Archive for the ‘Angiogenesis’ Category
Tuesday, April 24th, 2012
S100A12 (Calgranulin C) belongs to the S100 family of calcium-binding proteins. The 20 members of this group share EF-hand domains which are involved in binding of calcium. S100A12 is expressed by granulocytes, whereas its expression by monocytes remains controversial (1). S100A12 is secreted by activated granulocytes (2). S100A12 is a ligand for the receptor for advanced glycation end products (RAGE) expressed on macrophages, lymphocytes and endothelium. RAGE mediates an up-regulation of the connective tissue growth factor IGFBP-rP2 (insulin-like growth factor binding protein-related protein 2), which is a potent inducer of angiogenesis (3). Additionally, RAGE has been shown to increase adhesion of granulocytes to stimulated endothelial cells (4). S100A12 serum levels might serve as a marker for local disease activity in different forms of arthritis as well. Patients with active arthritis revealed significantly higher S100A12 levels than healthy controls. The high local expression of S100A12 at the site of inflammation seems to be responsible for the correlating levels that are detected in serum (5). In different mouse models of inflammation including arthritis, blocking this interaction with soluble RAGE (sRAGE) and anti-S100A12 antibodies revealed clear anti-inflammatory effects (6). Further studies on the functional role of S100A12 in human arthritis have to prove the usefulness of new biological therapies that focus on pro-inflammatory activities of human S100A12. The expression of S100A12 in human arthritis provokes the question whether S100A12 protein and its interaction with RAGE might be a target for novel therapies. Novus Biologicals offers an extensive selection of S100A12 study tools, including S110A12 recombinant protein, cell lysate and highly specific antibodies with reactivity against different species.
- PMID: 10399917, 10973813
- PMID: 10726775
- PMID: 11316739
- PMID: 11854121
- PMID: 14644132
- PMID: 11581294
Tags: Arthritis, RAGE, RAGE antibody, S100A12, S100A12 antibody
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Immunology, Inflammation, Rheumatoid Arthritis | No Comments »
Friday, February 24th, 2012
Platelet Endothelial Cell Adhesion Molecule 1 (PECAM1) is a single-pass membrane receptor also known as CD31 (cluster of differentiation 31.) CD31 is expressed at high levels at endothelial cell junctions, and therefore the CD31 antibody is widely used as an endothelial marker, one use being to measure the progression of angiogenesis following recurrence of tumors. Other CD31 antibody studies have suggested a possible use as a myeloid progenitor cell marker, and in the identification of different granular sarcoma subsets.
Novus Biologicals is constantly refining our CD31 antibody catalog to ensure customers have a wide range of reagents to choose from, covering as many assay applications as possible. In addition to standard monoclonals and polyclonals, our catalog also contains a variety of CD31 antibody reagents conjugated to various chromogenic and fluorochromic dyes. Each monoclonal product has a clone identifier in brackets. This identifies which cloned cell line the CD31 antibody was derived from (which may have been established for several years) and is an important factor as different clones can give different results, affecting continuity of research.
A perfect example of this is the CD31 antibody clone TLD-3A12, developed by K.C Williams, et al. in 1996 for rat CNS studies. Novus offers the TLD-3A12 antibody in unconjugated (NB100-64796), Biotin (NB100-63701) FITC (NB100-63703) and R-Phycoerythrin (NB100-63704) formats. However, studies have shown this clone partially blocks the proliferative response of antigen-specific CD4+ T cells when exposed to the antigen and cells expressing it, so for functional studies an alternative is recommended.
Please contact our technical support department (technical@novusbio.com) with any inquiries or for help selecting the best CD31/PECAM1 antibody for your experiment.
Tags: antibody conjugation, CD31, CD31/PECAM1, CD31/PECAM1 antibody, Conjugated antibody, Monoclonal antibody, PECAM1, Polyclonal antbody
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer | No Comments »
Thursday, February 16th, 2012
The matrix metalloproteinases are zinc-dependent protease enzymes which interact with a range of ECM (extracellular matrix) proteins, and are activated by proteolytic cleavage. We at Novus Biologicals offer a wide range of top quality MMP reagents, including MMP3, MMP7, MMP9, MMP13 and MMP2 specific antibodies.
