263625 Results for: "CAFRAMO+LTD+CA&pageNo=10"

Supplier: Prosci

Pax genes contain paired domains with strong homology to genes in Drosophila, which are involved in programming early development. Lesions in the Pax-6 gene account for most cases of aniridia, a congenital malformation of the eye, chiefly characterized by iris hypoplasia, which can cause blindness. Pax-6 is involved in other anterior segment malformations besides aniridia, such as Peters anomaly, a major error in the embryonic development of the eye with corneal clouding with variable iridolenticulocorneal adhesions. The Pax-6 gene encodes a transcriptional regulator that recognizes target genes through its paired-type DNA-binding domain. The paired domain is composed of two distinct DNA-binding subdomains, the amino-terminal subdomain and the carboxy-terminal subdomain, which bind respective consensus DNA sequences. The human Pax-6 gene produces two alternatively spliced isoforms that have the distinct structure of the paired domain.

Supplier: Prosci

At least five CD1 genes (CD1a, b, c, d, and e) are identified. CD1 proteins have been demonstrated to restrict Tcell response to non-peptide lipid and glycolipid antigens and play a role in non-classical antigen presentation. CD1a is a non-polymorphic MHC Class 1 related cell surface glycoprotein, expressed in association with Beta-2 microglobulin. CD1a antibody labels Langerhans cell histiocytosis (Histiocytosis X), extranodal histiocytic sarcoma, a subset of T-lymphoblastic lymphoma/leukemia, and interdigitating dendritic cell sarcoma of the lymph node. When combined with antibody against TTF-1 and CD5, CD1a antibody is useful in distinguishing between pulmonary and thymic neoplasms since it is consistently expressed in thymic lymphocytes in both typical and atypical thymomas, but only focally in 1/6 of thymic carcinomas and not in lymphocytes in pulmonary neoplasms. CD1a antibody is reported to be a new marker for perivascular epithelial cell tumor (PEComa).

Supplier: Prosci

This antibody reacts with both SUMO2 and SUMO3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursors that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets for a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO1/2/3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO1 utilizes Ubc9 for conjugation to several targets, which include MDM2, p53, PML and RanGap1. SUMO2/3 contribute to a greater percentage of protein modification than does SUMO1 and they can form polymeric chains. In addition, SUMO3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Rockland Immunochemical

Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor. Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth, vascular permeability, cell migration, and endothelial cell proliferation and growth, it may play a role in stimulating vasolidation via nitric oxide-dependent pathways and in inhibition of apoptosis. VEGF binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Alternative splicing of the mRNA for VEGF-A results in several isoforms of the protein being produced. Rat and bovine VEGF are one amino acid shorter than the human factor, and the bovine and human sequences show a homology of 95 percent. In contrast to other factors mitogenic for endothelial cells such as FGF-1, FGF-2 and PDGF, VEGF is synthesized as a precursor containing a typical hydrophobic secretory signal sequence of 26 amino acids. Glycosylation is not required for efficient secretion of VEGF. VEGF121 is acidic, freely secreted, and widely expressed. This isoform is produced by alternative promoter usage and alternative initiation. It starts at an alternative upstream CUG codon and is post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus, the endoplasmic reticulum and the Golgi or the extracellular matrix. Recombinant Human VEGF-121 produced in E.coli is a double, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 28423 Daltons.

Supplier: Invitrogen

Thermo Scientific Heavy and Light Amino Acids are used to specifically analyze protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC) quantification kits. Store at 2 - 8˚C.

Supplier: Heidolph NA, LLC

The Carousel 6 Plus™ Reaction Station simultaneously heats, stirs, and refluxes multiple samples under an inert atmosphere

Supplier: Bio-Rad

Aminex® Carbohydrate Analysis HPLC Columns separate compounds using a combination of size exclusion and ligand exchange mechanisms.

