May 24th, 2012
Ku70 is a 70 kDa protein that was shown to be involved in multiple cellular pathways, mainly involving DNA repair and recombination. Among these are the non-homologus end repairs of DNA double strand breaks. Ku70 was first identified as an autoantigen in the serum of patients with Scleroderma Ploymyosistosis Syndrome (1). Auto antibodies against Ku70 were also found in other autoimmune diseases such as Scleroderma and Systemic Lupus Erythromatosus. Ku proteins are multifunctional proteins that possess deubiquitylation activity and play a key role in DNA repair and transcriptional regulation (2). Substantial biochemical evidence also indicates that various proteins physically interact with the Ku complex. For example, Ku70/80 interacts with both the protein and RNA components of human telomerase, suggesting that the Ku complex is involved in telomere maintenance in eukaryotes (3), these complexes have been shown to inhibit apoptosis through an association with the proapoptotic factor Bax, Interactions between Ku70 and p18-cyclin E, and Ku70 and Bax, provide a balance between apoptosis and cell survival in response to genotoxic stress (4). Interaction of Ku70 proteins with mismatch repair (MMR) proteins has been detected in human cells by using antibodies against Ku70. Interactions were detected by anti-Ku70 antibody either by immunoprecipitation or by IHC studies. These data suggest a strong role for MMR protein involvement in the repair of double strand breaks in DNA via Ku70 (5). Novus Biologicals offers an extensive selection of Ku70 study tools, which include cell lysates and highly specific antibodies with reactivity against different species.
- PMID: 19448404
- PMID: 0755664
- PMID: 15824061
- PMID: 17325036
- PMID: 21075794
Tags: Autoimmunoe Disease, Bax, Bax antibody, Cyclin E, Cyclin E antibody, Double Strand Break Repair, Ku70, Ku70 antibody, Mismatch Repair, Scleroderma, Scleroderma Ploymyosistosis Syndrome, Systemic Lupus Erythromatosus
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Apoptosis, DNA Repair, Immunology | No Comments »
May 22nd, 2012
BrdU (5-bromo-2-deoxyuridine) is a thymidine analogue which is incorporated into the cells of DNA synthetic phase. Replicating cells undergo DNA synthesis in a highly regulated, S-phase of the cell cycle. The regulation of cell proliferation is central to tissue morphogenesis during the development of multicellular organisms. Furthermore, loss of control of cell proliferation underlies the pathology of diseases like cancer. As such there is great need to be able to investigate cell proliferation and quantitate the proportion of cells in each phase of the cell cycle (1). Since a cell’s decision to proliferate is made in the G1 phase immediately before initiating DNA synthesis and progressing through the rest of the cell cycle, detection of DNA synthesis at this stage allows for an unambiguous determination of the status of growth regulation in cell cultures. Anti-BrdU antibodies have been successfully employed to determine the cell proliferation in cultured tumor cells with high accuracy (2). Accurate determination of the S-phase fraction in proliferative cells has also been determined using anti-BrdU antibodies in various tissues by immunohistochemistry. (3). Analysis of cell kinetics using BrdU antibodies is advantageous in comparison to the conventional autoradiographic methods due to the regulatory issues with the radioactive materials. BrdU antibodies are a powerful tool to study cell proliferation more rapidly through cell based assays and are highly sensitive. Novus Biologicals offers highly sensitive anti-BrdU antibodies for your research needs with reactivity against different species.
- PMID: 2083223
- PMID: 1280304
- PMID: 21551319
Tags: BrdU, BrdU antibodies, cell cycle, DNA Synthesis, G1 phase, S-phase, Thymidine analog
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, DNA Repair, Tumor | No Comments »
May 21st, 2012
Increasing evidence shows that a variety of cancers arise from the transformation of normal stem cells into cancer stem cells (CSCs). CSCs are thought to sustain cancer progression, invasion, metastasis. Studies using Bmi1 antibodies have shown that the chemoresistance of CSCs are in part due to the activation of Bmi1 polycomb ring finger oncogene, previously known as B cell-specific Moloney murine leukemia virus integration site 1 (Bmi1), a stem cell factor, and a polycomb group family member of proteins, Bmi1 is reported to regulate the proliferation activity of normal, stem, and progenitor cells. Additional studies with Bmi1 antibodies have shown that Bmi1 also influences cell cycle, immortalization, and senescence (1). Increased levels of Bmi 1 have been detected by anti-Bmi1 antibodies in cervical carcinoma patient serum samples and cell lines by ELISA and Western blot (2). Numerous studies using anti Bmi1 antibodies demonstrate that Bmi1, is upregulated in a variety of cancers, and has a positive correlation with clinical grade/stage and poor prognosis of the disease (3). The exact mechanism of action by which Bmi1 controls the cellular events is not fully understood; hence Bmi1 is an attractive therapeutic target in management of several cancers. Novus Biologicals offers a wide array of products and tools to study the biochemical and molecular mechanisms of Bmi1, including antibodies, lysates and recombinant proteins for your research.
