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Monkey Spermatid Differentiation

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Bax is a key component for cellular induced apoptosis through mitochondrial stress (1). Upon apoptotic stimulation, Bax forms oligomers and translocates from the cytosol to the mitochondrial membrane (2). Through interactions with pore proteins on the mitochondrial membrane, Bax increases the membrane's permeability, which leads to the release of cytochrome c from mitochondria, activation of caspase-9 and initiation of the caspase activation pathway for apoptosis (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Bax is a key component for cellular induced apoptosis through mitochondrial stress (1). Upon apoptotic stimulation, Bax forms oligomers and translocates from the cytosol to the mitochondrial membrane (2). Through interactions with pore proteins on the mitochondrial membrane, Bax increases the membrane's permeability, which leads to the release of cytochrome c from mitochondria, activation of caspase-9 and initiation of the caspase activation pathway for apoptosis (3,4).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Nectin-2, also known as CD112 and poliovirus receptor-related 2 (PVRL2), is a single-pass type I membrane glycoprotein ubiquitously expressed on various human tissues (1). It is a calcium independent cell adhesion molecule known to interact with several cell surface receptors, including DNAM-1 (CD226), LFA-1 (CD11a), Nectin-3 (CD113), TIGIT (VSTM3), and PVRIG (CD112R) (2-7). It is one of the major constituents of adherins junctions, and therefore plays a central role in a number of cellular processes, including adhesion, migration, and proliferation (2-8). Within the immune system, Nectin-2 modulates immune cell signaling. Upon interaction with DNAM-1 expressed on T and NK cells, Nectin-2 stimulates proliferation and cytokine production (4). Upon interaction with PVRIG, Nectin-2 inhibits proliferation (7). Thus, Nectin-2 can be either a co-stimulator or a co-inhibitor of immune cell function depending on competitive receptor interactions. Nectin-2 also serves as an entry for certain mutant strains of herpes simplex virus and pseudorabies virus, and it is involved in cell to cell spreading of these viruses (8,9). Alternate transcriptional splice variants, encoding different isoforms, have been characterized (10,11).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: High mobility group protein B2 (HMGB2) belongs to a family of highly conserved proteins that contain HMG box domains (1,2). All three family members (HMGB1, HMGB2, and HMGB3) contain two HMG box domains and a C-terminal acidic domain. HMGB1 is a widely expressed and highly abundant protein (2). HMGB2 is widely expressed during embryonic development, but it is restricted to lymphoid organs and testis in adult animals (3). HMGB3 is only expressed during embryogenesis (4). While expression varies, the biochemical properties of the different family members may be indistinguishable. The HMG box domains facilitate the binding of HMGB proteins to the minor groove of DNA, which results in local bending of the DNA double helix (1,2). HMGB proteins are recruited by and help facilitate the assembly of site-specific DNA binding proteins to their cognate binding sites in chromatin. For example, HMGB1 and HMGB2 facilitate the binding of Hox proteins, Oct proteins, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters (1,2). Furthermore, HMGB2 interacts with RAG1 to facilitate RAG complex binding to the recombinant signal sequence (RSS) and stimulate DNA-bending and subsequent VDJ cleavage at antigen receptor genes (5,6). In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation. HMGB2 is secreted by myeloid cells and promotes proliferation and migration of endothelial cells by binding to the receptor for advanced glycation endproducts (RAGE) (7). Research studies have shown that HMGB2 overexpression in hepatocellular carcinoma is associated with poor prognosis and shorter survival time (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Quaking (QKI) is a member of the signal transduction and activator of RNA (STAR) protein family of RNA binding proteins (1,2). Mutations in the mouse Qki locus results in impaired myelin formation resulting in tremors (3). QKI proteins exist as homodimers, and disruption of the dimerization process is lethal in mice (2). QKI exists in different isoforms that differ in their C-terminus, resulting in unique subcellular localizations (4). The nuclear isoform of QKI, QKI-5, is involved in regulation of alternative splicing of MAG mRNA, which encodes for a protein important for myelin sheath formation and maintenance (4,5). QKI has also been implicated in schizophrenia and oligodendrocyte differentiation (6). QKI can function as a tumor suppressor, as it is regulated by p53 to stabilize miRNAs that regulate TGF-Β signaling (7).