Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.

ClpP Protein, Clostridium botulinum, Recombinant (His & SUMO) is expressed in E. coli.

Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover. Cathepsin O Protein, Human, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag. The predicted molecular weight is 28.5 kDa and the accession number is P43234.

May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine. Carboxypeptidase A6 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 52.2 kDa and the accession number is Q8N4T0.

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.

Human Artemin is a GDNF family ligand that is distantly related to the TGF-β superfamily of molecules. It is synthesized as a preproprotein, and contains a variable length pre-, or signal sequence, plus a 68 amino acid (aa) proregion and a 113 aa mature segment. Following synthesis and proteolytic processing, mature ARTN is secreted as a presumably glycosylated, 28 kDa disulfide-linked homodimer that contains three intrachain disulfide bonds and the typical TGF-β signature cysteine-knot motif. In the mature region, human ARTN is 89% and 88% aa identical to rat and mouse ARTN, respectively. Human ARTN is active on rodent cells. The receptor for ARTN has been identified as the ligand binding subunit GFRα-3 plus the signal transducing subunit, RET. The GFRα-1/RET receptor complex has also been suggested to be a ligand binding unit for ARTN. ARTN is known to be a chemoattractant for sympathetic neuron axons innervating the developing cardiovascular system. It also promotes sensory neuron survival and likely plays a role in the development of the peripheral nervous system. Finally, it has been reported to reverse neuropathic pain due to nerve injury, and to help resolve morphological changes associated with nerve damage.

Mouse Apoptosis-mediating surface antigen FAS (Fas) belongs to the death receptor subfamily of the TNF receptor superfamily and is designated TNFRSF6. Mouse Fas contains 1 death domain and 3 TNFR-Cys repeats. It detected in various tissues including thymus, liver, lung, heart, and adult ovary. As a receptor for TNFSF6/FASLG, The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both.

CD46 was discovered in 1986 during a search for novel C3b-binding proteins. CD46 is expressed ubiquitously and functions as a co-factor in the factor I-mediated proteolytic cleavage of C3b and C4b. Its vital role in preventing complement deposition on host tissue is underpinned by the fact that deficiency of CD46 is a predisposing factor for numerous disease conditions arising from complement-mediated 'self-attack'. CD46 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 34.05 kDa and the accession number is A0A2K5WCS2.

CD46 was discovered in 1986 during a search for novel C3b-binding proteins. CD46 is expressed ubiquitously and functions as a co-factor in the factor I-mediated proteolytic cleavage of C3b and C4b. Its vital role in preventing complement deposition on host tissue is underpinned by the fact that deficiency of CD46 is a predisposing factor for numerous disease conditions arising from complement-mediated 'self-attack'. CD46 Protein, Canine, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 34.11 kDa and the accession number is A0A8C0YZN5.

Mouse Metalloproteinase inhibitor 2(TIMP-2), belongs to a family of proteins that regulate the activation and proteolytic activity of matrix metalloproteinases (MMPs). There are four mammalian members of the family; TIMP‑1, TIMP‑2, TIMP‑3, and TIMP‑4. The TIMP-2 is detected in testis, retina, hippocampus and cerebral cortex. The function of TIMP 2 protein is to inhibit MMPs non covalently by the formation of binary complexes. Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.And the interaction with MMP-14 facilitates the activation of pro-MMP-2.It has been shown that the binding of TIMP 2 to a3b1 integrin results in the inhibition of endothelial cell proliferation and angiogenesis.

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.

Kallikrein-4, also known as Enamel matrix serine proteinase 1, Kallikrein-like protein 1, KLK-L1, Serine protease 17, KLK4, PRSS17, and EMSP1, is a secreted protein that belongs to the peptidase S1 family and Kallikrein subfamily. Kallikrein-4 / KLK4 is a serine protease expressed during enamel maturation, and proteolytic processing of the enamel matrix by KLK4 is critical for proper enamel formation. Kallikrein-4 / KLK4 contains one peptidase S1 domain. Kallikrein-4 / KLK4 is secreted by transition- and maturation-stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-2). The late protease is kallikrein 4 (KLK4). The principal functions of MMP-2 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins. Defects in Kallikrein-4 / KLK4 are the cause of Amelogenesis Imperfecta Hypomaturation type 2A1 (AI2A1) which is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions.

BMP-3b / GDF-10 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Studies in mice suggest that the protein encoded by this gene plays a role in skeletal morphogenesis. In the bone morphogenetic cascade, cartilage differentiation, hypertrophy, and cell death are followed by bone formation. In this regard, all BMPs are cartilage morphogenetic proteins since cartilage is formed first. An overexpression or dysregulation of BMP pathways may lead to heterotopic bone formation or fibrodysplasia ossificans progressiva (FOP). BMPs have been implicated in FOP. The pioneering work of Sakou has implicated BMP-3b / GDF-10 in ossification of the posterior longitudinal ligament of the spine in Japanese patients. The BMP-specific antagonists such as noggin or chordin might be used therapeutically in clinical conditions with pathologically excessive bone formation. The osteoinductive capacity of BMPs has been demonstrated in preclinical models, and the efficacy of BMPs for the treatment of orthopaedic patients is now being evaluated in clinical trials. It was suggested that further progress in the clinical application of the BMP-3b / GDF-10 will depend upon the development of carriers with ideal release kinetics for the delivery of the BMPs.