All the above proteins are known to play important roles in embryonic development, wound healing, angiogenesis, carcinogenesis, tumour invasion and apoptosis. Overexpression of MMP2 and MMP9 is associated with tumour migration, metastasis and aggressive, invasive cancers such as chondrosarcomas, malignant astrocytomas, melanomas and breast cancer. It is thought this occurs through degradation of the ECM proteins, primarily Collagen IV and Laminin 5, allowing migration of metastatic cells through the basement membrane, with enhanced tumour growth.
The heat shock protein HSP90 is uploaded at times of cellular stress, with increasing evidence to show that it acts as a molecular chaperone. A recent study by D. Stellas et al. [PMID: 20602761] suggested HSP90 could be a target for antibody therapy. The team used various monoclonal antibodies (mAbs) to probe the interaction of HSP90 isoforms with MMP2 and MMP9. They also examined the role of a new HSP90 mAb, called 4C5, in inhibiting metastasis and metastatic cell invasion, using a mouse model of human breast cancer.
The breast cancer cells secreted HSP90, which then interacted with MMP2 and MMP9 to activate them. MMP9/MMP2 antibody assays showed that while 4C5 antibodies did not restrict the release of inactive MMP2/MMP9 from cancer cells, their activation was blocked through disruption of the extracellular HSP90/MMP binding mechanism by mAb 4C5. This in turn prevented the metastatic deposit of tumour cells into the lung tissue. The conclusion was that 4C5 antibodies could have potential therapeutic use in cancer.
Tags: Collagen IV, Collagen IV antibody, HSP90, HSP90 antibody, Laminin 5, Laminin 5 antibody, MMP antibody, MMP13, MMP13 antibody, MMP2, MMP2 antibody, MMP3, MMP3 antibody, MMP7, MMP7 antibody, MMP9, MMP9 antibody
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Apoptosis, Cancer, Heat Shock Proteins, Tumor | No Comments »
Tuesday, October 18th, 2011
The main function of the matrix metalloproteinase (MMP) family was originally thought to be restricted to degradation of extracellular matrix (ECM) proteins. However, studies with their antibodies have identified several other functions. We at Novus Biologicals have an extensive range of MMP antibodies for research.
The MMP family is divided into two subgroups: soluble MMPs, and membrane-type MMPs (MT-MMPs). Studies using transmembrane MMP antibodies have shown a pivotal role in tumourigenesis, with expression raised in many types of cancer.
Work with MMP2 antibodies identified the enzyme as a possible early tumour marker. MT1-MMP (also called MMP-14) activates MMP2; antibody experiments have suggested this interaction may be involved in tumour invasion. Elevated expression of MT1-MMP has been strongly linked to tumour cell growth, differentiation and migration, leading to metastasis. Importantly, it has a crucial role in tumour angiogenesis.
In 2009, L.Devy et al. reported that inhibition of MT1-MMP by selective antibodies blocked metastasis, angiogenesis and tumor progression, suggesting the protein has therapeutic potential as a target for Vascular Disrupting Agents (VDAs). VDAs work by disrupting angiogenesis, starving the tumour of nutrients and oxygen.
A number of VDAs are based on colchicine, a natural toxin derived from the Autumn Crocus. These target the colchicine-binding site of tubulin, inducing vasculature changes and eventual tumor necrosis. However, they have systemic cardiotoxic effects in healthy tissue, compromising their therapeutic value.
Recently, a team from Bradford University developed [PMID: 20663911] a novel colchicine-based agent, ICT2588, which is selectively metabolised to an active VDA (ICT2552) within tumours, with negligible levels in normal tissues. A number of MMP antibodies were used, including the MT1-MMP and MMP2 antibody. The results showed ICT2588 to be non-toxic until specifically activated in MT1-MMP–dependent angiogenic tumor neovasculature.
