27728 Results for: "affinity chromatography"

Supplier: Prosci

TSPAN12 is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility.The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility.

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Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.

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PSMC3IP plays an important role in meiotic recombination. It stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. It may inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3.

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S100 calcium binding protein A1 (S100-alpha/ S100A1), The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of this protein has been implicated in cardiomyopathies.

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Cortactin is overexpressed in breast cancer and squamous cell carcinomas of the head and neck. The encoded protein is localized in the cytoplasm and in areas of the cell-substratum contacts. This gene has two roles: (1) regulating the interactions between components of adherens-type junctions and (2) organizing the cytoskeleton and cell adhesion structures of epithelia and carcinoma cells. During apoptosis, the encoded protein is degraded in a caspase-dependent manner. The aberrant regulation of this gene contributes to tumor cell invasion and metastasis. Two splice variants that encode different isoforms have been identified for this gene.

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Stem Cell Factor (SCF) is a hematopoietic growth factor that exerts its activity at the early stages of hematopoiesis. SCF stimulates the proliferation of mast cells and is able to augment the proliferation of both myeloid and lymphoid hematopoietic progenitors in bone marrow culture. It also mediates cell to cell adhesion and acts synergistically with other cytokines, probably interleukins. A soluble form is produced by proteolytic processing of isoform 1 in the extracellular domain.

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RNF10 contains a ring finger motif, which is known to be involved in protein-protein interactions. The specific function of this protein has not yet been determined. EST data suggests the existence of multiple alternatively spliced transcript variants, however, their full length nature is not known.The protein encoded by this gene contains a ring finger motif, which is known to be involved in protein-protein interactions. The specific function of this protein has not yet been determined. EST data suggests the existence of multiple alternatively spliced transcript variants, however, their full length nature is not known.

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FKHR belongs to the forkhead family of transcription factors, which are characterized by a distinct forkhead domain. It may play a role in myogenic growth and differentiation. The mammalian DAF-16-like transcription factors, FKHR, FKHRL1, and AFX, function as key regulators of insulin signaling, cell cycle progression, and apoptosis downstream of phosphoinositide 3-kinase. Gene activation through binding to insulin response sequences has been essential for mediating these functions. D-type Cyclins (in Class III) is required for FKHR mediated inhibition of cell cycle progression and transformation. FKHR gene is mapped to chromosome 13q14

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SDPR Antibody: The serum deprivation-response protein (SDPR) is a calcium-independent phospholipid-binding protein whose expression is increased in serum-starved cells. SDPR is a substrate for protein kinase C (PKC) phosphorylation and recruits the polymerase I and transcript release factor (PTRF) to caveolae. Removal of this protein causes caveolae loss and its over-expression results in caveolae deformation and membrane tubulation. Both SDPR and PTRF, as well as the other member of the cavin family PRKCDBP were down regulated in breast cancer cell lines and breast tumor tissue, suggesting that expression of the cavin family proteins could be a useful prognostic indicator of breast cancer progression.

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TACI is a lymphocyte specific member of the tumor necrosis factor (TNF) receptor superfamily. It interacts with calcium-modulator and cyclophilin ligand (CAML). The protein binds to both APRIL and BAFF and induces activation of the transcription factors NFAT (nuclear-factor of activated T cells), AP1, and NF kappa B and plays a crucial role in humoral immunity by interacting with a TNF ligand. This gene is located within the Smith Magenis syndrome region on chromosome 17.

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CARM1 Antibody: Protein arginine N-methyltransferases, such as CARM1, catalyze the transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine. Protein arginine methylation has been implicated in signal transduction, metabolism of nascent pre-RNA, and transcriptional activation. CARM1 functions as a transcriptional co-activator for various nuclear receptors and NF-κB. It has also been shown to methylate histone H3 arginines, inhibiting the binding of corepressors and protecting chromatin from deacetylation, thereby facilitating transcription.

