Other Proteins

PRPF19 or pre-mRNA-processing factor 19 is the human homolog of yeast Pso4. PRPF19 is a gene essential for cell survival, DNA repair and association with terminal deoxynucleotidyl transferase (1). PRPF19 forms a stable complex with SETMAR (Metnase) which is a SET and transposase fusion protein in humans and plays a positive role in double-strand break (DSB) repair. PRPF19 mediates association of SETMAR with sites of DNA damage (2). SNEV is an orthologue of PRPF19 and is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly. PRPF19 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Apoptosis/Autophagy, and Cell Cycle Proteins research.

PTEN (phosphatase and tensin homolog) is a tumor suppressor that is frequently mutated in a large number of cancers (1). PTEN has phosphatidylinositol-3, 4, 5-trisphosphate 3-phosphatase activity and contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. Unlike most of the protein tyrosine phosphatases, PTEN preferentially dephosphorylates phosphoinositide substrates and is responsible for negatively regulating the intracellular levels of phosphatidylinositol-3, 4, 5-trisphosphate in cells. PTEN functions as a tumor suppressor by negatively regulating the PI3K/AKT signaling pathway (2). PTEN protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, AKT/PKB Pathway, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, Phosphatases, and WNT Signaling research.

PTK7 or pseudo protein tyrosine kinase 7 is a member of the receptor protein tyrosine kinase family of proteins that transduce extracellular signals across the cell membrane. PTK7 lacks detectable catalytic tyrosine kinase activity but is involved in the WNT signaling pathway and plays a role in multiple cellular processes including polarity and adhesion (1). PTK7 interacts with β-catenin and functions upstream from glycogen synthase kinase 3. PTK7 has been isolated from colon carcinoma and was designated colon carcinoma kinase-4 (2). In conjunction with other T cell markers, PTK7 has utility as a biomarker for detecting minimal residual disease of T-ALL in the bone marrow. PTK7 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, and Neurobiology research.

PTK9 is an actin monomer-binding protein conserved from yeast to mammals which has been localized to cortical G-actin-rich structures that may be regulated by the small GTPase RAC1. PTK9 has tyrosine kinase activity similar to that of recombinant FGFR2, with optimal activity over pH 6.5 to 7.4 and a preference for manganese over magnesium as a divalent cofactor (1). PTK9 plays a central role in regulation of actin dynamics and cell motility in lymphoma cell homeostasis in vivo and represent as a bona fide lymphoma drug target (2). PTK9 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cancer, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, and Neurobiology research.

PTPRM is a member of the protein tyrosine phosphatase family and can participate in a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation (1). PTPRM has been shown to mediate cell-cell aggregation through the interaction with another molecule of PTPRM on an adjacent cell. PTPRM can interact with scaffolding protein RACK1/GNB2L1 and this interaction may be necessary for downstream signaling in response to cell-cell adhesion (2). PTPRM has been shown to be expressed in human pulmonary vascular endothelia where it directly binds to VE-cadherin and regulates both the tyrosine phosphorylation state of VE-cadherin and barrier integrity. PTPRM Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, Neurobiology, and Phosphatases research.

The RAS gene superfamily encodes a group of closely related 21,000 dalton (p21) proteins with special affinity for guanine nucleotides (GTP). RAS and several other cellular proteins with similar biochemical properties are collectively known as G-proteins and they play key roles in a wide variety of cellular activities, including cell growth, differentiation, secretion, and protein trafficking (1). There are three forms of RAS gene in cells termed H-RAS, N-RAS, and K-RAS. RAS proteins play a direct causal role in human cancer and in other diseases. Mutant H-RAS, N-RAS, and K-RAS occur in varying frequencies in different tumor types (2). Other members of the RAS superfamily may also contribute to cancer. RAS Protein is ideal for investigators involved in Signaling Proteins, G-Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, and Neurobiology research.

Rb is the retinoblastoma gene product and was the first tumor suppressor cloned. Rb is a negative regulator of the cell cycle through its ability to bind the transcription factor E2F and repress transcription of genes required for S phase (1). Rb can bind to MDM2 and this overcomes both the antiapoptotic function of MDM2 and the MDM2-dependent degradation of p53. Rb associates with the Polycomb group (PcG) proteins to form a repressor complex that blocks entry of cells into mitosis (2). Rb colocalizes with nuclear PcG complexes and is important for association of PcG complexes with nuclear targets. Rb Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Cancer, Cell Cycle, and Neurobiology research.

Rb is the retinoblastoma gene product and was the first tumor suppressor cloned. Rb is a negative regulator of the cell cycle through its ability to bind the transcription factor E2F and repress transcription of genes required for S phase (1). Rb can bind to MDM2 and this overcomes both the antiapoptotic function of MDM2 and the MDM2-dependent degradation of p53. Rb associates with the Polycomb group (PcG) proteins to form a repressor complex that blocks entry of cells into mitosis (2). Rb colocalizes with nuclear PcG complexes and is important for association of PcG complexes with nuclear targets. Rb Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Cancer, Cell Cycle, and Neurobiology research.

Rel B is part of the NFkB complex and forms heterodimeric complexes with p50 (NFKB1) and p52 (NFKB2) (1). The homodimeric complexes of Rel B alone do not show DNA-binding activity. IHC analysis has shown that Rel B expression correlated with dendritic cell activation. NFkB-inducing kinase NIK is required for osteoclastogenesis in response to pathologic stimuli and overexpression of Rel B rescues differentiation of mouse NIK -/- osteoclast precursors. Rel B is required for RANKL-induced osteoclastogenesis in vitro and for TNF -induced bone resorption in vivo. This indicates that the alternative NFkB pathway, via Rel B, plays an essential and unique role in RANKL signaling toward osteoclast development (2). Rel B Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Apoptosis/Autophagy, Cancer, Inflammation, Neurobiology, and NFkB Pathway research.