Proteins & Peptides

HbA-2 or HbD peptide corresponds the delta-subunit specific sequence in the hemoglobin delta-subunit found in HbA-2. Functional hemoglobin (Hb) is a hetero tetramer and the dominant form of Adult Hb is composed of 2 alpha and 2 beta subunits (α2β2). Hemoglobin A-2 (HbA-2) is a normal but minor variant of hemoglobin A that consists of two alpha and two delta chains (α2δ2). Hemoglobin A-2 may be increased in beta thalassemia or in people who are heterozygous for the beta thalassemia gene, and HbA2 is also linked to neurological disorders. HbA-2 form exists in small amounts in all adult humans (1.5-3.1% of all hemoglobin molecules) and is increased in people with Sickle-cell disease. Its normal biological role is not well understood. HbD peptide is suitable for use as a control with HbA-2 antibody. This peptide is ideal for investigators involved in Cardiovascular and developmental biology research.

Host Cell Protein Lysate was prepared by solubilizing mock induced E. coli cells. Host Cell Proteins are process-related impurities derived from a host cell expression system that may be present in trace amounts in a final drug substance. HCP Antibodies are used to detect impurities in biologically-based therapeutics. Detecting impurities often unseen by 1-D electrophoresis, a 2D electrophoresis western blot analysis delivers more complete insight into the immunocoverage of protein components of the host cell lysate.

AKT2 peptide detects AKT2 which is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and rac (related to A and C kinases). AKT is a key regulator of many signal transduction pathways. AKT Exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation.

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3

The nucleosome is comprised of 146 bp of DNA wrapped around a series of histone proteins arranged as an octamer consisting of 2 copies of histone H2A, H2B, H3 and H4. Within the nucleosome core the histone proteins are covalent modified at specific residues predominantly within the N-terminal tail including lysine (acetylation, methylation, SUMOylation, and ubiquitinylation), arginine methylation and citrullination, serine and threonine phosphorylation, as well as proline isomerization. The lysine side chains can carry up to three methyl groups (mono-, di- and tri- methylated forms) and the arginine side chain can be monomethylated or can be dimethylated as the symmetric or asymmetric forms. The modifications show temporal, disease-specific, and other types of cell-specific regulation and there are specific families of enzymes that regulate the methylation, demethylation, acetylation, deacetylation and other modifications. Research has indicated that whereas the histone mark H3K4Me3