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IL-17RE Antibody: The interleukin 17 receptor E (IL-17RE) shares limited similarity to the receptor of IL-17A, a ubiquitous type I membrane glycoprotein that with IL-17A plays a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. IL-17RE is the functional receptor of IL-17C and has been suggested to mediate mucosal immunity to infection with intestinal pathogens. IL-17C is produced by epithelia in response to bacterial challenge and binds to a receptor complex formed by IL-17RE and IL-17RA on the epithelial cell surface, thereby regulating the immune function of epithelial cells in an autocrine manner.

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The protein encoded by BAD gene is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

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ALG6 is a member of the ALG6/ALG8 glucosyltransferase family. It catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene encoding ALG6 are associated with congenital disorders of glycosylation type Ic.This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic. 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.

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ST14 is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.

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Midkine exhibits neurite outgrowth-promoting activity and may play a role in nervous system development and/or maintenance. Its expression is predominant only for a short period from approximately one-half to two-thirds of the way through gestation; before and after that, it is barely detectable. Midkine was first found in differentiating mouse teratocarcinoma cells. It has neurotrophic activities and is mitogenic to certain, but not to all, fibroblast cell lines.

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ENA-78 is a a 9.9kD inflammatory chemokine that belongs to the CXC chemokine family. ENA-78 is expressed by fibroblasts, is induced by bacterial lipopolysaccharides, and is chemotactic for neutrophils. This chemokine is produced concomitantly with Interleukin 8 (IL8) in response to stimulation with either Interleukin 1 (IL1) or Tumor Necrosis Factor alpha (TNFA). This chemokine is a potent chemotaxin involved in neutrophil activation.

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SPP1 Antibody: The secreted protein 1 (SPP1), also known as osteopontin, is a major noncollagenous protein of bone, but is also found in the extracellular matrix of other mineralized tissues and in bodily fluids. In bone, SPP1 is produced by osteoblasts, osteocytes, macrophages, and osteoclasts (1,2). SPP1 binds to cells through integrin and non-integrin receptors, as well as the adhesion receptor CD44 in an RGD-independent manner, enabling SPP1 to induce a number of functional effects including macrophage chemotaxis, cytoprotection, and regulation of T helper type 1 cells. SPP1 can regulate biomineralization by inhibiting the formation of hydroxyapatite (3) and the growth of calcium oxalate crystals.

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Nucleoporins are the main components of the nuclear pore complex (NPC) of eukaryotic cells. They are involved in the bidirectional trafficking of molecules, especially mRNAs and proteins, between the nucleus and the cytoplasm. NUP155 does not contain the typical FG repeat sequences found in most vertebrate nucleoporins.Nucleoporins are the main components of the nuclear pore complex (NPC) of eukaryotic cells. They are involved in the bidirectional trafficking of molecules, especially mRNAs and proteins, between the nucleus and the cytoplasm. The protein encoded by this gene does not contain the typical FG repeat sequences found in most vertebrate nucleoporins. Two protein isoforms are encoded by transcript variants of this gene.

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The protein encoded by BAD gene is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

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Interleukin 28 (IL-28B), also known as interferon lambda 3, is cytokine distantly related to type I interferons and the IL-10 family. The IL-28B gene and the closely related cytokine genes IL-28A and IL-29 form a cytokine gene cluster on a chromosomal region mapped to 19q13. Expression of the cytokines encoded by the three genes can be induced by viral infection and can induce anti-viral activity. All three cytokines have been shown to interact with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor-beta (IL10RB) and interleukin 28 receptor-alpha (IL28RA).

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GRIP1 Antibody: Glutamate receptors play an important role in neural plasticity, development and degeneration. The glutamate receptor interacting proteins, GRIP1 and GRIP2, members of the PDZ domain-containing protein family, mediate the trafficking and membrane organization of a number of transmembrane proteins. GRIP1 and GRIP2 specifically bind to the AMPA receptor subunits, GluR 2/3 and are involved in the targeting of GluR 2/3 to the synapse. GRIP1 is expressed in early development before the expression of AMPA receptors, while GRIP2 expression parallels that of AMPA receptors during later developmental stages. GRIP1 and GRIP2 may be involved in the induction of cerebellar long-term depression (LTD).

