Shop

Description

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ‘beads on a string’ structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into RNA. Research focus area: Epigenetics.

Key Applications:
-Western Blotting
-Immunocytochemistry
-ChIP-seq
-Chromatin Immunoprecipitation (ChIP)

Description

Actin is an abundant cytoskeletal protein found in all cells (True, 1990). The protein’s 42 kD peptide chain assumes two physical forms: globular actin, which may serve as a cytoplasmic storage pool, and fibrous actin, which, in conjunction with myosin, generates muscle contraction (True, 1990). In non-muscle cells, actin appears to be involved in a variety of functions, such as cell motility, exocytosis, and phagocytosis (True, 1990). Distribution of the six known isoforms of actin – four muscle actins (alpha-skeletal, alpha-vascular smooth, alpha-cardiac, and gamma-enteric smooth) and two cytoplasmic actins (alpha and gamma) is tissue specific (Otey, 1986; Lessard, 1988). Research focus area: Cell Structure

Key Application:
-ELISA
-Immunocytochemistry
-Immunofluorescence
-Immunohistochemistry
-Immunohistochemistry (Paraffin)
-Western Blotting

Description

Glutamate receptors (GluRs) can be categorized as ionotropic or metabotropic and subcatergorized by their agonist preferences (NMDA, AMPA or Kainic acid). There are four types of AMPA selective GluR subunits (GluR1, GluR2, GluR3 and GluR4). Tetrameric or pentameric combinations of different subunits contributes to the functional diversity of AMPA receptors. In general, AMPA receptors mediate fast synaptic current at most excitatory synapses, with stoichiometry characterized by subtype composition. Although subunit composition of AMPA receptors varies, they must contain at least one edited GluR2 subunit to be calcium impermeable. The critical residue controlling calcium permeability is in the pore loop region. In GluR1, GluR3, and GluR4, this positionis occupied by a Gln residue. In GluR2, it is occupied by an Arg residue. It has been shown experimentally that the presence of Arg in this position blocks CA2+ ion permeability, while a Gln does not. Relative calcium permeability in AMPA receptor channels may be significant in pathological neurotoxic damage and long term changes in nervous system responses. Research focus area: Neuroscience

Key Applications:
-ELISA
-Immunocytochemistry
-Immunohistochemistry
-Immunoprecipitation
-Radioimmunoassay
-Western Blotting

Description

IRS1 (Insulin Receptor Substrate 1) transmits insulin signals via metabolic and mitogenic pathways. IRS1 is heavily phosphorylated on both serine and tyrosine residues. These phosphorylated tyrosines enable IRS to act as a docking protein that binds SH2 domains of such proteins as PI3 Kinase (phosphatidylinositol 3-kinase) and GRB2, resulting in activation. Over expression and phosphorylation of serine is associated with insulin resistance and breast cancer. Some of the more notable phosphorylation sites are Ser302 that is phosphorylated following insulin stimulation. Ser307, phosphorylated by JNK and IKK, is a key regulatory site that appears to disrupt the IRS1/IR interaction and inhibits insulin-mediated activation of the PI3 kinase and MAPK pathways, and Ser636/639 that is known to be phosphorylated by p70S6K downstream of mTOR and acts as a negative feedback loop. Research focus area: Signaling

Key Applications:
-Western Blotting
-Immunoprecipitation
-Immunocytochemistry

Description

p62 is also known as sequestosome-1, and is a 62 kDa ras-GAP associated protein. p62 is thought to bind to src-family tyrosine kinases and may also provide a linker action for activated src-family kinases with their downstream effectors. p62 has an RNA-binding region and may have RNA-binding ability. p62 is associated with activation of transcription factor NF-κB, involved in cell differentiation, immune response and potassium channel regulation. p62 has recently been linked to extrinsic apoptosis and may be a key player in tumorigenesis. Research focus area: Cancer.

Key Applications:
-Western Blotting
-Flow Cytometry
-Immunocytochemistry

Description

Histone H2A.X is a variant of histone H2A, and is similarly associated with genomic DNA. However, histone is structurally different from other members of the H2A family in possessing a C-terminal tail that contains the Ser139 residue that is phosphorylated in response to breaks in double-stranded DNA. The phosphorylation of H2A.X is a rapid process that is mediated by ATM/ATR proteins.

Description

As a member of the histone H2A family, histone H2A.x (H2A.x) is a variant histone H2A which replaces conventional H2A in a subset of nucleosomes. H2A.x is involved in the DNA repair of double-strand breakage (DSB) damage on nuclear DNA. After a double strand DNA break, H2A.x is rapidly phosphorylated at serine 139 by ATM kinase and becomes gamma-H2AFX. This phosphorylation step can extend up to several thousand nucleosomes from the actual site of the DSB and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. As a part of posttranslational modifications during apoptosis caused by severe DNA damage, high expression of phosphorylated H2A.x is considered as an accurate indicator of apoptosis.

Description

Histone H2A is one of the 5 main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail H2A is involved with the structure of the nucleosomes of the ‘beads on a string’ structure

** This product has been discontinued, please contact us for more information.

Description

Myosin phosphatase target subunit 1 (MYPT1), also called Myosin-binding subunit of Myosin phosphatase, is one of the subunits and an integral component of the Myosin phosphatase. Myosin phosphatase regulates the interaction of Actin and Myosin downstream of the guanosine triphosphatase Rho, which inhibits Myosin phosphatase through the action of Rho-kinase. It is also involved in smooth muscle contraction. Inhibition of Myosin light chain phosphatase results in Ca2+ sensitization of smooth muscle contraction. This inhibition is modulated through phosphorylation of MYPT1 by a ZIP-like kinase, which associates with MYPTI and phosphorylates the inhibitory site in smooth muscle. The phosphorylation of MYPT1 by protein kinase C results in altered dephosphoryation of Myosin by attenuating the binding of protein phosphatase 1 catalytic subunit (PP1c) and the phosphorylated 20 kDa Myosin light chain to MYPT1. PP1c interacts with at least four binding sites on the amino-terminus of MYPT1. MYPT1 is localized on stress fibers, and is distributed close to the cell membrane and at cell-cell contacts to regulate Myosin phosphatase activity.