chymotrypsin-like

Expression system: HEK293 Cells
Length: 1-264, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-198, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 15-207, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 29-269, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 29-269, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 29-269, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 29-270, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 29-270, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 31-271, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 28-269, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 28-269, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 21-246, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 21-260, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 21-247, Full Length of Mature Protein
Activity: Not Tested

VLCTLP Protein, Macrovipera lebetina, Recombinant (hFc) is expressed in Mammalian cell. The accession number is E0Y421.

Chymotrypsin-Like Elastase Family Member 3A (CELA3A) is an enzyme that contains one peptidase S1 domain. ELA3A belongs to the peptidase S1 family of the Elastase subfamily. ELA3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. ELA3A may also function in the intestinal transport and metabolism of cholesterol. ELA3A is efficient protease with alanine specificity but only little elastolytic activity. ELA3A preferentially cleaves proteins after alanine residues.

Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. PLpro is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons.

Expression system: HEK293 Cells
Length: 1-246, Full Length
Activity: Not Tested

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified. Mouse Serpin A11, also known as SERPINA11, is a member of the serpin family.

Expression system: Baculovirus Insect Cells
Length: 1-397, Full Length
Activity: Not Tested

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified.Mouse SerpinB3, also known as Squamous cell carcinoma antigen 1, SCCA-1, SERPINB3, SCCA and SCCA1, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB3 may act as a protease inhibitor to modulate the host immune response against tumor cells. Mouse SerpinB3a and SerpinB3b, but not Serpinb3c, are functional, inhibiting both serine and cysteine proteinases with different inhibitory profiles due to the difference of two amino acids in their reactive site loops. SerpinB3a is ubiquitously expressed in most tissues, whereas expression of SerpinB3b is limited to keratinocytes. SerpinB3a and SerpinB3b may play different roles by inhibiting intrinsic or extrinsic proteinases with different expression distributions and different inhibitory profiles.

Expression system: HEK293 Cells
Length: 1-405, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-448, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-414, Full Length
Activity: Enzyme activity