Rockland produces highly active antibodies and conjugates to collagens. Collagens are highly conserved throughout evolution and are characterized by an uninterrupted ''Glycine-X-Y'' triplet repeat that is a necessary part of the triple helical structure. For these reasons, it is often extremely difficult to generate antibodies with specificities to collagens. The development of ‘type’ specific antibodies is dependent on NON-DENATURED three-dimensional epitopes. Rockland extensively purifies collagens for immunization from human and bovine placenta and cartilage by limited pepsin digestion and selective salt precipitation. This preparation results in a native conformation of the protein. Antibodies are isolated from rabbit antiserum and are extensively cross-adsorbed by immunoaffinity purification to produce 'type' specific antibodies. Greatly diminished reactivity and selectivity of these antibodies will result if denaturing and reducing conditions are used for SDS-PAGE and immunoblott

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

Goat Serum blocking reagent or NGS can be used as a blocking agent to treat plastic surfaces, membrane or tissue after they have been sensitized with primary antibody or antigen. It provides an alternative to bovine serum albumin (BSA) and non-fat dry milk. It is effective in reducing nonspecific binding of proteins to reaction surfaces, thereby maximizing signal-to-noise ratio. This blocking agent is recommended for use in immunoassays where the primary antibody was produced in goat, as a source of non-specific serum protein or on tissue for immunohistochemical applications.

Bovine Serum Albumin (BSA) is used for various biochemical applications including ELISA (Enzyme-Linked Immunosorbent Assay), high content screening assays, western blotting, FACS Buffer and immunohistochemistry. BSA as a blocking reagent is particularly useful with casein-sensitive antibodies, such as phospho-specific antibodies. Also used as a nutrient in cell and microbial culture. In restriction digests, BSA is used to stabilize some enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes and other vessels. Bovine Serum Albumin can also be used to determine the quantity of other proteins, by comparing an unknown quantity of protein to known amounts of BSA.

Mouse Plasma is used as a component of bioassays, immunoassays or enzyme assays. Mouse Plasma provides a broad spectrum of macromolecules, carrier proteins for lipoid substances and trace elements, attachment and spreading factors, low molecular weight nutrients, and hormones and growth factors that promote cell growth and health. Mouse Plasma is also available as a sterile preparation for use as a cell culture supplement.