Tags: Angiogenesis, MMP antibody, MMP14, MMP14 antibody, MMP2, MMP2 antibody, Vascular Disrupting Agent
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Tumor | No Comments »
Tuesday, September 20th, 2011
We at Novus Biologicals place a lot of emphasis on the kinase signaling pathways. Kinases, or phosphotransferase enzymes play a key role in phosphorylation signaling. Over 500 human protein kinases have so far been discovered. They play essential roles in glucose metabolism, apoptosis, lipid transport, cell migration, cellular differentiation and other cellular functions. Additionally, they often play multiple roles, in more than one cascade. The complex nature of phosphotransferase pathways can be shown by the many areas that AKT antibody research covers.
Antibody research has identified three Akt proteins that play essential roles in many signaling pathways. Akt1 is known to play key roles in a number of pathways, including apoptosis, protein synthesis, skeletal muscle growth and angiogenesis. Akt1 inhibits the pro-apoptotic BAD/Bcl-2/Bcl-X complex by BAD phosphorylation, and has been implicated in many types of cancer.
Akt2 is needed for activation of the glucose transporter GLUT-4, and is essential to the insulin signaling pathway. It also silences GSK3, which inhibits a number of proteins, including glycogen synthase, by phosphorylation. Akt antibody research has shown Akt2 plays a similar role in Wnt signaling; GSK-3 phosphorylates beta Catenin in this pathway.
The kinase signaling pathways are complex and time consuming to research, so anything antibody suppliers can do to make life easier is welcome. We at Novus Biologicals recently introduced a new range of Mix-and-Match Pathway Assay Kits, which allow comparison of six key kinase signalling pathways – including those utilising AKT. Antibody analysis is easily achieved, using a simple ELISA multiwell format.
Tags: Akt antibody, AKT1, AKT1 antibody, AKT2, AKT2 antibody, BAD, BAD antibody, Bcl2, Bcl2 antibody, BCL2L1, BCL2L1 antibody, beta Catenin, beta Catenin antibody, Glucose Transporter GLUT4, Glucose Transporter GLUT4 antibody, Glycogen Synthase, Glycogen Synthase antibody, GSK3 GSK3 antibody, Kinases, Mix-and-Match Pathway Assay Kit, Phosphorylation, Signal Transduction, Signaling Pathways, Wnt Signalling
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Apoptosis, Cancer, Lipid & Metabolism, Tumor | No Comments »
Thursday, September 1st, 2011
Hypoxia-Inducible Factor-1 (HIF-1) is a highly conserved heterodimeric transcription factor. Novus’ antibody catalogue contains an extensive range of both HIF-1 alpha and HIF-1 beta, useful for hypoxia, angiogenesis, cancer and many other areas of research.
The Hypoxia-inducible factors play an essential role in homeostasis, responding to changes in the available oxygen content of the cell. Specifically, they respond to hypoxic, or low oxygen conditions. There are three main members of the human HIF family, each comprising an alpha and beta subunit, encoded by a separate gene. All these proteins are represented in our antibody catalog, which has a particularly extensive range of top quality HIF-1 alpha antibody products.
Much of our knowledge of Hypoxia Inducible Factors is based on studies of HIF-1, which is expressed in practically all oxygen-breathing species. The alpha and beta subunits share a similar tri-domain structure. DNA binding takes place at a bHLH domain on the N-terminus; heterodimerization takes place at a central Per-ARNT-Sim (PAS) domain, and recruitment of transcriptional coregulators is facilitated at the C-terminus.
In normoxic conditions, HIF alpha subunits undergo rapid degradation following hydroxylation by HIF prolyl-hydroxylases, and ubiquitination by VHL E3 ubiquitin ligase. In 2004, HIF-1 alpha antibody research by Semenza, et al. suggested HIF prolyl-hydroxylase utilizes oxygen as a substrate, and is inhibited in hypoxic conditions. Further inhibition occurs as a result of succinate build-up.
Our HIF-1 alpha antibody products may also be of use to drug research groups, and further study in this area is ongoing. Recently, several selective HIF prolyl-hydroxylase inhibitors were developed, for use in oral treatment of anaemia. Inhibition of HIF prolyl-hydroxylase leads to prolonged activity of HIF-1 alpha, resulting in increased levels of erythropoietin.
