Recombinant Human PRSS3/Mesotrypsin Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-7392P

Recombinant Human PRSS3/Mesotrypsin Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-7392P
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Product Overview

Host Species Human
Accession NP_002762
Synonym Brain trypsinogen Mesotrypsin Mesotrypsinogen MTG Pancreatic trypsinogen III Protease, serine, 3 Protease, serine, 4 (trypsin 4, brain) PRSS3 PRSS4 Serine protease 3 Serine protease 4 T9 TRY3 TRY3_HUMAN TRY4 Trypsin 3 Trypsin III Trypsin IV Trypsin-3 Trypsinogen 4 Trypsinogen 5 Trypsinogen IV
Description Recombinant Human PRSS3/Mesotrypsin Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 28 kDa including tags
Purity Greater than 90% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Digestive protease that cleaves proteins preferentially after an Arg residue and has proteolytic activity toward Kunitz-type trypsin inhibitors.
Subcellular Location Secreted.
Protein Families Peptidase S1 family
Database References
Tissue Specificity Detected in pancreas and pancreatic fluid (at protein level). Expressed in pancreas and brain. Detected in ileum.

Gene Functions References

  1. PRSS3 is downregulated by intragenic hypermethylation in HCC. * Epigenetic silencing of PRSS3 facilitates growth, migration, and invasion of HCC. * PRSS3 intragenic methylation has implication in diagnosis of HCC. PMID: 28844099
  2. PRSS3 acts as an oncogene in invasive ductal carcinoma of the breast development and progression PMID: 28423522
  3. Study developed a new high resolution crystal structure of mesotrypsin complexed with diminazene through a structure-based molecular docking screen that could help facilitate derivatization efforts, addressing current pan-inhibition of human trypsins through rigidification of diminazene to select for a conformation that maximizes interactions with the non-conserved Arg-193 residue. PMID: 28463992
  4. Data show that silencing tumor-endothelial cells (EC) for trypsinogen 4 accumulated tissue factor pathway inhibitor-2 (TFPI-2) in the matrix. PMID: 26318044
  5. These findings suggest that inhibitor cleavage represents a functional adaptation of mesotrypsin that may have evolved in response to positive selection pressure. PMID: 26175157
  6. High PRSS3 expression in EOC tissues was significantly associated with advanced FIGO stage and lymph node metastasis. PMID: 25735255
  7. Data suggest that mesotrypsin cleavage of Kunitz domains may contribute to cancer progression. PMID: 25301953
  8. Mesotrypsin generated saposins A-D from prosaposin, and mature caspase-14 contributed to this process by activating mesotrypsinogen to mesotrypsin. Knockdown of these proteases markedly down-regulated saposin A synthesis in skin equivalent models. PMID: 24872419
  9. extra-pancreatic trypsinogen 3 is produced by esophageal adenocarcinoma cells and activates PAR-2 in an autocrine manner. PMID: 24146905
  10. IFN regulatory factor 2 (Irf2) has a regulatory role in trypsinogen5 gene transcription, which is resistant to a major endogenous trypsin inhibitor, Spink3 PMID: 22042864
  11. Report PRSS3/mesotrypsin upregulation in breast cancer cells and identify CD109 as the functional proteolytic target of mesotrypsin. PMID: 20035377
  12. PRSS3 plays an important role in the progression, metastasis and prognosis of human pancreatic cancer. PMID: 20947888
  13. Investigation did not reveal an association between PRSS3 variants and chronic pancreatitis. PMID: 20484962
  14. Because mesotrypsin is resistant to naturally occurring trypsin inhibitors, confined expression of the isoforms of mesotrypsinogens and enteropeptidase may indicate that mesotrypsin is involved in keratinocyte terminal differentiation PMID: 19924134
  15. Processing by mesotrypsin may ablate the protease inhibitory function of APP/protease nexin 2 in vivo and may also modulate other activities of APP/protease nexin 2 that involve the Kunitz domain. PMID: 19920152
  16. X-ray structure in complex with the inhibitor benzamidine at 1.7 A resolution; crystal structure reveals basis for inhibitor resistance PMID: 11827488
  17. biological function of human mesotrypsin is digestive degradation of trypsin inhibitors PMID: 14507909
  18. The results classify E32del mesotrypsinogen as a frequent polymorphic variant, which is not associated with chronic alcoholic pancreatitis PMID: 15855826
  19. PRSS3 promoter methylation is associated with advanced bladder cancer PMID: 15987713
  20. we determined the promoter hypermethylation status of PRSS3 in a case series study of primary NSCLC, and found methylation of this gene to be common, occurring in 53% (86 of 166) of tumors examined. PMID: 16013053
  21. Results suggest that human trypsin 4 may be one of the candidate proteases involved in the pathomechanism of multiple sclerosis via cleavage of myelin basic protein. PMID: 16412431
  22. analysis of structural rearrangement during the acylation step in human trypsin 4 on 4-methylumbelliferyl 4-guanidinobenzoate substrate analogue PMID: 16492676
  23. mesotrypsin cannot activate pancreatic zymogens, but might activate certain proteinase-activated receptors because of its thrombin-like subsite specificity; alpha1AT Pittsburgh is an effective mesotrypsin inhibitor PMID: 16759229
  24. human trypsinogen 4 is widely but unevenly distributed in the human brain. It is localized in neurons and glial cells, predominantly in astrocytes & the extracellular matrix. PMID: 17406981
  25. trypsin IV and p23 are inhibitor-resistant trypsins that can cleave and activate PARs, causing PAR(1)- and PAR(2)-dependent inflammation and PAR(2)-dependent hyperalgesia. PMID: 17623652
  26. This study reveals enhanced mRNA expression of trypsinogen IV and SERT and a higher 5-HT content in the small intestine of IBS patients compared to healthy subjects. PMID: 18363639
  27. Absence of mesotrypsinogen gene (PRSS3) copy number variations in patients with chronic pancreatitis. PMID: 18665091
  28. Here, we report that nexin-1 inhibits trypsin-4, and forms stable complexes only with this trypsin-isoenzyme. This result suggests that nexin-1 could modulate trypsin activity in brain where both nexin-1 and trypsin-4 are expressed. PMID: 19249338


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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