43325 Results for: "Neu5Ac[1Me,4789]alpha(2-3)Gal[246.1]-beta-MP"

Supplier: Proteintech

LRSAM1 also named as hTAL, RIFLE orTsg101 associated ligase is a 723 amino acid protein, which contains 6 LRR repeats, 1 Ring-type zinc finger and 1 SAM domain. LRSAM1 is localizes in cytoplasm and highly expressed in adult spinal cord motoneurons as well as in fetal spinal cord and muscle tissue. As a E3 ubiquitin protein ligase, LRSAM1 mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic and exocytic cargos, LRSAM1 gene mutation has an association with Charcot Maire Tooth disease 2P.

Supplier: Prosci

GALNT14 (EC 2.4.1.41) belongs to a large subfamily of glycosyltransferases residing in the Golgi apparatus. GALNT enzymes catalyze the first step in the O-glycosylation of mammalian proteins by transferring N-acetyl-D-galactosamine (GalNAc) to peptide substrates. GALNT14 (EC 2.4.1.41) belongs to a large subfamily of glycosyltransferases residing in the Golgi apparatus. GALNT enzymes catalyze the first step in the O-glycosylation of mammalian proteins by transferring N-acetyl-D-galactosamine (GalNAc) to peptide substrates.

Supplier: Prosci

Syntenin-1 is a molecule linking syndecan-mediated signaling to the cytoskeleton. Syntenin-1 is primarily localized to membrane-associated adherens junctions and focal adhesions but also found at the endoplasmic reticulum and nucleus. The syntenin protein contains tandemly repeated PDZ domains that bind the cytoplasmic, C-terminal domains of a variety of transmembrane proteins. Syntenin-1 may affect cytoskeletal-membrane organization, cell adhesion, protein trafficking, and the activation of transcription factors. It seems to function as an adapter protein, in adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Syntenin-1 seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA) and play a role in vesicular trafficking.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Prosci

Connexins, such as GJA9, are involved in the formation of gap junctions, intercellular conduits that directly connect the cytoplasms of contacting cells. Each gap junction channel is formed by docking of 2 hemichannels, each of which contains 6 connexin subunits.Connexins, such as GJA9, are involved in the formation of gap junctions, intercellular conduits that directly connect the cytoplasms of contacting cells. Each gap junction channel is formed by docking of 2 hemichannels, each of which contains 6 connexin subunits (Sohl et al., 2003 [PubMed 12881038]).

Supplier: Prosci

SARM Antibody: Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. SARM (SAM and ARM-containing protein), along with other molecules such as TIRP, TRIF, TIRAP, and MyD88, is thought to serve as an adaptor protein for the TLRs that allows for the activation of downstream kinases and NF-kappa B, and ultimately the expression of proteins involved in host defense. While SARM has not been conclusively shown to associate directly with TLRs, the presence of a Toll-interluekin-1 (TIR) domain in SARM is consistent with a role as a signaling molecule.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Prosci

Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V (D)J recombination.The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V (D)J recombination. 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.

Supplier: Bioss

WDR79 contains six WD (tryptophan-aspartate) repeat domains found in a number of proteins that function as adaptor molecules in signal transduction and cytoskeletal organization. The WD repeat is defined by four or more repeating units of a conserved core of approximately 40 amino acids ending with tryptophan-aspartic acid (WD). WD repeats may serve as sites of protein-protein interaction for adaptor proteins and facilitate multiprotein complex formation. The function of the WDR79 protein has not been characterized, however significant and consistent single nucleotide polymorphisms in the WDR79 gene have been found to be associated with ER negative breast cancer.

Supplier: Proteintech

TIPE2 (TNF-α-inducible protein 8-like 2, or TNFAIP8L2), a newly identified protein, is essential for maintaining immune homeostasis. TIPE2 shares considerable sequence homology with members of the tumor necrosis factor-α-inducible protein 8 (TNFAIP8) family, which are thought to regulate cellular and immune homeostasis. TIPE2 acts as a negative regulator of Toll-like receptor and T-cell receptor function and is preferentially expressed in lymphoid tissues. TIPE2 plays an essential role for a signal transduction pathway that links inflammatory immune response to specific conditions after cerebral ischemia

Supplier: Bioss

Caldesmon, Filamin 1, Nebulin and Villin are differentially expressed and regulated Actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in non-muscle tissues and cells. Filamin 1, which is ubiquitously expressed and exists as a homodimer, functions to crosslink Actin to filaments. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of absorptive cells.