- PMID: 16963837
- PMID: 22132147
- PMID: 20805665
Tags: and senescence, Bmi1, Bmi1 antibody, Cancer Stem Cells, cell cycle, immortalization, Moloney murine leukemia virus
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Stem Cells | No Comments »
May 18th, 2012
A growing body of data and studies using actin antibodies supports a view of the actin cytoskeleton of smooth muscle cells as a dynamic structure that plays an integral role in regulating the development of mechanical tension and the material properties of smooth muscle tissues. The increase in the proportion of filamentous actin that occurs in response to the stimulation of smooth muscle cells and the essential role of stimulus-induced actin polymerization and cytoskeletal dynamics has been convincingly documented using actin antibodies in many smooth muscle tissues and cells using a wide variety of experimental approaches including Western blotting(1). Western blotting is a powerful technique using antibodies to characterize a multitude of cellular proteins. As an internal control to assure even protein loading and gel migration, the blots are commonly probed with antibodies for ubiquitous “housekeeping” gene products. It has recently been shown that cell confluence significantly affects the levels of housekeeping genes; alpha-tubulin and Glyceraldehyde-3-Phosphate Dehydrogenase levels were affected by cell densities. On the other hand the levels of beta-actin remained unchanged at a wide range of cell densities, implying actin as a more reliable loading control (2). Novus Biologicals offers a wide variety of actin recombinant proteins and antibodies with reactivity against various species.
- PMID: 18596210
- PMID: 20171969
Tags: Actin, actin antibody, alpha Tubulin, alpha Tubulin antibody, GAPDH, GAPDH antibody, Housekeeping gene, Loading control, Western blot
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Support Products | No Comments »
May 17th, 2012
Ghrelin is the only potent orexigenic peptide in circulation. It stimulates food intake and leads to metabolism regulation, positive energy balance, adipogenesis, and body weight gain. However, in studies using ghrelin antibodies, the physiological significance of ghrelin in the regulation of energy homeostasis is controversial, since loss of ghrelin function in rodents does not necessarily lead to anorexia and weight loss (1). Research using ghrelin antibodies shows that ghrelin is a brain-gut circuit peptide with an important role in the physiological regulation of appetite, response to hunger and starvation, metabolic and endocrine functions as energy expenditure, gastric motility and acid secretion, insulin secretion and glucose homeostasis, as well as in the potential connection to the central nervous system (2). Besides its functions in regulating energy homeostasis, ghrelin has pronounced cardioprotective effects and was shown to improve cardiac performance in chronic heart failure (CHF). Studies using ghrelin antibodies suggest that the multifunctional nature of ghrelin makes it an interesting pharmacological target for various diseases. Additional ghrelin antibody-based studies show that inhibition of ghrelin could be a promising approach in obesity-related disorders, while an enhancement of the ghrelin response is considered beneficial in several pathologic conditions marked by malnutrition, wasting and cachexia, including CHF, cancer, chronic pulmonary disease or chronic infections (3). Novus Biologicals offers an extensive selection of Ghrelin study tools for your research needs, including many highly specific monoclonal antibodies, control lysates and proteins, as well as RNAi with reactivity against different species.
- PMID: 22249814
- PMID: 22041110
- PMID: 22074572
Tags: Adipogenesis, Anorexia nervosa, Chronic Heart Failure, Energy regulation, Ghrelin, Ghrelin antibody, Glucose metabolism
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Diabetes, Heart Disease, Lipid & Metabolism | No Comments »
May 15th, 2012
Disulfide bond formation is a pivotal step in the maturation and release of secretory proteins that are controlled by specific endoplasmic reticulum (ER) resident enzymes. An important element in this process is ERO (ER oxidoreduction), a glycosylated flavoenzyme tightly associated with oxidative protein folding that lacks the known ER retention motifs. ER resident protein 44kDa (ERp44) is an ER resident protein that mediates ERO1 localization in ER and thus prevents the secretion of unassembled cargo proteins with unpaired cysteine (1). The production of secretory proteins at the ER depends on a ready supply of energy and metabolites as well as close monitoring of the biochemical conditions that favor oxidative protein folding. ER oxidoreductases and chaperones fold nascent proteins into their export-competent three-dimensional structure. Interference with these protein folding enzymes leads to the accumulation of unfolded proteins within the ER lumen, causing an acute organellar stress that triggers the unfolded protein response (2). Ero1 alpha antibody studies have revealed expression is almost exclusively found on the mitochondria-associated membrane (MAM). The localization of ERO1-alpha on the MAM is dependent on oxidizing conditions within the ER. Chemical reduction of the ER environment, but not ER stress in general leads to release of ERO1 alpha from the MAM. In addition, the correct localization of ERO1alpha to the MAM also requires normoxic but not hypoxic conditions (3). ERO1 oxidizes protein disulfide isomerase (PDI), which, in turn, introduces disulfides into ER client proteins. To maintain an oxidized state, ERO1 couples disulfide transfer to PDI with reduction of molecular oxygen, forming hydrogen peroxide thus, ERO1 activity constitutes a potential source of ER-derived oxidative stress (4). Novus Biologicals offers a wide variety of tools to investigate the role of ERO1L in ER stress in the form of antibodies, recombinant protein, Western blot lysates and RNAi.