GDF-8 / Myostatin / MSTN is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. GDF-8 / Myostatin / MSTN is highly expressed in skeletal muscle, and myostatin loss-of-function leads to doubling of skeletal muscle mass. Experiments in mice have improved that GDF-8 / Myostatin / MSTN is a key regulator of mesenchymal stem cell proliferation and differentiation, and mice lacking Myostatin encoding gene show decreased body fat and a generalized increase in bone density and strength. The increase in bone density is observed in most anatomical regions, including the limbs, spine, and jaw, and myostatin inhibitors have been observed to significantly increase bone formation. GDF-8 / Myostatin / MSTN is also expressed in the early phases of fracture healing, and GDF-8 / Myostatin / MSTN deficiency leads to increased fracture callus size and strength. Together, these data suggest that GDF-8 / Myostatin / MSTN has direct effects on the proliferation and differentiation of osteoprogenitor cells and that GDF-8/Myostatin/MSTN antagonists and inhibitors are likely to enhance both muscle mass and bone strength.

IdeS (IgG-degrading enzyme of Streptococcus pyogenes) is a secreted cysteine endopeptidase from the human pathogen S. pyogenes with an extraordinarily high degree of substrate specificity, catalyzing a single proteolytic cleavage at the lower hinge of human IgG. This proteolytic degradation promotes inhibition of opsonophagocytosis and interferes with the killing of group A Streptococcus. IdeS Protein, Streptococcus pyogenes, Recombinant (His & GST) is expressed in E. coli expression system with His and GST tag. The predicted molecular weight is 63.1 kDa and the accession number is F8V4V0-1.

Required for the control of apoptosis during postnatal growth. Essential for proteolytic processing of an antiapoptotic form of OPA1 which prevents the release of mitochondrial cytochrome c in response to intrinsic apoptotic signals. Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP). Promotes changes in mitochondria morphology regulated by phosphorylation of P-beta domain. PARL Protein, Human, Recombinant (Myc) is expressed in E. coli expression system with C-Myc tag. The predicted molecular weight is 37.8 kDa and the accession number is Q9H300.

Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. Neurotrypsin Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 43.4 kDa and the accession number is P56730.

Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin. Staphopain B Protein, S. aureus, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 46.9 kDa and the accession number is Q99V46.

Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.

Regulates pathways leading to the activation of NF-kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-linked ubiquitination of target proteins. Inhibits activation of NF-kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa-B. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14.

Plasma membrane-anchored serine protease that directly induces processing of pro-uPA/PLAU into the active form through proteolytic activity. Seems to be capable of activating ENaC.; (Microbial infection) In gut epithelial cells, facilitates human coronavirus SARS-CoV-2 infection through, at least, the cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. TMPRSS4 Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 49.8 kDa and the accession number is Q9NRS4.

Plasma membrane-anchored serine protease that directly induces processing of pro-uPA/PLAU into the active form through proteolytic activity. Seems to be capable of activating ENaC. TMPRSS4 Protein, Mouse, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 57.8 kDa and the accession number is Q8VCA5.

Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis. TPP2 Protein, Mouse, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 28.3 kDa and the accession number is Q64514.

Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. Accumulates within infected cells as an inactive proenzyme (proV-CATH), which is activated by proteolytic cleavage upon cell death. AcMNPV Viral cathepsin Protein (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 39.9 kDa and the accession number is P25783.

Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover. Cathepsin O Protein, Human, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.5 kDa and the accession number is P43234.

Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter.

Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin F which may have 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release. Whole toxin only has protease activity after reduction, which releases LC. Requires complex eukaryotic host polysialogangliosides for full neurotoxicity. It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function.; Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '60-Gln-|-Lys-61' bond of synaptobrevin-1/VAMP1 and the equivalent 'Gln-|-Lys' sites in VAMP2 and VAMP3. Cleaves the '48-Gln-|-Lys-49' bond of A.californica synaptobrevin (AC P35589).; Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and the receptor protein SV2A, SV2B and SV2C in close proximity on host synaptic vesicles; although not all evidence indicates these are the receptors. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation. The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol.

Defensins are cationic peptides. It is an important ingredient of the innate immune system. β-defensins are expressed on some leukocytes and epithelial surfaces. Four human β-Defensins have been identified to date: BD-1, BD-2, BD-3 and BD-4. β-defensins contain a six-cysteine motif, they forms three intra-molecular disulfide bonds. β-defensins are also chemoattractant towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors; they are released by proteolytic cleavage of a signal sequence.

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 (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.

