Seattle Genova is trying to offer our customers great protease production services that maintain the bioactivities of your proteins just as they were in nature. To achieve this, we can offer both nature protein purification services and recombinant protein production services. We have formulated very specialized procedures to make sure the produced proteins will maintain their biological activities. And our well-developed bioassays can ensure extensive activity validations before we release the proteins.
Background of Protease
Proteases conduct a non-reversible procedure to hydrolyze peptide bonds, such as reducing the initiating methionine from the recently synthesized cytoplasmic peptide, removing signal peptides and removing targeting signal peptides. Established on the mechanism of catalysis, proteases are distributed into five classes, metalloproteases, serine, cysteine, threonine and aspartic proteases in mammals. For aspartic proteases and metalloproteases, an active water molecule is utilized as a nucleophile to attack the substrate. For the rest three categories, they use an amino acid residue (Cys, Ser or Thr) as the nucleophile. In the Degradome Database, within the 569 human proteases, metalloproteases and serine proteases are the main 2 populated protease families. Normally, proteases contain multiple domains, comprising the catalytic domain and the non-catalytic domain. Non-catalytic domains comprise domains guiding cellular localizations, autoinhibitory domains and domains for understanding specific substrates. In very few cases, proteases have better than one domain responsible for peptide bond hydrolysis. Research has shown that proteases function in all phases of tumour progression, comprising growth, survival, angiogenesis and invasion. Due to their significant roles in regulating multiple biological processes, protease is highly governed by several mechanisms, such as operating at the gene expression level, endogenous inhibitors and turning on/off zymogens.
Aspartate Protease & Regulator-enzyme
Aspartic proteases are a group of protease enzymes that use two highly conserved aspartic acid residues in the active site for a catalytic split of their peptide substrates. Unlike serine or cysteine proteases these proteases do not construct a covalent intermediate during cleavage. Nearly all available aspartyl proteases are inhibited by pepstatin. HIV protease is different in that it is a homodimer and each of the monomeric units contributes an aspartic acid.
Cysteine Protease & Regulator-enzyme
Cysteine proteases (CPs) are responsible for various biochemical processes arising in living organisms and they have been implicated in the development and progression of numerous diseases that comprise abnormal protein turnover. The crucial physiological role of Cysteine proteases is the metabolic degradation of peptides and proteins. The activity of Cysteine proteases is governed among others by their specific inhibitors: cystatins.
Metalloprotease & Regulator-enzyme
Metalloproteases are the most various of the four main protease types, with more than 50 families assessed to date. Most metalloproteases expect zinc, but some aim for cobalt, which activates the water molecule. The metal ion is organized to the protein by amino acid ligands. The recognized metal ligands are His, Glu, Asp and Lys. The majority of these proteases are endopeptidases in comparison to the aminopeptidases. MMPs, Adams and Adams are governed by TIMPs, which have various specificity toward several members of these families.
Serine Protease & Regulator-enzyme
Serine proteases (SPs) are a family of proteases that operate a uniquely generated serine residue in the substrate-binding pocket to catalytically hydrolyze peptide bonds. All of the serine proteases comprise three residues at their active site: a serine, a histidine, and an aspartate. Serine proteases fall into two broad classifications based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.
Proteases in cancer-enzyme
Proteases in normal cells are significant in carrying out biological processes. In living systems, a balance between proteases and their anti-proteases, and disruption of balance to numerous diseases like cancer. Steps starting from tumour initiation, growth, metastasis and finally invasion into some other site involve all five categories of proteases: serine, cysteine, aspartate, threonine and matrix metalloproteases. A huge number of reports have indicated a correlation between the activity of lysosomal cysteine proteases and tumour progression.
Trust us to give you high-quality data with a rapid turnaround time. Our team of specialists along with our wide services portfolio makes it easy to:
•Screen for inhibitors/targets utilizing our panel of numerous different assays comprising Cathepsins, Caspases, Dipeptidyl Peptidases (DPPs), Deubiquitinases, and other Proteases
•Assign from IC50 determination and single-point concentrations
•Obtain data within days of compound submission
•Conduct follow-up studies employing the same proteins manufactured in-house
•Get questions answered or project advice in a time-efficient manner
√Casein substrate – the regulation activity of any protease that cuts casein into peptide fragments
√Trypsin standard – quantify protease activity near trypsin, a universally accepted reference
√Sensitive – 1000 times more sensitive than assays that utilize unmodified forms of casein
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