Anti Aging Products Based On DNA

According to recent statistics, many young Americans flock to their doctor in search of various ways to wipe away life’s early signs of aging. Even modern science and technology are challenging the truth that life is finite and old age is inevitable. Scientists are burning the midnight oil in formulating some sort anti aging products that can deliver early detection, prevention, treatment and reversal of aging. They are constantly working to enhance the quality of human life span and this is what appears to be the most important riddle for this millennium.

Though not refuting the preeminence of modern science, let us also not forget that no matter what, one cannot escape the wrath of time. Andrew Marvell, the famous English poet has rhetorically stressed on time’s rage on a beauty in his poem, “To His Coy Mistress”: “Time's winged chariot hurrying near; and yonder all before us lie Deserts of vast eternity. Thy beauty shall no more be found”.

It is said that as soon as an individual takes birth, his or her process of dying starts. From the moment of birth, we begin a process of growth and development that continues in to the years of reproduction. However, as the Mother Nature dictates, most of us begin to experience lose muscle tone, and most importantly, the graceful motions of youth. Although admittedly, one cannot stop time or reverse back the aging clock but the only step to maintain the youthful appearance is to slow down the aging process.

During the Human Genome Project, scientists revealed that our DNA influences one’s ageing process. If an individual’s DNA is impaired or there is some flaw, then evidently, it starts showing up on the face and also it results in hastened aging process. Thus, to slow down this accelerated aging process, Anti aging products based on one’s DNA, are being prepared by many pharmaceutical companies. The idea behind these DNA based anti aging products is very simple: a DNA cheek swab test ascertains which faulty genes in the DNA are causing accelerated aging process. After this detection, DNA based Anti aging products is prepared to repair the damaged DNA or faulty genes. Anti aging products contain the essential nutrients that repair the damage done to the DNA by environmental stresses, thus, fighting the hastened aging process.

DNA Screenings: A Thing of the Future is hereDNA Screenings

Knowing your family's genetic history may someday save your life or that of someone you love. Based on genetic technology, a unique DNA analysis can be made for an individual, stating all the deficiencies and potential genetic disorders, thus, preparing one to fight the signs and symptoms of diseases. What better gift can a loved one leave behind?

The vast spectrum of DNA can give us insight on the value it can play in our lives. These startling revelations came into light during Human Genome Project. DNA research and Human Genome Mapping has allowed scientists to discover about how one’s unique DNA influences one’s health. Based on these studies, a simple DNA test at home lets a person know what exact supplements one’s body needs and how much. This revolutionary breakthrough has lead to the designing of vitamin supplements based on one’s unique DNA.

An individual’s DNA holds the secret to enhanced state of wellbeing as well as diminished state of wellbeing. Even a slight difference in this genetic code leads to a living being’s vulnerability to diseases. vitamin supplements are made after DNA analysis, meeting an individual’s needs and requirements to keep him or her healthy. Total wellbeing can be attained through DNA customized supplements as they contain the essential nutrients which help to regain the lost health and also slows the aging process. As these supplements are tailor made, therefore, each supplement is based on an individual’s own requirements, augmenting the complete well being

QuikChIP Chromatin Immunoprecipitation Kits

IMGENEX QuikChIP Certified Antibodies The Basics...
The principle of the ChIP assay is simple: selective enrichment of a chromatin fraction containing a specific target. However, the process can be technically challenging. It is with these challenges in mind that IMGENEX developed the QuikChIP Kit for chromatin immunoprecipitation. QuikChIP includes optimized ready-to-use buffers and inhibitory reagents, as well as a comprehensive technical manual.

* Quick & simple
* Optimized ready-to-use buffers & protocol
* Useful for Histone and non-histone proteins

Reagents for 25 ChIP assays and sheared Chromatin preparations


QuikChIP Certified Antibodies

IMGENEX offers a growing number of antibodies that have been validated for use in ChIP assays and we are continually testing and validating new products for use in ChIP. Below is a list of our currently available QuikChIP Certified Antibodies. Be sure to check our website often as we are releasing new antibodies every week!

Sheared Chromatin

IMGENEX QuikChIP™ Sheared Chromatin is ready-to-use, sheared, cross-linked chromatin prepared from mammalian cell extracts. This novel product enables researchers to carry out ChIP assays in the absence of cell culture facilities or sonication equipment. It is also useful as a sheared, cross-linked chromatin positive control, alongside your own cell extracts.

Conditions for cell culture, DNA-protein cross-linking, and the sonication shearing process have been optimized for each human and mouse cell type.

