Antibody News

CIP2A: The Cancerous Inhibitor of Protein Phosphatase 2A

Wednesday, September 19, 2012 - 08:00

Immunohistochemistry: CIP2A Antibody

The autoantigen p90 is a recently discovered protein that binds to and inhibits Protein Phosphatase 2A (PP2A) activity, thereby playing a critical role in cancer progression. Thus, p90 was renamed the "cancerous inhibitory protein of PP2A" or CIP2A. Most interestingly CIP2A was shown to inhibit of the degradation of c-Myc oncoprotein and was reported to be overexpressed in several cancers (1). However, the clinical relevance of CIP2A to human cancers had not been demonstrated, and the mechanism of its regulation and its clinical role in cancer are unknown. A recent study evaluated tissue microarrays consisting of 223 gastric...

CENPF Antibodies as Potential Cancer Markers

Monday, September 17, 2012 - 10:49

Centromere protein F (CENPF), also named mitosin, is a large human protein of 3113 amino acid residues. Its expression and localization are cell cycle-dependent. The protein levels are low in G1 phase but elevated from S to early M phase. CENPF is a nuclear matrix protein in interphase but is relocated to the kinetochore, the major site of microtubule attachment on chromosome, in M phase (1). Accumulating evidence suggests that CENPF is an important protein involved in chromosome alignment and kinetochore-microtubule interaction.

Western Blot: CENPF Antibody

Depletion of CENP-F results in chromosome misalignment and improper...

FOXP3: Master Regulatory Transcriptional Factor

Thursday, September 13, 2012 - 12:23

FOXP3, a forkhead family transcription factor specially expressed in regulatory T (Treg) cells, controls the expression of many key immune-regulatory genes. Treg cells are a population of T lymphocytes that have critical roles in the immune system homeostasis and tolerance to self and foreign antigens, the body's response to cancer and infectious agents. The transcription factor Foxp3 is crucial for Treg differentiation and function, and various Foxp3 mutations, both in scurfy mice and IPEX (immune dysregulation polyendocrinopathy, enteropathy, X chromosome-linked syndrome) patients, result in the development of complex autoimmune diseases, resulting from Treg deficiency (1). However, FOXP3 is also expressed in activated conventional human T cells, it was found that FOXP3...

Beclin 1: Regulator of Autophagy and Apoptosis

Wednesday, September 12, 2012 - 09:00

Beclin 1 is the mammalian orthologue of the yeast Apg6/Vps30 gene. Beclin 1 can complement the defect in autophagy present in apg6 yeast strains and stimulate autophagy when overexpressed in mammalian cells (1) and can bind to Bcl2, an important regulator of apoptosis (2) suggesting a role in two fundamentally important cellular pathways: autophagy and apoptosis. Beclin 1 is mono allelically deleted in human breast and ovarian cancers and is expressed at reduced levels in tumors, and is present in a complex bound to glutamate receptor δ2 (GluRδ2) in the nervous system leading to the activation of autophagy and death of cerebellar Purkinje cells (3).

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Calreticulin: a Multiprocess Calcium Buffering Chaperone

Monday, September 10, 2012 - 09:05

Calreticulin is a Calcium binding chaperone that has multiple functions both inside and outside the endoplasmic reticulum. Calreticulin is involved in the quality control of newly synthesized proteins and glycoproteins, interacting with various other ER chaperones, specifically Calnexin. Calreticulin also plays a crucial role in regulating intracellular Calcium homeostasis, associating calreticulin with a wide variety of signaling processes.  The role of calreticulin outside of the ER is extensive, which includes wound healing and immunity (1).

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Carbonic Anhydrase IX Roles in Tumor Growth, Survival and Invasion

Friday, September 7, 2012 - 10:19

Carbonic anhydrase IX (CAIX) is a membrane-associated carbonic anhydrase, strongly induced by hypoxia. CA IX is overexpressed by several cancer cells from many tumor types, and is a component of the pH regulatory system invoked by these cells to combat the deleterious effects of a high rate of glycolytic metabolism. CA IX functions to help produce and maintain an intracellular pH favorable for tumor cell growth and survival, while at the same time participating in the generation of an increasingly acidic extracellular space, facilitating tumor cell invasiveness (1).