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PTRF Antibody: The polymerase I and transcript release factor (PTRF) enables the dissociation of paused ternary polymerase I transcription complexes from the 3' end of pre-rRNA transcripts, regulating rRNA transcription by promoting the dissociation of transcription complexes and the re-initiation of polymerase I on nascent rRNA transcripts. PTRF also localizes to caveolae at the plasma membrane and is thought to play a critical role in the formation of caveolae and the stabilization of caveolins, translocating from caveolae to the cytoplasm after insulin stimulation. PTRF is also thought to modify lipid metabolism and insulin-regulated gene expression. Mutations in this gene result in a disorder characterized by generalized lipodystrophy and muscular dystrophy.

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ALDOC gene is a member of the class I fructose-biphosphate aldolase gene family. ALDOC is a glycolytic enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehyde, respectively.This gene encodes a member of the class I fructose-biphosphate aldolase gene family. Expressed specifically in the hippocampus and Purkinje cells of the brain, the encoded protein is a glycolytic enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehyde, respectively.

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KIRREL (NEPH1) is a member of the nephrin-like protein family, which includes NEPH2 and NEPH3. The cytoplasmic domains of these proteins interact with the C terminus of podocin (NPHS2), and the genes are expressed in kidney podocytes, cells involved in ensuring size- and charge-selective ultrafiltration. NEPH1 is a member of the nephrin-like protein family, which includes NEPH2 (MIM 607761) and NEPH3 (MIM 607762). The cytoplasmic domains of these proteins interact with the C terminus of podocin (NPHS2; MIM 604766), and the genes are expressed in kidney podocytes, cells involved in ensuring size- and charge-selective ultrafiltration (Sellin et al., 2003 [PubMed 12424224]).

Supplier: Prosci

Interleukins (ILs) are a large group of cytokines that are produced mainly by leukocytes, although some are produced by certain phagocytes and auxiliary cells. ILs have a variety of functions, but most function to direct other immune cells to divide and differentiate. Each IL acts on a specific, limited group of cells through a receptor specific for that IL.

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Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation.

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VTCN1 Antibody: T cell immunity plays a critical role in host immune surveillance of tumour cell growth and metastatic spread. VTCN1, also known as B7-H4, is a member of the B7 family of immune regulatory molecules. Expressed primarily on the membrane of lymphoid cells, VTCN1 is an immunoinhibitory protein that interacts with receptors on the surface of T lymphocytes, thus mediating cellular and humoral immune responses. Overexpression of VTCN1 is associated with certain malignancies, including ovarian and breast cancer, which may be a mechanism by which tumour cells suppress T cell immunity and facilitate tumour progression. VTCN1 may thus be a useful biomarker for the early detection of ovarian cancer.

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UBA5 is a member of the E1-like ubiquitin-activating enzyme family. UBA5 activates ubiquitin-fold modifier 1, a ubiquitin-like post-translational modifier protein, via the formation of a high-energy thioester bond.This gene encodes a member of the E1-like ubiquitin-activating enzyme family. This protein activates ubiquitin-fold modifier 1, a ubiquitin-like post-translational modifier protein, via the formation of a high-energy thioester bond. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. A pseudogene located on chromosome 1 has also been identified.

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Acts as part of the IKK complex in the conventional pathway of NF-κ-B activation and phosphorylates inhibitors of NF-κ-B thus leading to the dissociation of the inhibitor/NF-κ-B complex and ultimately the degradation of the inhibitor. As part of the non-canonical pathway of NF-κ-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-κ-B RelB-p52 complexes. Also phosphorylates NCOA3. Phosphorylates 'Ser-10' of histone H3 at NF-κ-B-regulated promoters during inflammatory responses triggered by cytokines.