Supplier: Prosci

EED is a member of the Polycomb-group (PcG) family. PcG family members form multimeric protein complexes, which are involved in maintaining the transcriptional repressive state of genes over successive cell generations. This protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin beta7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins. This protein mediates repression of gene activity through histone deacetylation, and may act as a specific regulator of integrin function.This gene encodes a member of the Polycomb-group (PcG) family. PcG family members form multimeric protein complexes, which are involved in maintaining the transcriptional repressive state of genes over successive cell generations. This protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin beta7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins. This protein mediates repression of gene activity through histone deacetylation, and may act as a specific regulator of integrin function. Two transcript variants encoding distinct isoforms have been identified for this gene.

Supplier: Prosci

STAT1 is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. This protein can be activated by various ligands including interferon-alpha, interferon-gamma, EGF, PDGF and IL6. This protein mediates the expression of a variety of genes, which is thought to be important for cell viability in response to different cell stimuli and pathogens.The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. This protein can be activated by various ligands including interferon-alpha, interferon-gamma, EGF, PDGF and IL6. This protein mediates the expression of a variety of genes, which is thought to be important for cell viability in response to different cell stimuli and pathogens. Two alternatively spliced transcript variants encoding distinct isoforms have been described.

Supplier: G-Biosciences

DETERGENT ASSAY CMC-535

Supplier: Molecular Devices

The SpectraMax® iD5 Multi-Mode Microplate Reader is the complete laboratory solution to help you increase your research capabilities and comes with built-in absorbance, fluorescence, luminescence, time-resolved fluorescence (TRF), and tunable fluorescence polarization (FP) read modes

Supplier: Prosci

Thyroglobulin is a 660kDa dimeric pre-protein with mutiple glycosylation sites, detected at ~300kDa in western blot. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for thyroglobulin antibody even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently thyroglobulin antibody negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Thyroglobulin antibody, combined with calcitonin antibody, can identify medullary carcinomas of the thyroid. Furthermore, thyroglobulin antibody, combined with TTF1 antibody, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Supplier: Prosci

This antibody recognizes proteins of 80-200kDa, identified as different members of the CEA (Carcinoembryonic Antigen) family. CEA is synthesized during development in the fetal gut and is re-expressed in increased amounts in intestinal carcinomas and several other tumors. This antibody does not react with nonspecific cross-reacting antigen (NCA) and with human polymorphonuclear leucocytes. The antibody shows no reaction with a variety of normal tissues and is suitable for staining of formalin/paraffin tissues. CEA is not found in benign glands, stroma, or malignant prostatic cells. antibody to CEA is useful in detecting early foci of gastric carcinoma and in distinguishing pulmonary adenocarcinomas (60-70% are CEA+) from pleural mesotheliomas (rarely or weakly CEA+). CEA antibody positivity is seen in adenocarcinomas from the lung, colon, stomach, esophagus, pancreas, gallbadder, urachus, salivary gland, ovary, and endocervix.

Supplier: Prosci

This mAb recognizes granulocyte-colony stimulating factor (G-CSF) in the cytoplasm of mature granulocytes. It shows no reactivity with any other cell types. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. It reacts with early precursor and mature forms of myeloid cells. It is useful for the detection of myeloid leukemias and granulocytic sarcomas. It can be used as a marker of granulocytes in normal tissues or inflammatory processes.G-CSF is a pleiotropic cytokine that influences differentiation, proliferation and activation of the neutrophilic granulocyte lineage. The human G-CSF cDNA encodes a 207 amino acid precursor containing a 29 amino acid signal peptide that is proteolytically cleaved to form a 178 amino acid residue mature protein. Two G-CSFs, which are identical except for a three amino acid deletion in the amino-terminus of one form of the protein have been isolated from human cells. Murine and human G-CSF s share 73% sequence identity at the amino acid level.