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ADFP and Lipid Storage Disease

Thursday, September 6, 2012 - 09:03

Adipocyte differentiation-related protein (ADFP) is found on the surface of lipid droplets in most mammalian cell types. In mammals, lipid droplets are most abundant in adipose tissue, where stored triacylglycerol (TAG) provides the primary energy reserve for the organism. Lipid droplets in steroidogenic cells contain cholesteryl esters used in the synthesis of steroid hormones. Most other mammalian cells contain smaller lipid droplets, whose function remains unclear.

Immunocytochemistry/Immunofluorescence: ADFP Antibody

These lipids droplets may serve as local energy reserves...

CD11b/CD18 and Neutrophil-Epithelial Interactions as Targets for Anti-Inflammatory Therapies

Tuesday, September 4, 2012 - 12:38

The beta-2 integrins, a family of four cell surface transmembrane glycoproteins expressed only on leukocytes, include CD11a/CD18, CD11b/CD18, CD11c/CD18, and CD11d/CD18. They consist of a common beta subunit (CD18) and homologous alpha subunits (CD11a-d) that bind noncovalently to form an alpha/beta heterodimer. Studies with functionally inhibitory monoclonal antibodies to CD11b/CD18 demonstrate the role of CD11b/CD18 in inflammatory processes, including polymorpho nuclear leukocyte (PMN) adhesion and migration across the endo and epithelium (1).

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Myc-tag: The "Monkey Wrench" of Proteomic Tools

Thursday, August 30, 2012 - 12:21

c-Myc is a well-characterized transcription factor encoded by the c-Myc gene on human chromosome 8q24. This cellular proto-oncogene, also known as p62, is commonly activated in a variety of tumor cells and plays a crucial role in cellular proliferation, differentiation, apoptosis, and cell cycle progression. The myc-tag antibody contains a short sequence epitope that is widely and commonly used as a protein fusion tag. It is a very powerful investigative research toolfor applications such as immunochemistry, protein purification, ELISA purification, and protein localization (1).

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"Actin the Fool" about Cytoskeleton Structure

Tuesday, August 28, 2012 - 13:58

Actins are highly conserved, commonly found and abundant proteins involved in several types of cell motility as well as cytoskeleton maintenance. In vertebrate species, three main groups of actin isoforms, the alpha, beta and gamma, have been identified. Alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Beta and gamma actins co-exist in most cell types as components of the cytoskeleton and mediators of internal cell motility. Actin antibodies have been used for basic studies such as classifying and identifying how different subtypes of plant plasmodesmata function in intracellular transport across cell and tissue boundaries (1). to determining the stoichimetry of Nck-/N-WASp (neural Wiskott-Aldrich syndrome protein)-dependent...

Vimentin in Wound Healing

Monday, August 27, 2012 - 09:57

Vimentin is a fundamental 10 nm type III intermediate filament (IF) protein found in many mesenchymal and epithelia tissues, tissue culture cells, and developing neuronal and astrocytic precursor cells of the central nervous system. It frequently co-polymerizes and forms heteropolymer filaments with other IF proteins such as GFAP (in astrocytes), desmin (in muscle cells) and neurofilament proteins (in developing neurons). Vimentin antibodies were used in human mammary epithelial cell studies to show that vimentin mediates cell migration within classic in vitro wound-healing models (1). Comparative expression data indicates that vimentin expression correlates with transformed cells with highly invasive capability (2).

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TrkB and Nervous System Function

Thursday, August 23, 2012 - 11:23

Neutrophins and their receptors play an important role in regulating the development of both the central and peripheral nervous systems. Neurotrophin ligand binding to each of their respective Trk cellular receptors is essential for the growth and survival of neurons. Specifically, TrkB and its primary ligand brain-derived neurotrophic factor (BDNF) are rapidly and transiently induced in response to neuronal injury, as monitored by TrkB antibodies, as well as crucial for synaptic plasticity (1).

Immunohistochemistry: Trk B Antibody

Using TrkB antibodies for Western and immunohistochemistry, Unsain,...

TLR9 Antibodies in Immunity Research

Tuesday, August 21, 2012 - 10:35

Toll-like receptor 9 (TLR9) is a member of the toll-like receptor family that plays a key role in pathogen recognition and activation of innate immunity. Scientists using TLR9 antibodies have found the protein is highly conserved from Drosophila to humans, with a high degree of structural and functional homology (1,2). TLR proteins recognize pathogen-associated molecular patterns (PAMPs) expressed on a wide spectrum of exogenous and endogenous ligands – including infectious agents - and regulate the cytokine production required for effective immunity development. Studies in mice and humans with TLR9 antibodies demonstrate that TLR9 detects unmethylated CpG dinucleotides in bacterial DNA to trigger the downstream immune response (3).