Supplier: Proteintech

Interleukin-15 (IL-15) is a pleiotropic cytokine that plays an important role in both innate and adaptive immunity. IL-15 is mainly produced by activated monocytes, macrophages and dendritic cells, and is structurally similar to IL-2 . These two cytokines share the same IL-2/15Rβ and common γ-chain receptor subunits. In addition, IL-2 and IL-15 have their own private α-chain receptor subunit, IL-2Rα and IL-15Rα, respectively . The IL-15Rα chain is expressed by many cell types including monocytes, DCs, NK, T cells and fibroblasts. Several isoforms of IL-15Rα exist and are generated either by alternative splicing or by proteolytic cleavage .

Supplier: Bioss

Phosphatase enzymes catalyse hydrolysis of phosphoric acid esters of various alcohols, e.g. a hexose phosphate, to yield the alcohol and free inorganic phosphate. This may be a way of recycling phosphate in the cell, and the level of phosphate may be elevated under conditions of phosphate starvation (in algae for example). Acid phosphatases have pH optima below 7, whereas alkaline phosphatases are most active above pH 7. Commercial quantities of acid phosphatase are obtained from plant sources e.g. potato and wheat germ, whereas similar quantities of alkaline phosphatase are obtained from animal intestine and bacteria.

Supplier: Prosci

Vaspin (Visceral adipose tissue-derived serpin; Serpin A12), a serine protease inhibitor (serpin), is an insulin-sensitizing adipocytokine that has been isolated from both visceral and subcutaneous white adipose tissue. Based on recent findings, vaspin is suggested to regulate immune responses and inflammation and was found to be correlated with various metabolic parameters. Vaspin may represent a novel biomarker for obesity and impaired insulin sensitivity and might serve as a newtherapeutic target of metabolic syndrome.

Supplier: Prosci

SARM Antibody: Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. SARM (SAM and ARM-containing protein), along with other molecules such as TIRP, TRIF, TIRAP, and MyD88, is thought to serve as an adaptor protein for the TLRs that allows for the activation of downstream kinases and NF-kappa B, and ultimately the expression of proteins involved in host defense. While SARM has not been conclusively shown to associate directly with TLRs, the presence of a Toll-interleukin-1 (TIR) domain in SARM is consistent with a role as a signaling molecule.

Supplier: Proteintech

GFRA2, also named as GDNFRB, RETL2 and TRNR2, belongs to the GDNFR family. It is a receptor for neurturin. GFRA2 mediates the NRTN-induced autophosphorylation and activation of the RET receptor. It is a potent survival factor for central dopaminergic neurons, motor neurons, and several other populations of neurons in the central and peripheral nervous systems. The GDNF signal is mediated by a complex of the receptor tyrosine kinase RET and a glycosylphosphatidylinositol (GPI)-linked protein, GDNFRA. GFRA2 has three isoforms with MW 34-36 kDa, 39-41 kDa and 50-52 kDa. This antibody recognizes all the three isoforms.

Supplier: Proteintech

The effects of cAMP in most tissues and cell types are mainly modulated via protein kinase A, a heterotetrameric protein complex consisting of two regulatory and two catalytic subunits. The regulatory subunit of cAMP-dependent protein kinase (PRKAR2A) is one of the regulatory subunits and the gene is located on chromosome region 3p21.3-p21.2. The expression of PRKAR2A is tightly regulated during spermatogenesis, a significant increase in expression of this gene was also found in the human myometrium during pregnancy. This antibody got two bands about 45 kDa and 50-55 kDa in western blotting, and the 50-55kDa may be caused by phosphorylation.