IMGENEX has now p73 phosphospecific antibody

The p53 family member, p73, also known as tumor protein 73 (TP73) has been recently identified as a structural and functional homolog of the tumor suppressor protein p53. In accordance with its structural similarity, p73 functions in a manner analogous to p53 by inducing tumor cell apoptosis and participating in the cell cycle checkpoint control through transactivating an overlapping set of p53/p73-target genes. Under these conditions p73 is tyrosine-phosphorylated by c-Abl, a prerequisite modification for p73 to elicit cell death in fibroblasts. Increasing knowledge of its function, however, has cast doubts on its role. Like p53, the protein contains different isoforms with distinct and sometimes opposite functions.
Like other members of the p53 family, p73 protein share the same modular organization consisting of an N-terminal transactivation domain, central sequence-specific DNA-binding domain, and a C-terminal tetramerization domain. However, the p73 gene encodes multiple isoforms varying in their N and C termini. In some cases, the use of a cryptic promoter generates isoforms lacking the transactivation domain located in the N terminus of p73 (deltaNp73 alpha and deltaNp73 beta). The p73 gene also generates several forms with varying C-terminal extensions,TAp73 (p73 alpha, beta, gamma, delta and epsilon). These splicing variants are expressed differently in normal human tissues and cell lines. The p73 gene has been mapped to human chromosome 1p36, a region that is frequently deleted in variety of human cancers including neuroblastoma, colon cancer, and breast cancer.
The precise functions of p73 proteins in the organism and the signaling pathways that regulate their activity are still not well established. An interesting recent report shows that p73 is required for p53-dependent apoptosis induced by DNA damage as well as p53-independent apoptosis. These observations and the fact that p73 expression is affected in certain tumors suggest that p73 may function as a tumor suppressor gene. However, p73 deficient mice are not particularly prone to cancer, and only rarely have mutation or inactivation of p73 expression been found in human tumors. On the contrary the deltaNp73 isoforms have oncogenic potential and act in a dominant negative manner against TAp73 as well as p53. The Delta N isoforms of p73 can also protect neurons from apoptosis. Besides like p53, p73 may also play a role in developmental processes. Several lines of evidence show that p73 may play a role in nervous system and immune system development, thus implicating the role of p73 in cellular differentiation.

Data Analysis through Tissue Analysis

The existing body of literature using Western blot analysis has been primarily defined with data from tumor, immortal, and primary cells growing in vitro. Collectively, results obtained over decades have been integral to the dogma that up- and down-regulation of proteins can be leveraged as Biomarkers of normal development, homeostasis, and disease. However, in contrast to tissues which are composed of multiple cell types, cell lines growing in culture which theoretically consist of clonal populations. Thus, validation or modification of western blot parameters collectively established from decades of cell line data in tissue lysates is key for Biomarker discovery.

IMGENEX can provide you with normal post mortem, cancerous, diseased, and normal adjacent clinical specimens matching your requirements. Custom collection protocols are welcomed. Specimens are available as frozen or formalin-fixed, paraffin-embedded tissue blocks, and include clinical case and detailed pathology reports, as well as final diagnosis and staging. Learn more about this service by visiting our website, or downloading our Tissue Procurement literature.

 