Supplier: Prosci

This mAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins. IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin s lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: Prosci

This antibody recognizes an intra-cytoplasmic marker antigen which shows a very high degree of specificity for plasma cells. This marker protein is present in normal as well as neoplastic plasma cells. Plasma cells, which are large lymphocytes derived from an antigen-specific B cell, secrete antibodies and are responsible for humoral immunity. Plasma cells differentiate from B cells upon stimulation by CD4+ lymphocytes. The B cell acts as an antigen-presenting cell (APC), consuming an offending pathogen, which is taken up by the B cell by phagocytosis and broken down within proteosomes. Plasma cells contain basophilic cytoplasm; their nucleus contains heterochromatin organized in a characteristic cartwheel arrangement. This marker antibody superbly recognizes normal and neoplastic plasma cells in routine formalin/paraffin tissue sections. It is of potential value in identifying myeloma or plasmacytoma in bone marrow or other tissues. It also helps differentiate lympho-plasmacytoid lymphoma from lymphocytic and follicular lymphoma. Note that this plasma cell marker antibody is not suitable for staining frozen tissues.

Supplier: Prosci

A disulphide-linked heterodimer, consisting of mb-1 (or CD79a) and B29 (or CD79b) polypeptides, is non-covalently associated with membrane-bound immunoglobulins on B cells. This complex of mb-1 and B29 polypeptides and immunoglobulin constitute the B cell Ag receptor. CD79a first appears at pre B cell stage, early in maturation, and persists until the plasma cell stage where it is found as an intracellular component. CD79a is found in the majority of acute leukemias of precursor B cell type, in B cell lines, B cell lymphomas, and in some myelomas. It is not present in myeloid or T cell lines. Anti-CD79a is generally used to complement anti-CD20 especially for mature B-cell lymphomas after treatment with RituximAb (anti-CD20). This antibody will stain many of the same lymphomas as anti-CD20, but also is more likely to stain B-lymphoblastic lymphoma/leukemia than is anti-CD20. Anti-CD79a also stains more cases of plasma cell myeloma and occasionally some types of endothelial cells as well.

Supplier: Prosci

Pax genes contain paired domains with strong homology to genes in Drosophila, which are involved in programming early development. Lesions in the Pax-6 gene account for most cases of aniridia, a congenital malformation of the eye, chiefly characterized by iris hypoplasia, which can cause blindness. Pax-6 is involved in other anterior segment malformations besides aniridia, such as Peters anomaly, a major error in the embryonic development of the eye with corneal clouding with variable iridolenticulocorneal adhesions. The Pax-6 gene encodes a transcriptional regulator that recognizes target genes through its paired-type DNA-binding domain. The paired domain is composed of two distinct DNA-binding subdomains, the amino-terminal subdomain and the carboxy-terminal subdomain, which bind respective consensus DNA sequences. The human Pax-6 gene produces two alternatively spliced isoforms that have the distinct structure of the paired domain.

Supplier: Zymo Research

ZymoScript RT PreMix is an optimized reverse transcription kit containing all the necessary components for quick and efficient cDNA synthesis.

Supplier: Prosci

Oncostatin M is a member of the IL6 family of cytokines. Functional receptors for IL6 family cytokines are multisubunit complexes involving members of the hematopoietin receptor superfamily. Many IL6 cytokines utilize gp130 as a common receptor subunit. OSM binds to the gp130 receptor subunit and, in association with the leukemia inhibitory factor receptor, induces a proliferative response in permissive cells. OSMR is an alternative subunit (for an OSM receptor complex (a heterodimer of gp130 and OSMR) that is activated by OSM but not by LIF.Oncostatin M is a member of the IL6 family of cytokines. Functional receptors for IL6 family cytokines are multisubunit complexes involving members of the hematopoietin receptor superfamily. Many IL6 cytokines utilize gp130 as a common receptor subunit. OSM binds to the gp130 receptor subunit and, in association with the leukemia inhibitory factor receptor, induces a proliferative response in permissive cells. OSMR is an alternative subunit (for an OSM receptor complex (a heterodimer of gp130 and OSMR) that is activated by OSM but not by LIF. 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: LGC Standards

