acid protease-a

Expression system: E. coli
Length: 60-98, Partial
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 25-405, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 65-407, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-728, Full Length of Mature Protein
Activity: Cell Activity

Lysosomal associated membrane protein 1 (LAMP1) is an approximately 120 kDa transmembrane glycoprotein that is a major protein component of lysosomal membranes. Mature mouse LAMP1 consists of a 346 amino acid (aa) intralumenal domain (ECD), a 24 aa transmembrane segment, and a 12 aa cytoplasmic tail. Its lumenal domain is organized into two heavily N-glycosylated regions separated by a Ser Pro-rich linker that carries a minor amount of O-linked glycosylation. Within the lumenal domain, mouse LAMP1 shares approximately 64% and 82% aa sequence identity with human and rat LAMP1, respectively. The sorting of LAMP1 to lysosomes relies on a tyrosine motif in the cytoplasmic tail. In cytotoxic T cells and mast cells, LAMP1 is expressed in the membranes of intracellular granules that contain effector molecules such as perforin, granzymes, eicosanoids, and histamine. A glycoform of LAMP1 known as M150 is expressed on the surface of activated macrophages where it promotes T cell co-stimulation and a Th1 biased immune response. Exposure of epithelial cells to pathogenic Neisseria bacteria induces the redistribution of LAMP1 to the cell surface where it can be cleaved by the Neisseria IgA1 protease.

Chymotrypsinogen B (CTRB1) is a 263 amino acid protein with signal peptide (1-18) and Chymotrypsinogen B (19-263). Chymotrypsinogen B have three chains:Chymotrypsin B chain A(19-31), Chymotrypsin B chain B(34-164), Chymotrypsin B chain C (167-263). Chymotrypsinogen B is a Serine Protease Hydrolase secrets into gastrointestinal tract as the inactive precursor Chymotrypsinogen.

Hyaluronan-binding protein 2(HABP2) is an extracellular serine protease which binds hyaluronic acid. It secreted as an inactive single-chain precursor and is then activated to a heterodimeric form, which consists of a 50 kDa heavy and a 27 kDa light chain linked by a disulfide bond. HABP2 is involved in cell adhesion, it can cleave the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' , but not the gamma-chain of fibrinogen. As a result of this, it does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator to the active two chain form, activates coagulation factor VII.

Expression system: E. coli
Length: 220-480, Partial
Activity: Not Tested

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.

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.

Latexin, also known as endogenous carboxypeptidase inhibitor, tissue carboxypeptidase inhibitor, TCI, ECI, and LXN, is a cytoplasm protein that belongs to the protease inhibitor I47 (latexin) family. It is highly expressed in the heart, prostate, ovary, kidney, pancreas, and colon. Latexin LXN is the only known endogenous specific inhibitor of zinc-dependent metallocarboxypeptidases (MCPs) present in mammalians so far. Latexin is originally identified as a molecular marker for the regional specification of the neocortex in development in rats. The 222 amino acid latexin in the human shows different expression distribution with high levels in heart, prostate, ovary, kidney, pancreas, and colon, but only moderate or low levels in other tissues including the brain. Latexin is also expressed at high levels and is inducible in macrophages in concert with other protease inhibitors and potential protease targets, and thus is suggested to play a role in inflammation and innate immunity pathways. Despite the non-detectable sequence similarity with plant and parasite inhibitors, Latexin is related to a human putative tumor suppressor protein, TIG1. Also, Latexin is implicated in Alzheimer's disease.

Cystatin-SN, also known as Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1 and CST1, is a secreted protein which belongs to thecystatin family. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. Cystatin-SN CST1 is expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Cystatin-SN CST1 is also expressed in saliva, tears, urine and seminal fluid. Human saliva appears to contain several cysteine proteinase inhibitors that are immunologically related to cystatin S but that differ in their specificity due to amino acid sequence differences. Human salivary cystatins include Cystatin-S, Cystatin-S1, Cystatin-S2, Cystatin- SA, Cystatin-SN, Cystatin-C and Cystatin-D. Cystatin-SN is a much better inhibitor of papain and dipeptidyl peptidase I than is cystatin-S, although both inhibit ficin equally well.

Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.

Expression system: E. coli
Length: 38-291, Full Length of Mature Protein
Activity: Not Tested