Supplier: Prosci

LMX1A Antibody: The LIM homeobox transcription factor 1 (LMX1A) belongs to the LIM-homeodomain family. Members of this family are known to be important for pattern formation during development. LMX1A binds an A/T-rich sequence and functions in the nucleus as a transcriptional activator to the insulin gene promoter. In the developing embryo, LMX1A is expressed along the neuraxis and leads to the development of the roof plate of the vertebrae. While LMX1A is crucial for the differentiation of dopamine neurons, the related LMX1B appears to be important for both the development and the survival of these cells. It has been suggested that LMX1A might be a useful biomarker or risk factor in tumor aggressiveness.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Biogems

The N418 monoclonal antibody specifically reacts with the integrin αx chain of the mouse CD11c, which is expressed on dendritic cells, CD4-/CD8+ intestinal intraepithelial lymphocytes (IEL) and some activated T lymphocytes. Low levels of CD11c were detected on mouse splenic natural killer cells and on the monocyte/macrophage lineage cells.CD11c expression is upregulated on IEL and T lymphocytes after activation. It binds to CD54, fibrinogen and iC3b and influences the leukocyte adhesive interactions. The N418 antibody binds to CD11c on splenic dendritic cells of the mouse in the T-dependent areas. It also contributes to the binding of iC3b.

Supplier: Stemcell Technologies

Mouse monoclonal IgG2a antibody against human CD51 (integrin αV), unconjugated.

Supplier: Bioss

Phosphatase enzymes catalyse hydrolysis of phosphoric acid esters of various alcohols, e.g. a hexose phosphate, to yield the alcohol and free inorganic phosphate. This may be a way of recycling phosphate in the cell, and the level of phosphate may be elevated under conditions of phosphate starvation (in algae for example). Acid phosphatases have pH optima below 7, whereas alkaline phosphatases are most active above pH 7. Commercial quantities of acid phosphatase are obtained from plant sources e.g. potato and wheat germ, whereas similar quantities of alkaline phosphatase are obtained from animal intestine and bacteria.

Supplier: Bioss

Phosphatase enzymes catalyse hydrolysis of phosphoric acid esters of various alcohols, e.g. a hexose phosphate, to yield the alcohol and free inorganic phosphate. This may be a way of recycling phosphate in the cell, and the level of phosphate may be elevated under conditions of phosphate starvation (in algae for example). Acid phosphatases have pH optima below 7, whereas alkaline phosphatases are most active above pH 7. Commercial quantities of acid phosphatase are obtained from plant sources e.g. potato and wheat germ, whereas similar quantities of alkaline phosphatase are obtained from animal intestine and bacteria.

Supplier: Prosci

The protein encoded by this gene is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. This protein binds to the intracellular membrane-distal phosphatase domain of tyrosine phosphatase LAR, and appears to localize LAR to cell focal adhesions. This interaction may regulate the disassembly of focal adhesion and thus help orchestrate cell-matrix interactions. Alternatively spliced transcript variants encoding distinct isoforms have been described.

Supplier: Genetex

Inclusion of an appropriate isotype control is essential for the proper interpretation of experimental results. Because isotype control antibodies have no relevant specificity, they enable the researcher to distinguish non-specific "background" binding from antigen-specific antibody binding. Non-specific binding of primary antibodies may occur due to either binding of antibody to Fc receptors or non-specific interactions with cellular proteins, lipids, or carbohydrates. Additionally, autofluorescence or endogenous enzyme activity in target cells may give a false positive that could be misinterpreted as antibody binding. These factors vary by target cell type and the isotype of the primary antibody. Therefore, the primary antibody used should be matched to an isotype control of identical species and isotype (including both heavy and light chains).

Supplier: Proteintech

EEF1A1, also named as EEF1A, EF1A and LENG7, belongs to the GTP-binding elongation factor family. This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. It is a typical housekeeping gene product required for the maintenance of cell growth and/or survival. In addition, EEF1A1 protects the aminoester bond against hydrolysis until a correct match between the codon on mRNA and the anti-codon on tRNA can be achieved. This antibody is a rabbit polyclonal antibody raised against residues near the C terminus of human EEF1A1.

Supplier: Prosci

LAPTM4A is a protein that has four predicted transmembrane domains. The function of its gene has not yet been determined; however, studies in the mouse homolog suggest a role in the transport of small molecules across endosomal and lysosomal membranes.This gene encodes a protein that has four predicted transmembrane domains. The function of this gene has not yet been determined; however, studies in the mouse homolog suggest a role in the transport of small molecules across endosomal and lysosomal membranes.