TRC Acid Blue 113 (Technical Grade)

Supplier: COSPHERIC MS

FLUORESCENT PE RED MICROSPHERE 100MG

Supplier: Prosci

Expression of the c-myc gene, which produces an oncogenic transcription factor, is tightly regulated in normal cells but is frequently deregulated in human cancers. The MXI1 gene encodes a transcriptional repressor protein thought to negatively regulate MYC function, and is therefore a potential tumor suppressor. This protein inhibits the transcriptional activity of MYC by competing for MAX, another basic helix-loop-helix protein that binds to MYC and is required for its function. Defects in MXI1 are frequently found in patients with prostate tumors.Expression of the c-myc gene, which produces an oncogenic transcription factor, is tightly regulated in normal cells but is frequently deregulated in human cancers. The protein encoded by this gene is a transcriptional repressor thought to negatively regulate MYC function, and is therefore a potential tumor suppressor. This protein inhibits the transcriptional activity of MYC by competing for MAX, another basic helix-loop-helix protein that binds to MYC and is required for its function. Defects in this gene are frequently found in patients with prostate tumors. Three alternatively spliced transcripts encoding different isoforms have been described. Additional alternatively spliced transcripts may exist but the products of these transcripts have not been verified experimentally.

Supplier: Prosci

STAT1 is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. This protein can be activated by various ligands including interferon-alpha, interferon-gamma, EGF, PDGF and IL6. This protein mediates the expression of a variety of genes, which is thought to be important for cell viability in response to different cell stimuli and pathogens.The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. This protein can be activated by various ligands including interferon-alpha, interferon-gamma, EGF, PDGF and IL6. This protein mediates the expression of a variety of genes, which is thought to be important for cell viability in response to different cell stimuli and pathogens. Two alternatively spliced transcript variants encoding distinct isoforms have been described.

Supplier: Prosci

A disulphide-linked heterodimer, consisting of mb-1 (or CD79a) and B29 (or CD79b) polypeptides, is non-covalently associated with membrane-bound immunoglobulins on B cells. This complex of mb-1 and B29 polypeptides and immunoglobulin constitute the B-cell Ag receptor. CD79a first appears at pre B-cell stage, early in maturation, and persists until the plasma cell stage where it is found as an intracellular component. It is found in the majority of acute leukemias of B-cell precursors, lines and lymphomas, and in some myelomas. It is not present in myeloid or Tcell lines. CD79a antibody is generally used to complement CD20 mAb, especially for mature B-cell lymphomas after treatment with Rituximab (anti-CD20). This CD79a antibody will stain many of the same lymphomas as CD20 mAb, but also is more likely to stain B-lymphoblastic lymphoma/leukemia than is CD20 mAb. CD79a antibody also stains more cases of plasma cell myeloma and occasionally some types of endothelial cells as well.

Supplier: Prosci

This antibody recognizes a 60kDa protein, identified as the heat shock protein 60. The antibody's epitope is localized between amino acids 383-447 of human HSP60. A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (hsp’s), more appropriately called as stress response proteins (srp’s). HSP60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial HSP60, but also against its mammalian homolog. Clone LK1 antibody, unlike LK2 antibody, recognizes only the mammalian (not bacterial) HSP60 and is useful in distinguishing HSP60 from mammals and bacteria.

Supplier: Prosci

The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The family member CHRNA7 is located on chromosome 15 in a region associated with several neuropsychiatric disorders. CHRFAM7A is is a hybrid between CHRNA7 and FAM7A. The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The family member CHRNA7, which is located on chromosome 15 in a region associated with several neuropsychiatric disorders, is partially duplicated and forms a hybrid with a novel gene from the family with sequence similarity 7 (FAM7A). Alternative splicing has been observed, and two variants exist, for this hybrid gene. The N-terminally truncated products predicted by the largest open reading frames for each variant would lack the majority of the neurotransmitter-gated ion-channel ligand binding domain but retain the transmembrane region that forms the ion channel. Although current evidence supports transcription of this hybrid gene, translation of the nicotinic acetylcholine receptor-like protein-encoding open reading frames has not been confirmed.

