET was originally identified as part of the SET-CAN fusion gene produced by a somatic translocation event in a patient with acute undifferentiated leukemia. In developing kidney, SET is highly expressed in the zone of nephron morphogenesis. SET has been shown to be a potent and specific inhibitor of protein phosphatase 2A, a family of major serine/threonine phosphatases involved in regulating cell proliferation and differentiation. SET is also involved in the regulation of renal cell proliferation and tumorigenesis. SET mRNA expression is markedly reduced in cells rendered quiescent by serum starvation, contact inhibition, or differentiation. SET protein expression is also much greater in developing rat and human kidney than in fully differentiated, mature kidney. High levels of SET mRNA and SET protein expression arefound in Wilms' tumor, but not in renal cell carcinoma, adult polycystic kidney disease or in transitional cell carcinoma.

Human SET was originally identified as part of the SET-CAN fusion gene produced by a somatic translocation event in a patient with acute undifferentiated leukemia. In developing kidney, SET is highly expressed in the zone of nephron morphogenesis. SET has been shown to be a potent and specific inhibitor of protein phosphatase 2A, a family of major serine/threonine phosphatases involved in regulating cell proliferation and differentiation. SET is also involved in the regulation of renal cell proliferation and tumorigenesis. SET mRNA expression is markedly reduced in cells rendered quiescent by serum starvation, contact inhibition, or differentiation. SET protein expression is also much greater in developing rat and human kidney than in fully differentiated, mature kidney. High levels of SET mRNA and SET protein expression arefound in Wilms' tumor, but not in renal cell carcinoma, adult polycystic kidney disease or in transitional cell carcinoma.

Sphingolipids play essential roles in various cellular events, including proliferation, differentiation, senescence, apoptosis, and inflammatory responses. Serine palmitoyltransferase (SPT) is the initial and rate-limiting enzyme in the de novo sphingolipid biosynthesis, and thus regulates the level of sphingolipids in cells. Immunohistochemical study revealed widespread distribution of the enzyme with most strong expression in brain and digestive tract. Two subunits, SPT1 and SPT2 at a stoichiometry of 1:1, are involved in the enzymatic activity of SPT.

Sphingolipids play essential roles in various cellular events, including proliferation, differentiation, senescence, apoptosis, and inflammatory responses. Serine palmitoyltransferase (SPT) is the initial and rate-limiting enzyme in the de novo sphingolipid biosynthesis, and thus regulates the level of sphingolipids in cells. Immunohistochemical study revealed widespread distribution of the enzyme with most strong expression in brain and digestive tract. Two subunits, SPT1 and SPT2 at a stoichiometry of 1:1, are involved in the enzymatic activity of SPT.

Axol's rat and human SAP kinase detects native SAP kinase by immunoprecipitation in rat and human (HeLa) cells. SAP kinase is induced by stress agonists such as UV irradiation, heat shock and inflammatory cytokines. These stress stimuli result in the phosphorylation of and enzymatic activation of Stress Activated Protein Kinases (SAP kinases).

Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells.

The function of this binding protein is not fully known. It is known to interact with the S100P and colocalizes with S100P in the nucleus. S100P may stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE). Expressed in brain, spleen, and lung. Not detected in pancreas or liver. In pancreas, expressed predominantly in islet cells and to a lesser extent in acinar cells, but not expressed in ductal cells. Up-regulated in various pancreatic ductal adenocarcinomas and pancreatic intraepithelial neoplasias. Detected in pancreatic ductal adenocarcinoma cells (at protein level). Not detected in non-neoplastic ductal epithelium (at protein level).

Receptor for SLIT1 and SLIT2 which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development. Defects in ROBO1 may be a cause of breast and lung cancer. ROBO1 maps within a region of overlapping homozygous deletions characterized in both small cell lung cancer cell lines (SCLC) and in a breast cancer cell line.

Receptor for SLIT1 and SLIT2 which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development. Defects in ROBO1 may be a cause of breast and lung cancer. ROBO1 maps within a region of overlapping homozygous deletions characterized in both small cell lung cancer cell lines (SCLC) and in a breast cancer cell line.

Receptor for SLIT1 and SLIT2 which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development. Defects in ROBO1 may be a cause of breast and lung cancer. ROBO1 maps within a region of overlapping homozygous deletions characterized in both small cell lung cancer cell lines (SCLC) and in a breast cancer cell line.

This protein is one of two non-identical subunits that constitute ribonucleoside-diphosphate reductase, an enzyme essential for the production of deoxyribonucleotides prior to DNA synthesis in the S phase of dividing cells. The gene for RRM1 is, along with several others, located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region are associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. RRM1 plays an important role in malignancies and disease that involve this region.

Two homologues of the rhombotin gene have now been isolated. One of these, designated Rhom-2, is located on human chromosome 11 at band 11p13, where a cluster of T-cell leukemia-specific translocations occur; all translocation breakpoints at 11p13 are upstream of the Rhom-2 gene. Human and mouse Rhom-2 are highly conserved and, like rhombotin, encode two tandem cysteine-rich LIM domains. Rhom-2 mRNA is expressed in early mouse development in central nervous system, lung, kidney, liver, and spleen but only very low levels occur in thymus. The Rhom-2 gene is such a common site of chromosomal damage in T-cell tumors. Chromosome bands 11p15 (rhombotin) and 11p13 (Rhom-2) are consistent sites of chromosome translocation in T-cell leukemia, with the 11p15 target more rarely involved.