Tags: Endoplasmic Reticulum, ERO1B, ERO1B antibody, ERO1L, ERO1L antibody, Oxidative Stress, PDI, PDI antibody, Protein Folding
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers | No Comments »
May 14th, 2012
Epigenetic alterations have come to prominence in biomedical research. In particular, hypermethylation of CpG islands located in the promoter regions of tumor-suppressor genes is now firmly established as an important mechanism for gene inactivation in cancer. Polycomb group (PcG) proteins are epigenetic chromatin modifiers involved in gene silencing, cancer development and the maintenance of adult and embryonic stem cells. One of the most remarkable achievements in the field has also been the identification of the methyl-CpG-binding domain family of proteins, which provide mechanistic links between specific patterns of DNA methylation and histone modifications. Interest in non-allelic histone variants has been renewed, in part because of recent work on H3 (and other) histone variants. However, only in mammals do three non-centromeric H3 variants (H3.1, H3.2, and H3.3) exist (1). Epigenetic changes underlie not only normal, but also pathological development. Bmi1 is recognized as a member of the PcG family of proteins (2). The PcG proteins function within distinct multisubunit complexes and epigenetically regulate gene expression by altering chromatin states at specific promoters. In concordance with its role in stem cells, Bmi-1 has been proposed to maintain cancer stem cell populations (3).
Pluripotent embryonic stem cells (ESCs) have the potential to produce every type of cell in the human body. Pluripotency is a unique epigenetic state, in that ESCs can self-renew, while retaining the potential for multilineage differentiation. OCT4 is highly expressed in pluripotent cells and becomes silenced upon differentiation. Interestingly, the precise expression level of OCT4 determines the fate of embryonic stem cells (4). Nevertheless, further investigations are required to fully elucidate the underlying molecular mechanisms responsible for the maintenance and initiation of pluripotency. Novus Biologicals offers an extensive collection of reagents to investigate epigenetic alterations, including Histone H3.2 K23me2 antibody (NB21-1162), Bmi1 antibody (NBP1-96140) and OCT4 antibody (NB100-2379) and our entire EpiPlus™ line.
- PMID: 16212490
- PMID: 1922340
- PMID: 12714970, PMID: 14574365
- PMID: 19480567
Tags: Bmi1, Bmi1 antibody, Chromatin Modifiers, DNA Methylation, Embryonic Stem Cell Marker, Embryonic Stem Cells, histone modification, Histone Modifications, Histones study, OCT4, Oct4 antibody, pluripotent, Pluripotent Embryonic Stem Cells
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Epigenetics, Stem Cells, Tumor | No Comments »
May 11th, 2012
Discovery of histone variants using highly specific antibodies has led to the emerging notion that alterations in histone modifications and further changes in chromatin structure are induced by exchange of histone variants. Covalent histone modifications and the incorporation of histone variants bring about changes in chromatin structure that in turn alter the gene expression. These modifications can be detected using highly specific antibodies, such as the Epi-Plus™ products from Novus.
Interest in non-allelic histone variants has been renewed, in part because of recent studies of H3 (and other) histone variants. However only in mammals do three non-centromeric histone H3 variants (H3.1, H3.2, and H3.3) exist. Studies have shown that the variants of histone H3 differ primarily in their chromatin deposition patterns and post- translational modifications (1). Additional studies using H3 antibodies have shown that the interplay among deposition of H3 variants likely participates in the functional organization of chromatin. Available literature suggests that dynamic replacement of histone variants plays an important role in genome remodeling during early development and that histone H3 proteins are highly conserved across all eukaryotes and are dynamically modified by post-translational modifications (2). Extreme conservation of known acetylation and methylation sites of lysines and arginines predicts that these post-translational modifications exist across the eukaryotes with canonical chromatin structures (3).
