BioVision, Inc., products

Polyclonal Antibody to detect 14-3-3 in Human, Mouse, Rat, pig, monkey, rabbit, dog, sheep and bovine samples. The 14-3-3 proteins comprise a family of highly conserved acidic proteins which play a role in both signal transduction and the cell cycle by binding to and regulating several different proteins. The family of proteins is present in particularly high concentrations in mammalian brain and may be involved in the regulation of neuronal activity. The 14-3-3 proteins exist as either homo- or heterodimers which interact via their N-terminal domains and are subject to phosphorylation by protein kinase C.

Human 4-1BB Ligand (4-1BBL) is a member of the emerging family of Ligands with structural homology to tumor necrosis factor. Human 4-1BBL is a 19.5 kDa protein containing 185 amino acid residues, comprising the TNF-like extra-cellular domain of 4-1BBL.

Human 4-1BB Receptor (4-1BBR) is an inhibitor of 4-1BBL and can block 4-1BBL bioactivity. Human 4-1BBR is a 17.7 kDa protein containing 167 amino acid residues.

A retinoid X receptors (RXRs) activator. Phytol is a diterpene alcohol commonly used as an aromatic ingredient in many fragrance compounds. Phytol and its metabolites have been reported to activate retinoid X receptors (RXRs) and to promote the activity of (peroxisome proliferator-activated receptor) PPAR/RXR heterodimers. Some of its lipophilic analogs show potent antitubercular activity.

Cas9 (CRISPR associated protein 9) is an RNA-guided DNA endonuclease enzyme associated with the CRISPR (Clustered Regularly Interspersed Palindromic Repeats) adaptive immunity system in Streptococcus pyogenes and other bacteria. Cas9 is used to interrogate and cleave foreign DNA, such as invading bacteriophage DNA or plasmid DNA. This is accomplished by unwinding foreign DNA and checking for if it is complementary to the 20 base pair spacer region of the guide RNA. If the DNA substrate is complementary to the guide RNA, Cas9 cleaves the invading DNA.

The Blue Fluorescent Protein (BFP) can be used as protein marker to study subcellular localization or translocation of proteins.

Green fluorescent protein (GFP) is a spontaneously fluorescent protein isolated from pacific jellyfish, Aequorea victoria. It transduces the blue chemiluminescence into green fluorescent light. Since the molecular cloning of GFP cDNA and demonstration of GFP as a functional transgene, GFP has become a powerful tool with exciting applications in developmental, cell and molecular biology. GFP fluorescence is not species specific and can be expressed in bacteria, yeast, plant and mammalian cells. GFP can fuse with proteins of interest without interfering significantly with their assembly and function.