Recognizes specifically a protein of ~60kDa, identified as human retinoic acid receptor (hRAR ). It does not react with hRAR , hRAR isotypes, and human retinoid X receptor (hRXR). Retinoids are metabolites of vitamin A (retinal) and are believed to represent important signaling molecules during vertebrate development and tissue differentiation. Two families of retinoid receptors have been identified. Retinoic acid receptors (RARs) include RAR , RAR and RAR , each of which has a high affinity for all-trans retinoic acids and belongs to the same class of nuclear transcription factors as thyroid hormone receptors, vitamin D3 receptor and ecdysone receptor. The ligand binding domains of the RARs are highly conserved and RAR isoforms are expressed in distinct patterns throught development and in the mature organism. Members of the retinoid X receptor (RXR) family, RXR , RXR and RXR , are activated by 9-cis-retinoic acid, a stereo- and photoisomer of all-trans-RA that is expressed in vivo in both liver and kidney and may represent a widely used hormone.

The immunogen for the anti-human retinoblastoma (Rb) was a recombinant protein corresponding to amino acids 393 to 572 of the human retinoblastoma sequence. Retinoblastoma encodes a phosphorylated protein p110 and binds and regulates E2F transcription factors. Rb functions as a major cell cycle regulator by its ability to repress gene transcription by all three RNA polymerases. In its hypophosphorylated form, Rb binds to a subset of E2F containing complexes converting them to repressors preventing expression of E2F target genes. These complexes repress transcription via E2F binding elements in the promotersof cell cycle control genes, such as E2F-1, c-myc, and cdc2 genes.

The immunogen for the anti-human retinoblastoma (Rb) was a recombinant protein corresponding to amino acids 393 to 572 of the human retinoblastoma sequence. Retinoblastoma encodes a phosphorylated protein p110 and binds and regulates E2F transcription factors. Rb functions as a major cell cycle regulator by its ability to repress gene transcription by all three RNA polymerases. In its hypophosphorylated form, Rb binds to a subset of E2F containing complexes converting them to repressors preventing expression of E2F target genes. These complexes repress transcription via E2F binding elements in the promotersof cell cycle control genes, such as E2F-1, c-myc, and cdc2 genes.

The immunogen for the anti-human retinoblastoma (Rb) was a recombinant protein corresponding to amino acids 393 to 572 of the human retinoblastoma sequence. Retinoblastoma encodes a phosphorylated protein p110 and binds and regulates E2F transcription factors. Rb functions as a major cell cycle regulator by its ability to repress gene transcription by all three RNA polymerases. In its hypophosphorylated form, Rb binds to a subset of E2F containing complexes converting them to repressors preventing expression of E2F target genes. These complexes repress transcription via E2F binding elements in the promotersof cell cycle control genes, such as E2F-1, c-myc, and cdc2 genes.

The immunogen for the anti-human retinoblastoma (Rb) was a recombinant protein corresponding to amino acids 393 to 572 of the human retinoblastoma sequence. Retinoblastoma encodes a phosphorylated protein p110 and binds and regulates E2F transcription factors. Rb functions as a major cell cycle regulator by its ability to repress gene transcription by all three RNA polymerases. In its hypophosphorylated form, Rb binds to a subset of E2F containing complexes converting them to repressors preventing expression of E2F target genes. These complexes repress transcription via E2F binding elements in the promotersof cell cycle control genes, such as E2F-1, c-myc, and cdc2 genes.

The immunogen for the anti-human retinoblastoma (Rb) was a recombinant protein corresponding to amino acids 393 to 572 of the human retinoblastoma sequence. Retinoblastoma encodes a phosphorylated protein p110 and binds and regulates E2F transcription factors. Rb functions as a major cell cycle regulator by its ability to repress gene transcription by all three RNA polymerases. In its hypophosphorylated form, Rb binds to a subset of E2F containing complexes converting them to repressors preventing expression of E2F target genes. These complexes repress transcription via E2F binding elements in the promotersof cell cycle control genes, such as E2F-1, c-myc, and cdc2 genes.

PTP PEST is an 88 kDa cytosolic protein tyrosine phosphatase which is ubiquitiously expressed in mammalian tissues. PTP PEST exhibits a high specific activity when assayed in vitro with artificial tyrosine-phosphorylated substrates. PTP PEST is subject to regulation via phosphorylation of ser 39 and is catalyzed by both protein kinase C and protein kinase A.

PTP µ is a receptor type protein tyrosine phosphatase which is composed of an extracelluar sement containing a MAM domain, an immunoglobulin domain and four ibronectin type III repeats, a transmembrane segment and two intracellular PTP domains. PTP µ is known to bind homolphilically, i.e., PTP µ on one cell will bind to PTP µ on another cell. Axol's PTP µ monoclonal antibody, clone SBK15, was raised against a.a.s 42-60 of of PTP µ coupled to KLH.