In a recent study using Histone H3 antibodies, methylated histone (H3) expressions in unexplained recurrent spontaneous abortion (URSA) and normal early pregnancy was found to be significantly lower (P < 0.0001) in URSA tissues than in controls as determined by immunohistochemistry and western blotting using Histone H3 antibodies (4), suggesting that methylation may cause URSA indicating the need for further work to explore the role of methylation in various disorders including cancer. Novus Biologicals offers a wide variety of study tools including antibodies, lysates, proteins and peptides for your research needs.
- PMID: 16212490
- PMID: 21998593
- PMID: 21910587
- PMID: 21606120
Tags: Chromatin Modifiers, EpiPlus, Histone H3, Histone H3 antibody
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Epigenetics | No Comments »
May 10th, 2012
Glial fibrillary acidic protein (GFAP) is the main intermediate filament protein in mature astrocytes, but also an important component of the cytoskeleton in astrocytes during development. Recent developments using GFAP antibodies in astrocyte biology, and the discovery of novel intermediate filament functions, have enticed interest in the function of GFAP. The structural role of GFAP in astrocytes has been widely accepted for a long time, but over the years, studies using GFAP antibodies have shown GFAP to be involved in astrocyte functions, during human brain development, aging and disease (1). Immunohistochemical analysis using GFAP antibodies revealed up regulation of GFAP protein in older mice compared to their young counter parts in neurodegenerative disorders suggesting astrogliosis due to initial neurodegeneration (2). As a member of the cytoskeletal protein family, GFAP is thought to be important in modulating astrocyte motility and shape by providing structural stability to astrocytic processes. In the central nervous system (CNS) of vertebrates, astrocytes become reactive and respond in a typical manner, termed astrogliosis. Astrogliosis is characterized by rapid synthesis of GFAP and is demonstrated by an increase in protein content or by immunostaining with GFAP antibody. Additionally, the major application of GFAP antisera is also used routinely in astrocyte identification in the CNS. Studies using GFAP antibodies showing that mice lacking GFAP are hypersensitive to cervical spinal injury caused by sudden acceleration of the head have provided more direct evidence for a structural role of GFAP (3). While the structure and function of GFAP has become more accepted, use of GFAP antibodies continue to be valuable in studying CNS injury, disease, and development. Novus Biologicals offers a wide range of products and tools for research studies, including antibodies, lysates and recombinant proteins.
- PMID: 21219963
- PMID: 21960009
- PMID: 9665584
Tags: Astrogliosis, Central Nervous System, Cytoskeletan, GFAP, GFAP antibody
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Neurodegeneration, Neuroscience | No Comments »
May 8th, 2012
The transcription factor beta protein 1 (BP1) is a member of the homeobox gene family and the distal-less subfamily. Expression of BP1 is highly tissue-specific and developmentally restricted. Among different human tissues, BP1 is found to be highly expressed in placenta, kidney and at lower levels in fetal liver (1). Such restricted pattern of expression is compatible with a specific gene function in development and/or differentiation. Transient transfection studies demonstrate that BP1 protein appears to act as a repressor of the human adult beta globin gene, through two silencers upstream of the beta globin gene (2,3). BP1 binding site sequence upstream of beta globin gene in Asian populations has been investigated for the polymorphism in the BP1 binding site upstream of beta globin gene, so as to provide the basis for exploration of relation between polymorphisms in the BP1 binding site and beta globin expression (4,5). Beta globin gene cluster polymorphisms are known to be strongly associated with severity of beta-thalassemia in the Asian populations (6). Recent studies also indicate that BP1 genes are dysregulated in various cancers and some new studies point to an important role for BP1, an isoform of DLX4 homeobox gene, in breast carcinogenesis and progression (7). Current research directed towards the elucidation of the role of BP1 in breast tumorogenesis holds a great promise in establishing BP1 as a novel target for drug therapy. Novus Biologicals offers an extensive selection of BP1 study tools, for Western blots, ELISA, IHC and RNAi including highly specific antibodies with reactivity against different species.
- PMID: 11909945
- PMID: 10087993
- PMID: 15308321
- PMID: 22040981
- PMID: 15551156
- PMID: 17894837
- PMID: 20877436
Tags: beta-thalassemia, BP1, BP1 antibody, Breast Cancer, Breast Cancer Antibodies, DLX4, DLX4 antibody
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Transcription Regulation, Tumor | No Comments »