Supplier: Proteintech

Cadherins are a family of transmembrane glycoproteins that mediate calcium-dependent cell-cell adhesion and play an important role in the maintenance of normal tissue architecture. E-cadherin (epithelial cadherin), also known as CDH1 (cadherin 1) or CAM 120/80, is a classical member of the cadherin superfamily which also include N-, P-, R-, and B-cadherins. It has been regarded as a marker for spermatogonial stem cells in mice. E-cadherin is expressed on the cell surface in most epithelial tissues. The extracellular region of E-cadherin establishes calcium-dependent homophilic trans binding, providing specific interaction with adjacent cells, while the cytoplasmic domain is connected to the actin cytoskeleton through the interaction with p120-, α-, β-, and γ-catenin (plakoglobin). E-cadherin is important in the maintenance of the epithelial integrity, and is involved in mechanisms regulating proliferation, differentiation, and survival of epithelial cell. E-cadherin may also play a role in tumorigenesis. It is considered to be an invasion suppressor protein and its loss is an indicator of high tumor aggressiveness. E-cadherin is sensitive to trypsin digestion in the absence of Ca2+. This polyclonal antibody recognizes 120-kDa intact E-cadherin and its 80-kDa trypsin-cleaved fragment.

Supplier: Adipogen

Profilin (PFN1) is a ubiquitous small (12-15kDa) phosphoinositide and poly-L-proline binding protein that plays a role in signal transduction pathways and actin filament dynamics. There are two mammalian profilins with similar biochemical properties. Whereas profilin I appears to be highly expressed in most tissues except for skeletal muscle, profilin II is predominantly expressed in brain and at lower levels also in skeletal muscle, uterus and kidney. Profilin is a mainly cytosolic protein with higher concentrations in dynamic membrane areas like the leading edge and ruffling membranes. Profilin binding to PIP2 interferes with PIP2 hydrolysis by soluble phospholipase C-gamma, an inhibition that can be overcome by tyrosine phosphorylation of PLC-gamma. Besides actin monomer sequestration and stimulation of actin nucleotide exchange, profilin can also promote cellular actin filament growth. Profilin is involved in the actin dependent intracellular motility of cytopathogenic bacteria, the regulation of cell adhesion and possibly also in linking the actin cytoskeleton and endocytosis. Profilin has been found to associate with defined complexes containing proteins such as Arp2/3 or the Rho/Rac pathways constituents ROCK-II and HEM2/NAP1. Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18).

Supplier: Prosci

TEF (thyrotroph embryonic factor) is a member of the PAR bZip (proline and acidic amino acid-rich basic leucine zipper) transcription factor family. It accumulates with robust circadian rhythms in tissues with high amplitudes of clock gene expression.Thyrotroph embryonic factor (TEF), a transcription factor, is a member of the PAR (proline and acidic amino acid-rich) subfamily of basic region/leucine zipper (bZIP) transcription factors. It is expressed in a broad range of cells and tissues in adult animals, however, during embryonic development, TEF expression appears to be restricted to the developing anterior pituitary gland, coincident with the appearance of thyroid-stimulating hormone, beta (TSHB). Indeed, TEF can bind to, and transactivate the TSHB promoter. It shows homology (in the functional domains) with other members of the PAR-bZIP subfamily of transcription factors, which include albumin D box-binding protein (DBP), human hepatic leukemia factor (HLF) and chicken vitellogenin gene-binding protein (VBP); VBP is considered the chicken homologue of TEF. Different members of the subfamily can readily form heterodimers, and share DNA-binding, and transcriptional regulatory properties.