Bid, BH3-interacting domain death agonist, was initially cloned based in its ability to interact with both Bcl-2 and Bax. Bid contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. Bid is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. Bid is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals.

Amphiregulin (AREG) is a ligand of the epidermal growth factor receptor (EGFR), a widely expressed transmembrane tyrosine kinase. AREG is synthesized as a membrane-anchored precursor protein that can engage in juxtacrine signaling on adjacent cells. Alternatively, after proteolytic processing by cell membrane proteases, mainly TACE/ADAM17, AREG is secreted and behaves as an autocrine or paracrine factor.

HTN3 belongs to the histatin/statherin family. Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. Post-translational proteolytic processing results in many histatins: e.g., histatins 4-6 are derived from histatin 3 by proteolysis. Histatins 1 and 3 are primary products of HIS1and HIS2 alleles, respectively. Histatins are believed to have important non-immunological, anti-microbial function in the oral cavity.

β-Defensin 1 (DEFB1) is a member of the β-defensin family, which is highly expressed by epithelial cells. β-defensins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal peptide. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-defensin 1 is an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization. Defects in β-Defensin-1 contribute to asthma diagnosis, with apparent gender-specific effects in human. β-defensin 1 may also play a role in the pathogenesis of severe sepsis. In addition, β-defensin 1 is associated with induction profiles in gingival keratinocytes.

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 (A191T), 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.

Complement is an integral component of the adaptive and innate immune systems and represents one of the major effector systems for the immune responses. The classical complement pathway is triggered by C1, a complex composed of the binding protein C1q and two proenzymes, C1r and C1s. Upon binding of IgG to the head of C1q, C1r undergoes autoactivation and in turn cleaves and activates C1s. C1r and C1s, the proteases responsible for activation and proteolytic activity of the C1 complex of complement, share similar overall structural organizations featuring five nonenzymic protein modules (two CUB modules surrounding a single EGF module, and a pair of CCP modules) followed by a serine protease domain. Besides highly specific proteolytic activities, both proteases exhibit interaction properties associated with their N-terminal regions. In contrast, C1r and C1s widely differ from each other by their glycosylation patterns: both proteins contain Asn-linked carbohydrates, but four glycosylation sites are present on C1r, and only two on C1s. As a highly specific serine protease, C1s executes the catalytic function of the C1 complex: the cleavage of C4 and C2, and thus instigates a sequence of activation steps of other components of the complement system, culminating in the formation of the membrane attack complex which induces cell lysis. Like other complement serine proteases C1s has restricted substrate specificity and it is engaged into specific interactions with other subcomponents of the complement system. The only other protein known to interact with C1s physiologically is SerpinC1, an inhibitor of serine protease, which inhibits C1s activity and thus plays a regulatory role in controlling the function of C1s enzyme.

Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae. In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome. May also cleave UQCC3 in response to mitochondrial depolarization. Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. Binds cardiolipin, possibly regulating its protein turnover. Required for the stability of the respiratory supercomplexes.

Thiol protease. Acts synergistically with RgpB to catalyze the maturation of fimbrial subunits, such as FimA. Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms (Probable). Gingipain R1 Protein, Porphyromonas gingivalis, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 56.0 kDa and the accession number is P28784.

Plasma membrane-anchored serine protease that participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia.; (Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Plasma membrane-anchored serine protease that participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia.; (Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9); involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum. C1RL Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 54.5 kDa and the accession number is Q3UZ09.

Involved in the ubiquitin-dependent proteolytic pathway in conjunction with the 26S proteasome. Deubiquitinates the androgen receptor and regulates the androgen receptor signaling pathway.

Derived from proteolytic degradation of complement C5, C5a anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation. Complement C5a Protein, Pig, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 10.6 kDa and the accession number is P01032.

Flagellin is the major structural protein monomer of bacterial flagella. Flagellin through binding to its receptor and activation of antigen presenting cells stimulates the innate and adaptive immune responses. Flagellin is used as an effective systemic or mucosal adjuvant to stimulate the immune system. Flagellin is an agonist of Toll-like receptor 5 (TLR5), a pattern recognition receptor (PRR) of the innate immune system expressed on the basolateral surface of intestinal epithelial cells and on the surface of a subset of intestinal dendritic cells. Flagellin is delivered into the cytosol of macrophages by the T3SS-1 of serotype Typhimurium, where it activates the cytosolic interleukin-1 (IL-1) converting enzyme-protease activating factor (IPAF), a nucleotide-binding and oligomerization domain-like receptor (NLR) of the innate immunesystem. Recognition of flagellin by IPAF leads to activation of the inflammasome, followed by proteolytic activation of IL-1 and IL-18.

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.

Growth/differentiation factor 8(Mstn, GDF-8) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. It is expressed specifically in developing and adult skeletal muscle. It exists as a homodimer, and interacts with WFIKKN2, leading to inhibit its activity. This protein can act specifically as a negative regulator of skeletal muscle growth. It regulates cell growth and differentiation in both embryonic and adult tissues.

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.