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Characterizing Synaptophysin is "a Snap"

Monday, August 20, 2012 - 09:12

Synaptophysin is an integral membrane glycoprotein found within the small synaptic vesicles in brain and endocrine cells. Studies with synaptophysin antibodies show that it is one of the most abundant small vesicle proteins, constituting approximately 7% of the total vesicle. Synaptophysin antibodies were used to monitor synaptophysin and synaptobrevin complexes in mature nerve terminals, where it was found that the dual complex associated with other fusion proteins such as syntaxin and SNAP25 to allow the SNARE complex to form, and therefore enable vesicle membrane fusion (1). Using synaptophysin antibodies for immunofluorescence and immunoEM (electron microscope) studies, Tixier-Vidal, et. al. showed that synaptophysin is released from the golgi apparatus in a vesicular form and transported to nerve endings (2).  While it has...

New Techniques Using Phosphoserine Antibodies

Thursday, August 16, 2012 - 12:51

Phosphoserine, the phosphorylated modification of the amino acid serine, is a central post-translational modification within a cell for many biological and biomedical processes. The phosphorylation of specifically four residue types - histidine, serine, threonine, and tyrosine occurs both within the cell as well as at the cell surface. This exquisitely controlled regulatory system controls a vast number of intertwined and interconnected downstream signaling pathways and cascades.  The signal transduction networks that rely on phosphorylation are very complex, such that multiple types of phosphorylation often occur within any one given protein, at multiple sites and hotspot areas. There exist a great number of techniques and technologies for phosphoamino acid detection and study, each with strengths as well as limitations, as reviewed by Yan, et. al. (1). Powerful new methods using...

"Whats the Hap" with GFAP?

Tuesday, August 14, 2012 - 11:27

Glial Fibrillary Acidic Protein (GFAP) is one of the major intermediate filament axonal proteins found in mature astrocytes, the star-shaped glial cells that comprise the majority of cells within the central nervous system (1). Astrocytes perform a wide range of functions - from uptake and regulation of neutrotransmitters, to intercellular space ionic balance and regulation, to blood/brain barrier formation, and recent studies suggest a role in learning and memory. Immunofluorescence studies with GFAP antibodies demonstrated the value of GFAP as a marker to distinguish astrocytes from all other glial cells in development (2). A Nature Genetics paper using GFAP antibodies to monitor GFAP expression was able to link the aberrant expression and overexpression of a mutated GFAP variant with a rare...

Using BrDU to Study Cell Proliferation

Monday, August 13, 2012 - 09:50

The thymidine analogue bromodeoxyuridine (BrdU) has a long, colorful history of heavy use in molecular and cytokinetic studies (1, 2). BrDU is incorporated into newly synthesized DNA only in S-phase cells, and then immunocytochemically detected with BrDU antibodies. This method allows for extremely accurate and comprehensive comparative studies of a variety of cells ranging from normal to neoplastic. Cells can be labeled in vitro or in vivo with the analogue, and then BrDU antibodies used to determine the resulting levels of incorporation. Such BrDU antibody studies allow quantitation of DNA-synthesis rates, cell fraction in S-phase, and construction of dynamic proliferation profiles (with such variables as S-phase transit rate and potential doubling time) using bivariate BrdU/DNA flow cytometry analyses. Some examples of the use of BrDU antibodies in oncology studies include their use to investigate replicative stress...

Beta Catenin in Cell Adhesion and T-cell Signaling

Friday, August 10, 2012 - 10:13

Beta Catenin is a cytosolic, 88 kDa intracellular protein that tightly associates with cell surface cadherin glycoproteins. It is one member of the catenin family that includes alpha Catenin, beta Catenin, and gamma Catenin. Colocalization studies using beta-catenin antibodies demonstrate that beta-catenin is a crucial link between cytoplasmic, cytoskeletal actin and transmembrane cadherin for tight cell-to-cell adhesion (1,2). Beta-catenin enters the nucleus and interacts with the Lymphoid enhancer factor-1 (LEF1) transcription factor family. It is normally inhibited by the glycogen synthase kinase (GSK) or casein kinase 1 as phosphorylation of beta-catenin targets it for ubiquitin-mediated degredation. The beta-catenin/TCF pathway is implicated in T-...