ATM (Ataxia Telangiectasia Mutated) Antibodies from Imgenex

ATM, the gene product mutated in the cancer susceptibility syndrome ataxia–telangiectasia, is related to proteins involved in DNA repair and cell-cycle control. It encodes a nuclear 350 kDa phosphoprotein containing a carboxy terminus phosphatidylinositol 3-kinase (Pl-3 kinase) catalytic domain shared by members of a superfamily of large eukaryotic proteins involved in intracellular signaling, DNA-damage induced cell cycle checkpoints, DNA repair and recombination. It was discovered as mutated proteins in patients with ataxia-telagiectasia (A-T), a severe genetic disorder characterized by cerebellar degeneration, neuromotor dysfunction, chromosomal instability, immune system defects, cancer predisposition, and acute sensitivity to ionizing radiations. In undamaged cells it is present as a dimer or oligomer molecule in which the kinase domain is silent because associated with the FAT region of another ATM monomer. Following DSB formation, it rapidly autophosphorylates on residue Serine 1981, and the inactive ATM dimers are converted (dissociated) into active ATM monomers. Active phosphorylated ATM molecules interact and phosphorylate downstream proteins that affect one or more of the cell cycle checkpoints. Some of the known substrates are the p53 protein and its ubiquitin ligase, MDM2; the Nbs1 protein; the Brca1 protein, which interacts with other repair proteins; the checkpoint kinase 2, Chk2; the Rad17 protein and the chromatin remodeling protein SMC1. Phylogenetic analyses reveal that the ATM protein is most closely related to several very large proteins that define a subgroup of the PI 3-kinase family which include the Schizosaccharomyces pombe Rad3 protein and its probable Saccharomyces cerevisiae homologue, Mec1p/Esr1p. Other proteins in the ATM family are S. cerevisiae Tor1p and Tor2p and their mammalian counterpart FRAP, which function, at least in part, by controlling progression through the G1 phase of the cell cycle. The ATM gene provides instructions for making a protein that is located primarily in the nucleus of cells, where it helps control the rate at which cells grow and divide and also assists cells in recognizing damaged or broken strands of DNA. It has been suggested that it acts as a lipid kinase, and feeds the phosphorylated lipids into signaling pathways to regulate cell-cycle progression or the activity of DNA-repair components. It regulates NF-κB activity and control the transcription of many genes that play important roles in the development and function of the immune system. In the DNA-damage response pathway, it acts upstream of p53 to induce cell cycle arrest at the G1/S and G2/M boundaries and a slowing of the S-phase. Signalling by ATM involves interactions with and phosphorylation of critical molecules, including the mitotic checkpoints Chk1 and Chk2. Apart from its role in ataxia telangiectasia (AT), ATM gene mutations have also been found in T-cell prolymphocytic leukaemia patients with no family history of AT and in non-Hodgkin’s lymphomas.

Epigenetic and Signal Transduction Reagents

IMGENEX offers over 90 Chromatin, DNA Methylation & Repair, and DNA Fragmentation-related antibodies, many of which have been cited in numerous peer-reviewed journals. These antibodies have been used to study transcriptional silencing, identify DNA-protein interactions, and characterize the sequence of molecular binding events.

Surging interest in understanding the mechanisms of epigenetics is attracting researchers worldwide from a wide variety of scientific disciplines. Epigenetics is the study of the heritable changes in gene function that occur without changes in DNA sequence. It is becoming increasingly apparent that an epigenetic phenomenon is integral to both normal and aberrant gene regulation.

Histone proteins are thought to be the major carriers of epigenetic information. Histones form the nucleosomal complexes that make up the eukaryotic chromatin, which packages and organizes DNA in the nucleus. The nucleosome, the basic repeating subunit of chromatin, is composed of DNA coiled around an octamer of two molecules, each with four core histone proteins: H2A, H2B, H3 and H4. Each core histone is composed of a structured, three-helix domain called the "histone fold" and two unstructured tails.

The N-terminal histone tails extend outward from the DNA to interact with the nuclear environment where they are the targets of multiple, diverse signaling pathways. Signal transduction pathways impinging on the N-terminal histone tails result in a number of post-translational modifications including acetylation, phosphorylation, poly(ADP-ribosylation), ubiquitination and methylation. These modifications play critical roles in regulating chromatin structure and gene expression

Actin Antibody in Imgenex

Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is the monomeric subunit of microfilaments, one of the three major components of the cytoskeleton, and of thin filaments which are part of the contractile apparatus in muscle cells. It is the most abundant protein in the typical eukaryotic cell, accounting for about 15% in some cell types. The protein is highly conserved, and forms a huge variety of structure in cells in concert with a huge numbers of actin binding proteins. The actin filaments interact with myosin to produce a sliding effect, which is the basis of muscular contraction and many aspects of cell motility, including cytokinesis. The individual subunits of actin are known as globular actin (G-actin) that assembles into long filamentous polymers called F-actin. Two parallel F-actin strands twist around each other in a helical formation, giving rise to microfilaments of the cytoskeleton. Microfilaments measure approximately 7 nm in diameter with a loop of the helix repeating every 37nm. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. It exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. Actin from many sources forms a tight complex with deoxyribonuclease (DNase I) although the significance of this is still unknown. The formation of this complex results in the inhibition of DNase I activity, and actin loses its ability to polymerise. It has been shown that an ATPase domain of actin shares similarity with ATPase domains of hexokinase and hsp70 proteins. In vertebrates there are three groups of actin isoforms: alpha, beta and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. MreB, a major component of the bacterial cytoskeleton, exhibits high structural homology to its eukaryotic counterpart actin. Further it has been suggested that members of the Rho family of small guanosine triphosphatases have emerged as key regulators of the actin cytoskeleton, and through their interaction with multiple target proteins, they ensure coordinated control of other cellular activities such as gene transcription and adhesion.