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Protease Protein

Hot Protease Protein Partial List by Molecule

 

Protease Protein by catalytic domains

Protease Protein by Species

Protease Proteins for Protein Tag Cleavage

Best EK\3C protease Assurance

  • • Steady product quality
  • • Lower priced, cost-effective
  • • Easy operation, time saving
  • • With poly His tag, easy to be removed
 
  • • High protease activity
  • • High purity, low pollution
  • • Suitable for recombinant protein's purification
  • • Be used in more then 1000 proteins' purification

High Quality Immune Checkpoint Protein Assurance


Figure 1. Good activity of EK \ 3C protease

Figure 2. High purity of EK \ 3C protease

Part of Featured Protease Proteins

Catalogue Product name Purity Endotoxin
12517-H08H Human Cathepsin D / CTSD Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
13082-H08H Human PGA4 / Pepsinogen A Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
10483-H08H Human Cathepsin B / CTSB Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
10487-H08H Human Cathepsin S / CTSS Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
10896-H08H Human ADAM12 Protein (His Tag) > 98 % as determined by SDS-PAGE < 1.0 EU/μg protein
50959-M08H Mouse CNDP1 Protein (His Tag) > 93 % as determined by SDS-PAGE < 1.0 EU/μg protein
11760-H07H Human DPP10 / DPRP3 Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
11820-H08H Human KLK-8 / Kallikrein-8 Protein (His Tag) > 98 % as determined by SDS-PAGE < 1.0 EU/μg protein
11760-H07H Human DPP10 / DPRP3 Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
10969-H08H Human Renin Protein (His Tag) > 95 % as determined by SDS-PAGE < 1.0 EU/μg protein
10836-H08H Human HPRG / HRG Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein
11834-H08H Human Fetuin-B / FETUB Protein (His Tag) > 95 % as determined by SDS-PAGE < 1.0 EU/μg protein
10207-H01H Human ECE-2 Protein (Fc Tag) > 95 % as determined by SDS-PAGE < 1.0 EU/μg protein
13550-H08B Human ADAMTSL1 / PUNCTIN Protein (His Tag) > 97 % as determined by SDS-PAGE < 1.0 EU/μg protein

More information about protease

Background of Protease

Proteases perform a non-reversible process to hydrolyze peptide bonds, such as removing the initiating methionine from the newly synthesized cytoplasmic peptide, removing signal peptides and removing targeting signal peptides. Based on the mechanism of catalysis, proteases are divided into five classes, metalloproteases, serine, cysteine, threonine and aspartic proteases in mammals. For aspartic proteases and metalloproteases, an active water molecule is used as a nucleophile to attack substrate. For the rest three classes, 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 top 2 populated protease families. Normally, proteases contain multiple domains, including catalytic domain and non-catalytic domain. Non-catalytic domains include domains guiding cellular localizations, autoinhibitory prodomains and domains for recognizing specific substrates. In very few cases, proteases have more than one domain responsible for peptide bond hydrolysis. Studies have shown that proteases function in all stages of tumor progression, including growth, survival, angiogenesis and invasion. Due to their crucial roles in controlling multiple biological processes, protease are highly regulated by several mechanisms, such as regulating at gene expression level, endogenous inhibitors and turning on/off zymogens.

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