Other Proteins

Human CD34 (P28906, 32 a.a. - 290 a.a.) partial recombinant protein with His tag at C-terminus expressed in Sf9 cells.

GenScript Ni Resin FF is a 6% highly cross-linked agarose medium covalently coupled to a chelating agent that binds Ni2+ by three coordination sites for high-affinity purification of polyhistidine-tagged recombinant proteins.

STING (stimulator of interferon genes), also known as TMEM173 (transmembrane protein 173), is a crucial protein in innate immunity. It is a membrane protein involved in the response to foreign DNA in hematopoietic lineage cells, such as NK and T cells, myeloid cells, and monocytes. It is also found in the retina, heart, and other tissues. STING gets activated by DNA sensors and triggers IFN (type I interferon) production, by stimulating TBK1, which then phosphorylates STAT6 (signal transducer and activator of transcription 6) or IRF3 (interferon regulatory factor 3). These in turn activate the expression of genes linked to immune responses. It can also function as a DNA sensor, by binding directly to the cyclic di-GMP. More recently STING€™s role in controlling ROS (reactive oxygen species) formation and that loss of STING reduces DNA damage have been identified. The development the STING agonist that be beneficial in combinatory cancer therapy.

Diablo (direct IAP binding protein with low pI), also named SMAC (second mitochondria-derived activator of caspases), is a ubiquitously expressed mitochondrial protein involved in apoptosis. Under normal conditions this protein is found in the intermembrane space of the mitochondria. However, when a cell undergoes apoptosis, the mitochondrial membrane becomes porous and Diablo moves the cytosol. Once in the cytosol it can bind and inhibit IAPs (inhibitor of apoptosis protein) proteins, allowing caspase activation. This protein has been linked to cancer, and overexpression of Diablo may sensitize cancer cells to apoptosis. The use of Diablo mimetics, alone or in combination with other therapeutical approaches, is a promising cancer therapy.

Covalent conjugation to ubiquitin (Ub) is one of the major post-translational modifications that regulates protein stability, function, and localization. Ubiquitination is the concerted action of three enzymes: a Ub-activating enzyme (E1),a Ub-conjugating enzyme (E2), and a Ub ligase (E3). The specificity and efficiency of ubiquitination are largely determined by the E3 enzyme, which directs the last step of the Ub-conjugating cascade by binding to both an E2ˆ¼Ub conjugate and a substrate protein. This step ensures the transfer of Ub from E2ˆ¼Ub to the substrate, leading to its mono- or poly-ubiquitination. CulL1, or cullin 1, is part of an E3 ligase complex, the SCF (SKP1 (s-phase kinase associated protein 1)- Cul1- F-box protein) complex, that also involves Skp2 and Rbx1 (RING-box protein 1). The SCF complex is involved in the ubiquitination of proteins that act on cell cycle, signal transduction and transcription, with Cul1 serving as a structural scaffold. Cullins can b

Covalent conjugation to ubiquitin (Ub) is one of the major post-translational modifications that regulates protein stability, function, and localization. Ubiquitination is the concerted action of three enzymes: a Ub-activating enzyme (E1),a Ub-conjugating enzyme (E2), and a Ub ligase (E3). The specificity and efficiency of ubiquitination are largely determined by the E3 enzyme, which directs the last step of the Ub-conjugating cascade by binding to both an E2ˆ¼Ub conjugate and a substrate protein. This step ensures the transfer of Ub from E2ˆ¼Ub to the substrate, leading to its mono- or poly-ubiquitination. CulL1, or cullin 1, is part of an E3 ligase complex, the SCF (SKP1 (s-phase kinase associated protein 1)- Cul1- F-box protein) complex, that also involves Skp2 and Rbx1 (RING-box protein 1). The SCF complex is involved in the ubiquitination of proteins that act on cell cycle, signal transduction and transcription, with Cul1 serving as a structural scaffold. Cullins can b

FGFR1 (fibroblast growth factor receptor 1), also known as FLT2, is a member of the FGFR family, a family of four membrane-spanning tyrosine kinases (FGFR1-4) which serve as high-affinity receptors for 17 growth factors (FGF1-17). The FGF Receptor family plays an important role in multiple biological processes, including mesoderm induction and patterning, cell growth and migration, organ formation and bone growth. FGFR1 is alternatively spliced generating multiple splice variants that are differentially expressed during embryo development and in the adult body. It undergoes splicing on the IgIII domain, the domain involved in ligand specificity, creating two alternative forms: IIIb and IIIc. FGFR1a (IIIc) can bind to FGF1, 2, 4, 5, 6, 19, 20, and 21. FGFR proteins are tightly regulated, being usually ubiquitinated by CBL (Cbl proto-oncogene E3 ubiquitin protein ligase) after activation, with FGFR1 being more susceptible to undergo ubiquitination. FGFR1 has been linked to breast, ovaria

CD8 is a co-receptor for the TCR (T cell receptor) in T cells, binding to MHC (major histocompatibility complex) class I proteins. CD8 is a typical marker of cytotoxic T cells and is involved in T cell signaling. CD8 has two isoforms, a and b. CD8b recruits Lck (lymphocyte-specific protein tyrosine kinase) to the TCR-CD3 complex, and Lck phosphorylates multiple proteins involved in activation of cytotoxic T-lymphocytes. It is thus critical for the lysis of cancer cells.