TLR9: "It Tolls for Thee"

Thursday, August 9, 2012 - 12:27

Toll-like receptors (TLRs) play an essential role in the activation of innate immunity, and TLRs are expressed in a large number of immune cells like B-lymphocytes, monocytes, plasmacytoid dendritic cells and at low levels in human respiratory cells as well as in epithelial cells. Immunohistochemistry and Western blott analysis using TLR9 antibodies in several human lung cancer specimens demonstrated high levels of TLR9 expression, suggesting TLR9 may be involved in the development of lung cancer and have the potential for the treatment of malignant tumors (1). Tissue microarray and immunoflorescence analysis in glioma cell lines and human brain tissues with TLR9 antibodies also revealed high levels of TLR9 expression. TLR9 expression increases according to the histopathological...

Perforin Antibodies for Detecting Immune System Diseases

Monday, August 6, 2012 - 12:46

 Perforin is a calcium-dependent pore forming cytolytic protein. Perforin is partially homologous to the terminal components of the membrane attack complex of complement and produces pores of up to 20nm in diameter on target membranes. Killer lymphocytes release perforin and granzymes from cytotoxic granules into the immunological synapse to destroy target cells as a critical mechanism in the defense against viruses and cancer (1).

Western Blot: Perforin Antibody

Increased perforin...

Phosphotyrosine: Affecting Locally Acting Globally

Friday, August 3, 2012 - 09:55

Over the past two decades, it has become clear that tyrosine phosphorylation plays a pivotal role in a variety of important signaling pathways in multicellular organisms. In the typical vertebrate cell, phosphotyrosine represents only a tiny fraction of total protein phosphorylation. Yet it is sufficient enough to induce malignant transformation (1), as unregulated phosphotyrosine signaling causes a breakdown in the normal regulation of cellular processes leading to several human diseases (2).

Western Blot: Phosphotyrosine Antibody

The oncogenic signaling pathways driving cell...

Synaptophysin and Dementing Disorders

Thursday, August 2, 2012 - 09:42

 Synaptophysin (a presynaptic vesicle protein) is an integral membrane glycoprotein originally isolated from presynaptic vesicles of bovine neurons. Synaptophysin is found in all nerve terminals and synaptophysin measurements have been used to quantify the number of terminals present during neuroanatomical remodeling and neural development (1). Accumulation of beta Amyloid and loss of synapses are hallmarks of Alzheimer's disease.

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Phosphoserine: A Basic Cellular Signal with Wide Ranging Effects

Tuesday, July 31, 2012 - 14:59

Phosphoserine is an ester of serine and phosphoric acid which results from posttranslational modifications. Phosphorylation is a key post-translational modification necessary for normal cellular signaling. Phosphorylated proteins mediate cell division, cellular differentiation, signal transduction and other key cellular signaling processes. Phosphorylation of serine residues on proteins is one of the keys to a cascade of reactions that are of great interest to many researchers. Phosphorylated serine residues have been detected by...

Using Myosin Antibodies for Tumor Identification

Thursday, July 26, 2012 - 10:53

Myosin is a super family of actin based molecular motors that hydrolyze ATP and generate physical force to move specific molecules inside the cell. This super family, divided into at least twenty four classes based on head domain sequence similarity and domain organization. The processivity of myosins along an actin filament and transport of intracellular ‘cargo’ are achieved by generating physical force from chemical energy of ATP followed by appropriate conformational changes (1).

Immunocytochemistry/Immunofluorescence: Myosin Antibody

Myosin has raised an interest because of its role in...

MYD88: Fanning Inflammation and Immune Responses

Monday, July 23, 2012 - 11:18

Myeloid differentiation primary response gene 88 (MYD88) encodes a cytosolic adapter protein that plays an essential role in innate and adaptive immune responses. MYD88 protein functions as an essential signal transducer in the interleukin-1 and in Toll-like receptor signaling pathways by acting as an adapter, which regulates the activation of several proinflammatory genes. MYD88 expression has been shown to be a critical factor against parasitic infections conferring resistance to the organisms in which it is expressed. Mice lacking MYD88 expression as detected by flow cytometry and Western blotting using antibodies against MYD88 were found to be more prone to parasitic infections (1).

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