Tags: Erythropoietin, Erythropoietin antibody, HIF Prolyl Hydroxylase, HIF Prolyl Hydroxylase antibody, HIF-1 alpha, HIF-1 alpha antibody, HIF-1 beta, HIF-1 beta antibody, Hypoxia
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Hypoxia | No Comments »
Monday, June 13th, 2011
The enzymes of the Matrix Metalloproteinase (MMP) family assist in the degradation of the extracellular matrix, under both normal and pathological conditions. MMP antibodies have identified roles in a number of physiological processes, such as embryonic development and tissue remodelling. They also regulate enzyme cascades, expression of various proteins and the migration of both normal and malignant cells.
The MMP2 antibody is used in a number of research areas, including metastasis, angiogenesis, apoptosis and tumor suppression. MMP2 antibody studies have shown MMP2 plays a specific role in the degradation of collagens and Gelatin 1. It also functions in angiogenesis, tissue repair, vascularization, inflammation, atherosclerotic plaque rupture, endometrial menstrual breakdown and tumour metastasis. It is secreted in inactive form, being activated by proteinase cleavage via the Ras signalling pathway.
In 2001, S. Papadopoulou et al. published MMP2 antibody research which used immunohistochemical staining techniques to compare MMP2 levels in both normal human colon mucosa and colorectal cancer cells. Both tissues showed immunohistological localization of MMP2. However, antigen levels were significantly higher in the tumour cells, with staining intensity higher in malignant adenocarcinomas than benign adenomas.
K.S Park et al. also used MMP2, MMP9 and TIMP2 (tissue inhibitor of metalloproteinase-2) antibodies to identify gene profiles which may increase the risk of colorectal cancer. Specific SNPs (single-nucleotide polymorphisms) were identified in both TIMP2 and MMP2, which were associated with tumourigenesis. M.J Kang. et al have also used MMP2 antibody products to probe the relationship of MMP2 SNPs to SNPs in VEGF and HIF1A, but no association was found.
We at Novus Biologicals have a wide range of top quality MMP2 antibody products. Please contact our technical support department (technical@novusbio.com) with any questions or for additional information on this product line.
Tags: Antibodies, Matrix Metalloproteinase, MMP2, MMP2 antibody, MMP9, MMP9 antibody, TIMP2, TIMP2 antibody, VEGF, VEGF antibody
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Apoptosis, Heart Disease, Inflammation, Tumor | No Comments »
Monday, May 9th, 2011
There are three human isoforms of the AKT gene, which plays a key role in several signalling pathways. Akt antibody studies have shown the Atk kinases to play a diverse number of roles within the cell, regulating angiogenesis, apoptosis, protein synthesis, intermediary metabolism and cellular differentiation. We at Novus Biologicals have a wide range of Akt products on our antibody database, targeting all three isoforms.
Akt antibody research has identified specific roles for the three isoforms of Akt. Akt1, the founding member of the family, is of major importance to cancer researchers. A key player in the PI3K/AKT/mTOR and several other pathways, Akt1 signalling promotes hypertrophy (growth) of skeletal muscle and other tissues, and promotes cell survival by inhibiting apoptotic processes. Akt2 plays an important role in insulin signalling, while Akt3 is thought to be involved with neuronal development.
Akt1 was originally identified as an oncogene in the AKT8 transforming retrovirus, and has since been shown to be critical to the growth and progression of a number of human neoplasms. It also plays an indirect role, acting on oncogenic signals resulting from mutations in tumor-suppressor genes and other oncogenes.Today, the entire Akt antibody database is used in cancer research. Overexpression of Akt2 and Akt3 has been directly linked to the development of epithelial neoplasms, breast tumors, prostate cancer, ovarian cancer and skin cell melanomas. Researchers at the MORI Institute, Tufts University, are using insertional mutagenesis and other genetic techniques to probe the function of all three isoforms. Other groups are using Akt antibody products to develop antineoplastic drugs.
