Antibodies

This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Immunology and Nuclear Signaling research. Variant histones H2A are synthesized throughout the cell cycle and are very different from classical S-phase regulated H2A. H2AvD is vital for viability, but the exact function of variant histones H2A is not known.  H2A is a core component of the nucleosome, an octamer containing two molecules each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 bp of DNA. HsAvD  is expressed both maternally and zygotically and is found in embryos through to adults (female only).  The human homologue, H2AX, is phosphorylated by ATM protein kinase when double strand DNA breaks occur.  In mouse, H2AX ''knock out'' mice have an increased incidence of cancer.

Anti-Human IgG (H&L) DyLight 800 generated in rabbit detects human Immunoglobulin G (IgG), both heavy and light chains of the antibody molecule are present. It is a protein complex composed of four peptide chains — two identical heavy chains and two identical light chains arranged in a Y-shape typical of antibody monomers. Each IgG has two antigen binding sites. Representing approximately 75% of serum immunoglobulins in humans, IgG is the most abundant antibody isotype found in the circulation. IgG molecules are synthesized and secreted by plasma B cells. Secondary Antibodies are available in a variety of formats and conjugate types. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition.

Anti-Mouse IgG1 ATTO 647N Antibody generated in goat detects reactivity to Mouse IgG1 (Gamma 1 chain). Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. IgG1 chain constitutes 66% of the IgG subclass and has a high affinity for binding to the Fc receptor of phagocytic cells. Secondary Antibodies are available in a variety of formats and conjugate types. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source and fragment composition.

Anti-Rabbit IgG (H&L) ATTO 647N Antibody generated in goat detects reactivity to Rabbit IgG. Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. The whole IgG molecule possesses both the F(c) region, recognized by high-affinity Fc receptor proteins, as well as the F(ab) region possessing the epitope-recognition site. Both the Heavy and Light chains of the antibody molecule are present. Secondary Antibodies are available in a variety of formats and conjugate types. When choosing a secondary antibody product, consideration must be given to species and immunoglobulin specificity, conjugate type, fragment and chain specificity, level of cross-reactivity, and host-species source

Camelids produce functional IgG isotypes that do not incorporate light chains. Comparative studies of old world camelids (Camelus bactrianus and Camelus dromedarius) and new world camelids (Lama pacos, Lama glama and Lama vicugna) have shown that heavy-chain-only immunoglobulins represent between 35% - 70% of total IgG in the sera of all species. At present, three subclasses of camelid IgG have been identified (IgG1, IgG2, IgG3), of which IgG2 and IgG3 lack the light chains. IgG1 binds strongly to protein A and G, is composed of conventional antibodies, and totals 25 % of serum IgG. Llama IgG1 antibodies migrate as a 150-kDa protein in SDS-polyacrylamide gel under non-reducing conditions. Under reducing conditions, IgG1 antibodies split into four proteins (two of each H- and L-chains), which gives protein bands of about 52-55 kDa (H-chain) and about 27 kDa (L-chain). Anti-Llama IgG1 generated in rabbit detects specifically the Llama IgG1 isotype. This anti-Llama secondary Antibody is s

Purified Anti-PtdIns(3)P monoclonal antibody.Subclass: IgG2aSource: MouseApplications: ELISA Immunofluorescence Alphascreen Fluorescence PolarizationPhosphoinositides (PIPns) are minor components of cellular membranes but are integral signaling molecules for cellular communication. Phosphatidylinositol 3-phosphate (PI(3)P) is enriched in early endosomes having roles in endosome fusion and receptor sorting and internalization in multivesicular bodies. PI(3)P has also been found at the plasma membrane and is involved in the translocation of the glucose transport protein GLUT4. Powered by Bioz See more details on BiozFeatured in Publications1) Nobukuni T. M. Joaquin et al. (2005). "Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase." Proc Natl Acad Sci U S A 102(40): 14238-43.2) Dowling J. J. A. P. Vreede et al. (2009). "Loss of myotubularin function results in T-tubule disorganization in zebrafish and human myotubular myopathy

Purified Anti-PtdIns(4)P monoclonal antibody.Subclass: IgMSource: MouseApplications: ELISA Immunofluorescence Fluorescence Polarization Protein-Lipid Overlay (PIP Strip)Phosphoinositides (PIPns) are minor components of cellular membranes but are integral signaling molecules for cellular communication. Phosphatidylinositol 4-phosphate (PI(4)P) is the biosynthetic precursor to PI(4 5)P2 and has an important roles in regulating sphingomyelin and glycosphingolipid metabolism and membrane trafficking at the exit of the Golgi complex. Powered by Bioz See more details on BiozFeatured in Publications1) Weber S. S. C. Ragaz et al. (2006). "Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole." PLoS Pathog 2(5): e46.2) Blagoveshchenskaya A. F. Y. Cheong et al. (2008). "Integration of Golgi trafficking and growth factor signaling by the lipid phosphatase SAC1." J Cell Biol 180(4): 803-12.3) Cheong F. Y. V. Sharma et al. (2010). "Spatia

Purified Anti-PtdIns(4 5)P2 (2C11) monoclonal antibody.Subclass: IgMSource: MouseApplications: ELISA Immunofluorescence Protein-Lipid Overlay (PIP Strip)Clonality: Monoclonal 2C11Phosphoinositides (PIPns) are minor components of cellular membranes but are integral signaling molecules for cellular communication. Phosphatidylinositol 4 5-bisphosphate (PIP2) has been shown to play a central role in a variety of cellular functions. Amongst its many functions PIP2 is a substrate for Phospholipase C-coupled G-protein pathways involved in intracellular calcium release in a number of tissues. It is also a substrate for class I phosphoinositide 3-kinase (PI3-K) forming PIP3. Powered by Bioz See more details on BiozProduct keywords: PIP2 PI(4 5)P2 PtdIns(4 5)P2 IgM anti-PIP2

Purified Anti-Sphingosine 1-Phosphate (S1P) monoclonal antibody.Subclass: IgGk1Source: MouseApplications: ELISA Immunohistochemistry ImmunocytochemistrySphingosine 1-Phosphate (S1P) is a key component of the sphingolipid signaling cascade. S1P initiates a proliferative pro-angiogenic and anti-apoptotic sequence of events contributing to cancer progression. Recently scientific literature has suggested that S1P is a potent tumorigenic growth factor that is likely released from tumor cells and that S1P may be a novel biomarker for early stage cancer detection. Sphingosine kinase has also been shown to be up-regulated in a variety of cancer types. S1P antibody (LT1002) was originally developed and patented at Lpath Therapeutics. Powered by Bioz See more details on BiozSelected Publications1) Visentin B Reynolds G Sabbadini R. (2012) Immunohistochemical detection of sphingosine-1-phosphate and sphingosine kinase-1 in human tissue samples. Methods Mol Biol. 874:55-67.2) O'Brien N Jone