NIRF (Np95/ICBP90-like RING finger protein), also known as E3 ubiquitin-protein ligase UHRF2, Nuclear zinc finger protein Np97 or RING finger protein 107, is a nuclear protein involved in cell cycle regulation. NIRF contains a PHD finger, two RING fingers, a ubiquitin-like domain and a YDG/SRA domain. It shares high structural homology with UHRF1 (also called ICBP90 in humans and Np95 in mice), however, in contrast to UHRF1, NIRF acts as a negative regulator of cell proliferation. It associates with the Cdk2-cyclin complex in its dephosphorylated form and induces G1 arrest. NIRF plays an important role in the regulation of the G1/S transition by blocking cell entry into the S-phase. While associated with Cdk2, NIRF becomes phosphorylated. NIRF can also act as a ubiquitin ligase and it ubiquitinates PCNP. In addition, NIRF can recruit and bind HDAC1 via its SRA domain. The overexpression of NIRF results in an increase of G1 phase cells. (Shipping Cost: €200.00)

Complement C3 Polyclonal

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. Acylation stimulating protein (ASP): adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2.

Complement C3 Polyclonal