ProSci Inc.

Description:   GPR12 has been identified as a constitutively active Lysophospholipid/Lysosphingolipid receptor.

Description:   Provisional protein phosphatase.

Description:   Anti-BSG Mouse Monoclonal Antibody

Description:   G protein-coupled receptor EX33 is an Orphan-A GPCR with an unknown ligand.

Description:   Anti-GADD45G Goat Polyclonal Antibody

Description:   Cluster of differentiation 14 (CD14), is a cell surface glycoprotein, and is a is a component of the innate immune system. CD14 is a myelomonocytic differentiation antigen preferentially expressed on monocytes, macrophages, and activated granulocytes. CD14 exists in two forms. Either it is anchored into the membrane by a glycosylphosphatidylinositol tail (mCD14) or it appears in a soluble form (sCD14). Soluble CD14 either appears after shedding of mCD14 (48 kDa) or is directly secreted from intracellular vesicles (56 kDa). CD14 acts as a co-receptor (along with the Toll-like receptor TLR 4 and MD-2) for the detection of bacterial lipopolysaccharide (LPS). CD14 can bind LPS only in the presence of lipopolysaccharide-binding protein (LBP). CD14 has been proposed to be involved in various biological processes, including transportation of other lipids, cell-cell interaction during different immune responses, as well as recognition of apoptotic cells. Although LPS is considered its main ligand, CD14 also recognizes other pathogen-associated molecular patterns. CD14+ cells are monocytes that can differentiate into a host of different cells. CD14 has been shown to interact with Lipopolysaccharide-binding protein.

Description:   PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.

Description:   SARS belongs to the class II amino-acyl tRNA family. The enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.This gene belongs to the class II amino-acyl tRNA family. The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser) and is related to bacterial and yeast counterparts.

Description:   PCBP1 appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly (rC)-binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. PCBP1 is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability.This intronless gene is thought to be generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 has paralogues PCBP3 and PCBP4 which is thought to arose as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly (rC)-binding proteins. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability.This intronless gene is thought to have been generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 have paralogues (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly (rC)-binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Description:   Anti-PBX1 Goat Polyclonal Antibody

Description:   VASP (vasodilator-stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. VASP is an actin-associated protein involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping proteins. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments and it plays a role in actin-based mobility of Listeria monocytogenes in host cells. It regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients. Phosphorylation of VASP at Ser157 causes a mobility shift in SDS gel electrophoresis from 46 to 50kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity.

Description:   CD166 antigen is a 100-105 kD typeI transmembrane glycoprotein that is a member of the immunoglobulin superfamily of proteins, which is also known as Activated leukocyte cell adhesion molecule (ALCAM) in human, SC-1/DM-GRASP/BEN in the chicken, and KG-CAM in the rat. CD166 is a cell adhesion molecule that binds to CD6. CD166 involved in neurite extension by neurons via heterophilic and homophilic interactions.

Description:   Cluster of Differentiation 86 (CD86) is also known as B-lymphocyte activation antigen B7-2, is a type I membrane protein that is a member of the immunoglobulin superfamily, and is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B72 is expressed at low levels on monocytes and can be upregulated through interferon γ. CD86 is the ligand for two different proteins on the T cell surface: CD28 (for autoregulation and intercellular association) and CTLA-4 (for attenuation of regulation and cellular disassociation). CD86 works in tandem with CD80 to prime T cells. Recent study has revealed that B7-2 promotes the generation of a mature APC repertoire and promotes APC function and survival. Furthermore, the B7 proteins are also involved in innate immune responses by activating NF-κB-signaling pathway in macrophages. CD86 thus is regarded as a promising candidate for immune therapy. CD86+ macrophages in Hodgkin lymphoma patients are an independent marker for potential nonresponse to firstline-therapy.

Description:   Cluster of Differentiation 86 (CD86) is also known as B-lymphocyte activation antigen B7-2, is a type I membrane protein that is a member of the immunoglobulin superfamily, and is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B72 is expressed at low levels on monocytes and can be upregulated through interferon γ. CD86 is the ligand for two different proteins on the T cell surface: CD28 (for autoregulation and intercellular association) and CTLA-4 (for attenuation of regulation and cellular disassociation). CD86 works in tandem with CD80 to prime T cells. Recent study has revealed that B7-2 promotes the generation of a mature APC repertoire and promotes APC function and survival. Furthermore, the B7 proteins are also involved in innate immune responses by activating NF-κB-signaling pathway in macrophages. CD86 thus is regarded as a promising candidate for immune therapy. CD86+ macrophages in Hodgkin lymphoma patients are an independent marker for potential nonresponse to firstline-therapy.

Description:   The exact function of C3orf64 remains unknown.

Description:   The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex. c-Jun can form either Jun/Jun homodimers or Jun/Fos heterodimers via the leucine repeats in both proteins. Jun B and Jun D, have been shown to be almost identical to c-Jun in their C-terminal regions, which are involved in dimerization and DNA binding, whereas their N-terminal domains, which are involved in transcriptional activation, diverge. JunB is involved in many types of human carcinoma including T-cell lymphomas, CML,primary cutaneous lymphomas. Aberrantly expressed c-Jun and JunB are a hallmark of Hodgkin lymphoma cells, stimulate proliferation and synergize with NF-kappa B. JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction.JunB is an important regulator of erythroid Differentiation.