Tags: Akt, Akt antibody, AKT1, AKT1 antibody, AKT2, AKT2 antibody
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Apoptosis, Cancer, Lipid & Metabolism, Neuroscience, Stem Cells | No Comments »
Monday, April 11th, 2011
Laminin is one of a large number of proteins expressed on the basal laminar of the ECM (extracellular matrix). The laminin antibody database covers several proteins, which interact with integrins and other receptor proteins to support cellular differentiation, morphology, migration, cell survival and the maintenance of tissue phenotypes. Laminin antibody studies have played a key role in research into angiogenesis and tumor development.
The ECM plays an essential role in angiogenesis, providing support for the developing blood vessel and releasing pro- and anti-angiogenic factors which regulate stability and cell survival. During angiogenesis, the ECM basal membrane is degraded, enabling migration of endothelial cells. Although angiogenesis is necessary for wound healing, it is also a feature of metastasis and tumor formation.
The laminins are a family of around 15 trimeric alpha/beta/gamma-chain proteins. Laminin I has been identified as a major promoter of angiogenesis, with endothelial cells shown to differentiate into capillary-like structures on a laminin I-enriched Matrigel matrix. Recent laminin antibody research has identified laminin I to have 20 angiogenic sites, with the α5ß1 and αvß3 integrins identified as surface receptors. These have been shown to specifically target the C16 Y1 chain peptide, which is the only Y1 chain to block laminin I adhesion to collagen and fibronectin. C16 has been shown to be angiogenic in vivo.
We at Novus Biologicals have an extensive antibody database covering laminin research. Our most popular products include a rabbit polyclonal Laminin antibody (NB300-144) and the corresponding active mouse Laminin protein (NBP1-78301) that was used at the immunogen. We also offer excellent sandwich ELISA assays kits for mouse (BEK-2056-2P) and rat (BEK-2055-2P) Laminin. These kits contain 96-well strips pre-coated with a capture laminin antibody; biotinylated polyclonal laminin antibody; an enzyme Avidin-Biotin-Peroxidase complex and a peroxidase substrate, allowing for convenient and accurate analysis of laminin concentrations in sera, plasma, lysates and supernates.
Tags: Fibronectin, Fibronectin antibody, Laminin, laminin antibody, Wound healing
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Tumor | No Comments »
Tuesday, March 15th, 2011
Ischemic cardiovascular disease is the leading cause of death for both men and women in the US and most other industrialized countries. Most commonly caused by atherosclerosis of the coronary arteries, ischemic cardiovascular disease is characterized by a reduced blood supply to the heart, leading to low oxygen, glucose, and pH levels.
Therapeutic angiogenesis using bone marrow cells has become a promising new field of treatment for ischemic cardiovascular disease (R Laham, et al.). However, maintaining the bone marrow-derived angiogenic cells (BMDACs) under an ischemic microenvironment remains a major obstacle for this treatment.
In a new study published in Blood Journal [PMID: 21389314], S Rey, et al. demonstrate that HIF-1 activity can be induced to metabolically reprogram BMDACs, resulting in a significant survival advantage in ischemic tissue. Specifically, dimethyloxalylglycine (DMOG) was used to induce HIF-1 activity, which reduced tissue necrosis and doubled the half-life of BMDACs in ischemic tissue. These findings indicate that a HIF-1-based gene and cell therapy approach will likely enhance the therapeutic efficacy of BMDACs.
Novus Biologicals antibodies against HIF-1 alpha, lactate dehydrogenase A, and PDK1 were used in this study for FACS and WB analysis, respectively. Novus currently offers a wide variety of excellent hypoxia antibodies for use in angiogenesis related research. Please contact our technical support department (technical@novusbio.com) with any questions or for help choosing the optimal antibody for your experiment.
Tags: Atherosclerosis, Heart Disease, HIF-1 alpha, HIF-1 alpha antibody, Lactate Dehydrogenase A, Lactate Dehydrogenase A antibody, PDK1, PDK1 antibody
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Cancer, Hypoxia | No Comments »
