Other Proteins

RGS1 is a member of the regulator of G-protein signaling family and attenuates the signaling activity of G-proteins. RGS1 binds to activated GTP-bound G alpha subunit and acts as a GTPase activating protein (GAP) thereby increasing the rate of conversion of GTP to GDP and terminating the signal (1). RGS1 is extensively up-regulated in renal cell carcinoma (RCC) tissues and melanoma. In melanoma, RGS1 expression is significantly correlated with increased tumor thickness, mitotic rate and presence of vascular involvement. Furthermore, there is significant association between increasing RGS1 expression and reduced relapse-free survival as well as disease-specific survival (DSS) survival (2). RGS1 Protein is ideal for investigators involved in Signaling Proteins, G-Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, ERK/MAPK Pathway, Inflammation, JNK/SAPK Pathway, p38 Pathway, and PKA/PKC Pathway research.

RHEB is a member of the small GTPase superfamily and encodes a lipid-anchored, cell membrane protein with five repeats of the RAS-related GTP-binding region. RHEB is vital in the regulation of growth and cell cycle progression. RHEB has GTPase activity and shuttles between a GDP-bound form and a GTP-bound form. Drosophila RHEB is a direct target of Tsc2 GTPase-activating protein (GAP) activity both in vivo and in vitro. Point mutations in the Drosophila RHEB gene inhibit cell growth while overexpression promotes cell growth. RHEB functions downstream of Tsc1 and Tsc2 in the mTOR signaling pathway. RHEB 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.

RYK or receptor-like tyrosine kinase is an atypical member of the family of growth factor receptor protein tyrosine kinases. RYK differs from other receptor tyrosine kinases at a number of conserved residues in the activation and nucleotide binding domains (1). RYK has a leucine-rich extracellular domain with a WIF-type WNT binding region, a single transmembrane domain, and an intracellular tyrosine kinase domain. RYK is involved in stimulating WNT signaling pathways such as the regulation of axon path finding (2). RYK Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Neurobiology, Receptor Tyrosine Kinases, and WNT Signaling research..

SCYL1 is a transcriptional regulator belonging to the SCY1-like family of kinase-like proteins. SCYL1 has a divergent N-terminal kinase domain that is thought to be catalytically inactive, and can bind specific DNA sequences through its C-terminal domain. SCYL1 activates transcription of the telomerase reverse transcriptase and DNA polymerase beta genes. SCYL1 forms multimers following transfection into COS-7 cells (1). A SCYL1 binding protein has been identified that co-localized with SCYL1 in cytoplasm and shows ubiquitous expression (2). SCYL1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Inflammation, Invasion/Metastasis, and Neurobiology research.

SCYL3 encodes a protein with a kinase domain and four HEAT repeats which interact with the C-terminal domain of ezrin, an ERM protein which play a role in cell adhesion and migration (1). C-terminal domain of SCYL3 interacts with the C-terminal alpha-helical domain of ezrin. Biochemical assays indicate that SCYL3 had associated rather than intrinsic protein kinase activity. SCYL3 is associated with the cytoplasmic face of the Golgi apparatus. This distribution is dependent upon the presence of the SCYL3 N-terminal myristoylation consensus sequence but is not dependent on an association with ezrin. SCYL3 is highly expressed in breast carcinoma cells and adult colon. SCYL3 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Inflammation, Invasion/Metastasis, and Neurobiology research.

SETD8 or SET domain containing lysine methyltransferase 8 is a lysine methyltransferase that monomethylates p53 in human cell lines. The monomethylation by SETD8 suppresses p53-mediated transcriptional activation of highly responsive target genes, such as p21 (CDKN1A) and PUMA (BBC3) but it has little influence on weak p53 targets (1). Depletion of SET8 augmented the proapoptotic and checkpoint activation functions of p53, and SETD8 expression is downregulated during DNA damage. SETD8 is a Wnt signaling mediator and is recruited by LEF1/TCF4 to regulate the transcription of Wnt-activated genes, possibly through H4K20 monomethylation at the target gene promoters (2). SETD8 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology research.

SETDB2 is a histone H3 methyltransferase that modulates gene expression epigenetically through histone H3 methylation. Methylation of histone H3 at lysine 9 (H3K9) by SETDB2 has emerged as an important player in the formation of heterochromatin, chromatin condensation, and transcriptional repression. SETDB2 is recruited to heterochromatin regions and contributes in vivo to the deposition of trimethyl marks. Depletion of SETDB2 coincides with a loss of CENP proteins and delayed mitosis, suggesting that SETDB2 participates in chromosome condensation and segregation (1). Using positional cloning approach, SETDB2 has been cloned from a quantitative trait locus on chromosome 13q14 that influences immunoglobulin E levels and asthma (2). SETDB2 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology research.

SETMAR or SET domain and mariner transposase fusion gene is a nonhomologous end-joining repair protein that regulates genomic integration of exogenous DNA by opening chromatin and facilitating joining of DNA ends (1). SETMAR has histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. SETMAR also has DNA nicking activity and may play a role in DNA repair (2). Human Pso4 forms a stable complex with SETMAR that regulates Metnase function in DNA repair. SETMAR has sequence-specific DNA-binding activity and recognizes the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element. SETMAR Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology research.

SIRT1 is a member of the sirtuin family of proteins which are homologs to the yeast Sir2 protein. Sirtuin family contain a sirtuin core domain and are grouped into four classes with SIRT1 being a member of class I. SIRT1 is a stress-response and chromatin-silencing factor (1). It is an NAD(+)-dependent histone deacetylase involved in various nuclear events such as transcription, DNA replication, and DNA repair. SIRT1 protein binds and deacetylates the p53 protein (2). Expression of wild type SIRT1 in human cells reduces the transcriptional activity of p53 indicating that SIRT1 is involved in the regulation of p53 function via deacetylation. SIRT1 Protein is ideal for investigators involved in Signaling Proteins, Deacetylase/Demethylase Proteins, Cancer, Cell Cycle, and Inflammation research.