recombinant-proteins

FLAG peptide, an eight-amino-acid sequence (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys), includes an enterokinase-cleavage site and is utilized for the purification of recombinant proteins.

L-Norvaline is an arginase inhibitor and a non-protein branched-chain amino acid. L-Norvaline has previously been reported as a natural component of the antifungal peptide of Bacillus subtilis. L-Norvaline and other modified branched-chain amino acids have received attention in recent studies because they appear to be incorporated into some recombinant proteins found in E. coli.

Beclabuvir is an allosteric inhibitor that binds to thumb site 1 of the HCV NS5B RNA-dependent RNA polymerase, inhibiting recombinant NS5B proteins from HCV genotypes 1, 3, 4, and 5 (IC50 < 28 nM).

BAY-524 is an inhibitor of Bub1(IC50 = 450 nM.human Bub1 in the presence of 2 mM ATP).

CP-609754 (LNK-754) is a potent and reversible farnesyltransferase inhibitor with potential anticancer activity. It inhibits farnesylation of recombinant human H-Ras (IC50=0.57 ng/mL) and K-Ras (IC50=46 ng/mL)[1]. In 3T3 H-ras (61L)-transfected cell lines, CP-609754 exhibits a slow on/off rate, inhibiting mutant H-Ras farnesylation with an IC50 of 1.72 ng/mL[1]. The compound is competitive for the prenyl acceptor (H-Ras protein) and noncompetitive for the prenyl donor farnesyl PPI, selectively inhibiting farnesylation of both H- and K-Ras proteins in 3T3 transfectants[1]. In vivo, CP-609754 shows antitumor activity against 3T3 H-ras (61L) tumors, with tumor regression achieved at 100 mg/kg twice daily and an ED50 for tumor growth inhibition at 28 mg/kg[1]. Continuous i.p. infusion of CP-609754 inhibits tumor growth by over 50% and reduces tumor farnesyltransferase activity by over 30% when plasma concentration is maintained above 118 ng/mL[1]. [1]. Stacy L Moulder, et al. A phase I open label study of the farnesyltransferase inhibitor CP-609,754 in patients with advanced malignant tumors. Clin Cancer Res. 2004 Nov 1;10(21):7127-35.

Beclabuvir, also known as BMS-791325, is an allosteric inhibitor that binds to thumb site 1 of the hepatitis C virus (HCV) NS5B RNA-dependent RNA polymerase. BMS-791325 inhibits recombinant NS5B proteins from HCV genotypes 1, 3, 4, and 5 at 50% inhibitory concentrations (IC50) below 28 nM. In cell culture, BMS-791325 inhibited replication of HCV subgenomic replicons representing genotypes 1a and 1b at 50% effective concentrations (EC50s) of 3 nM and 6 nM, respectively, with similar (3 to 18 nM) values for genotypes 3a, 4a, and 5a. B

AF3442 is a potent and selective mPGES-1 inhibitor (microsomal prostaglandin (PG) E synthase-1). AF3442 caused a concentration-dependent inhibition of PGE(2) in human recombinant mPGES-1 with an IC(50) of 0.06microM. AF3442 is a selective mPGES-1 inhibitor which reduced monocyte PGE(2) generation also in the presence of plasma proteins. Pharmacological inhibition of mPGES-1 did not translate into redirection of PGH(2) metabolism towards other terminal PG synthases in monocytes. The functional relevance of this observation deserves to be investigated in vivo.

Benastatin B is a polyketide synthase-derived benastatin that has been found in Streptomyces and has diverse biological activities. It inhibits glutathione S-transferase (GST; Ki = 3.7 µM for the rat liver enzyme).2 Benastatin B also inhibits the transglycosylase activity of A. baumannii, C. difficile, E. coli, and S. aureus recombinant penicillin-binding proteins (PBPs; IC50s = 16, 53.3, 30.7, and 31.6 µM, respectively).3 It is active against several bacteria, including methicillin-resistant S. aureus (MRSA; MIC = 3.12 µg/ml).

Recombinant Proteinase K, a serine protease, targets the carboxy-terminal peptide bonds of both aliphatic and aromatic amino acids. It is utilized to digest proteins and eradicate contamination in nucleic acid preparations [1].

GTPγS tetralithium (Guanosine 5'-[γ-thio]triphosphate tetralithium) is a G-protein activator, a non-hydrolyzable GTP analog that protects proteins from proteolytic degradation.GTPγS tetralithium is involved in the detection of cells expressing recombinant receptors and endogenous receptors. GTPγS tetralithium is involved in the detection of GPCR signaling in cells expressing recombinant receptors as well as in cells and tissues expressing endogenous receptors, and can be assayed to measure agonist-induced desensitization of two human polymorphic α2B-adrenoceptor variants.

Perforin-IN-2, a benzosulfonamide perforin inhibitor, mitigates transplant rejection in allogeneic bone marrow or stem cell transplantation. It binds to plasma proteins with a binding rate of 99.8%. In vivo, a concentration higher than 900 μM is required for optimal perforin inhibition. Perforin-IN-2 effectively inhibits the lytic activity of recombinant perforin on Jurkat T leukemia cells, with an IC50 of 6.65 μM, and also prevents the death of K562 leukemia target cells [1].

AC Antibody Purification Resin 2 is composed of spherical, highly cross-linked agarose beads characterized by a narrow size distribution and strong mechanical stability. It is utilized for the separation and purification of complex antibodies such as monoclonal, bispecific, and polyclonal antibodies as well as Fc fusion proteins. [Substrate: Highly cross-linked agarose microspheres; Particle size: 65μm; Ligand: Alkali-resistant recombinant Protein A; ADC Purification Resin.]

Azido-PEG3-DYKDDDDK (azide-PEG3-FLAG) TFA serves as a multifunctional fusion tag for the purification of recombinant proteins. This click chemistry reagent comprises an azide group, enabling it to undergo copper-catalyzed azide-alkyne cycloaddition (CuAAC) with alkyne-containing molecules. Additionally, it can participate in strain-promoted alkyne-azide cycloaddition (SPAAC) with molecules that possess DBCO or BCN groups.

FLAG peptide TFA is the trifluoroacetate (TFA) salt form of FLAG peptide. It serves as a versatile fusion tag for the purification of recombinant proteins. FLAG peptide TFA allows its fusion proteins to maintain their natural folding. It can be removed by enterokinase and eluted under non-denaturing conditions.

The StrepII tag is a short peptide tag used for the purification and detection of recombinant proteins.

Strep-tag peptide is a short peptide affinity tag with an inherent binding affinity for streptavidin, commonly utilized as an affinity tag for recombinant proteins.

HRV 3C Protease is a human rhinovirus-derived protease that recognizes the LEVLFQGP sequence and cleaves precisely between the Q and G residues, enabling efficient removal of affinity tags from recombinant proteins, HRV 3C Protease is widely employed in structural biology, protein purification workflows, and enzymology research.

Collagenase H Recombinant effectively digests and breaks down collagen proteins within the extracellular matrix (ECM), particularly collagen III. It plays a crucial role in the isolation and function of rat islets. Additionally, Collagenase H Recombinant is applicable in tissue engineering and cell culture.

Recombinant Trypsin is a serine protease that hydrolyzes proteins at the carboxyl side of lysine or arginine.

18:1 DGS-NTA(Ni) is a nickel-chelating lipid. It exhibits high affinity for histidine tags and can bind to the histidine tags on recombinant proteins. This compound is useful in the preparation of liposomes and nanomultilamellar vesicles (NMV), which are employed in studies of protein and peptide binding as well as for antigen delivery.