protease

Expression system: E. coli
Length: 1-204, Full Length
Activity: Not Tested

Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria.

Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in the blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. The mucosal mast cell (MMC) granule-specific beta-chymase, mouse mast cell protease-1 (mMCP-1), is released systemically into the bloodstream early in nematode infection before parasite-specific IgE responses develop and TGF-beta1 induces the constitutive release of mMCP-1 by homologs of MMC in vitro. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (L50F, E166V), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.80 kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (S144A), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.78 kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (L50F), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.8kDa and the accession number is YP_009725301.1.

SUMO protease, also known as Ulp, is a highly specific enzyme that removes small ubiquitin-like modifier (SUMO) from recombinant SUMO fusion proteins. Unlike proteases such as enterokinase or TEV, which recognize linear amino acid sequences, SUMO protease recognizes the native tertiary structure of SUMO, allowing precise cleavage without leaving extra residues at the cleavage site. This recombinant SUMO protease is derived from Saccharomyces cerevisiae, expressed in E. coli, and purified to obtain high yields of active enzyme under animal-free conditions. It is well suited for applications in drug and vaccine development, protein manufacturing, and other research uses. A C-terminal 6×His tag is included to enable easy removal of the protease following cleavage via Ni²⁺ affinity purification.

The viral main proteinase (M pro , also called 3CL pro ), which controls the activities of the coronavirus replication complex. It functions as a cysteine protease engaging in the proteolytic cleavage of the viral precursor polyprotein to a series of functional proteins required for coronavirus replication and is considered as an appealing target for designing anti-SARS agents. 3CLpro 3C-like Protease Protein, SARS-CoV-2, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 33 KDa and the accession number is P0DTC1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (Q189K), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.79 kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (H172Y), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.82 kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (F140A), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.72 kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (P132H), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 33.8 kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (L50F, E166A, L167F), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 34.5 kDa and the accession number is YP_009725301.1.

Expression system: E. coli
Length: 26-340, Partial
Activity: Not Tested

Expression system: E. coli
Length: 71-398, Full Length of Mature Protein
Activity: Not Tested

3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site. SARS-CoV-2 3CLpro 3C-like protease Protein (His & Avi) is expressed in E. coli expression system. The predicted molecular weight is 36.57 kDa and the accession number is YP_009725295.1.

3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site. SARS-CoV-2 3CLpro 3C-like protease Protein (His) is expressed in Baculovirus insect cells. The predicted molecular weight is 35.31 kDa and the accession number is YP_009725295.1.

HCV NS3 displays three enzymatic activities: serine protease, NTPase, and RNA helicase. HCV NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A, and NS5A-NS5B. HCV NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand (By similarity). Cleaves and inhibits the host antiviral protein MAVS. NS3 NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. One of the HCV proteases, NS3-4A serine protease, is a non-covalent heterodimer consisting of a catalytic subunit (the N-terminal one-third of NS3 protein) and an activating cofactor (NS4A protein) and is responsible for cleavage at four sites of the HCV polyprotein.

APP Protease nexin-II Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 101 kDa and the accession number is P05067-8.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein (L167F), SARS-COV-2, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 34.5kDa and the accession number is YP_009725301.1.

3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase. 3CLpro 3C-like Protease Protein, SARS-COV-2, Recombinant (aa 1-306) is expressed in E. coli expression system. The predicted molecular weight is 33.8 kDa and the accession number is YP_009725301.1.

Recombinant PreScission Protease (rPSP) is a highly purified, restriction-grade 6×His-tagged protease derived from human rhinovirus 3C (HRV 3C). It specifically cleaves at the recognition sequence Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP), with the cleavage occurring between the Gln and Gly residues. This protease is commonly used to remove affinity tags from fusion proteins. rPSP functions optimally at 30 °C, but retains activity at temperatures as low as 4 °C. Cleavage efficiency may vary with different fusion proteins, so optimization of enzyme amount, incubation time, and temperature is recommended. The His-tag allows easy removal of the protease after digestion using Ni²⁺ affinity chromatography. The recombinant enzyme consists of 217 amino acids, has a molecular mass of approximately 24 kDa, and is produced through proprietary purification methods. It is fully biologically active.

Tobacco Etch Virus (TEV) protease is a highly site-specific cysteine protease commonly used to remove affinity tags from fusion proteins. It recognizes the sequence Glu-Asn-Leu-Tyr-Phe-Gln↓Gly Ser (ENLYFQ↓G S), with cleavage occurring between the Gln and Gly or Ser residue. The most frequently used recognition site is ENLYFQG. The optimal cleavage temperature is 30 °C, though conditions such as enzyme amount, incubation time, and temperature may require optimization for different substrates. TEV protease includes an N-terminal 6×His tag, allowing for convenient removal after digestion via Ni²⁺ affinity chromatography. The recombinant enzyme consists of 231 amino acids, has a molecular mass of approximately 28.4 kDa, and is fully biologically active following purification.

Expression system: E. coli
Length: 1-106, Full Length
Activity: Not Tested