Recombinant Human TMPRSS11A His-tag, CF

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Recombinant Human TMPRSS11a His-tag (Catalog # 11785-TP) is measured by its ability to cleave the fluorogenic peptide substrate Boc-QAR-AMC (ES014).

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human TMPRSS11A His-tag, CF Summary

Details of Functionality
Measured by its ability to cleave the fluorogenic peptide substrate Boc-QAR-AMC (Catalog # ES014). The specific activity is >350 pmol/min/μg, as measured under the described conditions.
Source
Chinese Hamster Ovary cell line, CHO-derived human TMPRSS11A protein
Phe41-Ile421, with modifications in the non-catalytic chain and a C-terminal 6-His tag
Accession #
N-terminal Sequence
 Phe41 & Ala149 (non-catalytic chain), Ile187 (catalytic chain) 
Protein/Peptide Type
Recombinant Enzymes
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
17 kDa (non-catalytic), 29 kDa (catalytic).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
19-22 kDa (non-catalytic), 29-39 kDa (catalytic), & 51-56 kDa (intact), reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES and NaCl.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Assay Procedure
  • Assay Buffer: 50 mM Tris, 0.05% BRIJ 35, pH 8.0
  • Recombinant Human TMPRSS11A His-tag (rhTMPRSS11A) (Catalog # 11785-TP)
  • Substrate: BOC-Gln-Ala-Arg-AMC (Catalog # ES014), 10 mM stock in DMSO
  • Black 96-well Plate
  • Plate Reader with Fluorescence Read Capability
  1. Dilute rhTMPRSS11A to 2.0 µg/mL in Assay Buffer.
  2. Dilute Substrate to 600 µM in Assay Buffer.
  3. Load into a plate 50 µL of 2.0 µg/mL rhTMPRSS11A and start the reaction by adding 50 µL of 600 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 600 µM Substrate.
  4. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
  5. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

    

*Adjusted for Substrate Blank
**Derived using calibration standard 7-Amino, 4-Methyl Coumarin (AMC)
Per Well:
  • rhTMPRSS11A: 0.1 µg
  • Substrate: 300 µM

























Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human TMPRSS11A His-tag, CF

  • Airway Trypsin-Like Protease 1
  • EC 3.4.21
  • EC 3.4.21.
  • ECRG1
  • Epidermal Type II Transmembrane Serine Protease
  • Epidermal Type-II Transmembrane Serine Protease
  • Esophageal Cancer-Susceptibility Gene 1 Protein
  • HATL1
  • HESP
  • TMPRSS11A
  • Transmembrane Protease Serine 11A
  • Transmembrane Protease, Serine 11A

Background

Recombinant Transmembrane protease serine 11a (TMPRSS11a), also known as Airway trypsin-like protease 1 (HATL1), Esophageal cancer-susceptibility gene 1 protein (ECRG1), and HESP is a member of the type II transmembrane serine protease (TTSP) peptidase S1 family from the human airway trypsin-like (HAT) subgroup (1). TMPRSS11a is expressed in select tissues including esophagus, lung, and aged tissue (2,3). Similar to other members of the TTSP family, TMPRSS11a is produced as a zymogen and is autoactivated into disulfide-linked non-catalytic chains composed of the TM and sea urchin sperm protein (SEA) domain and catalytic chains with a highly conserved serine protease (SP) domain (1,4). TMPRSS11a consists of three distinct regions, including an N-terminal cytoplasmic tail, a single-pass transmembrane domain, and an extracellular domain composed of the SEA domain and C-terminal serine protease domain (4).  In human and mouse airways TMPRSS11A is expressed on the epithelial surface (5). Proteolytic cleavage of viral particle surface proteins by TMPRSS11a as a host protease is involved in facilitation of cell entry for influenza A viruses and coronaviruses (5-7). Carriers of the mutant alleles of TMPRSS11A are thought to have increased risk of severe COVID 19 in association with systemic inflammation, hypercoagulability, and organ damage (8). Inhibitors of TTSPs including TMPRSS11a present in the lung have been proposed as broad-spectrum antiviral agents (5). TMPRSS11a downregulation is reported to play a role in cancer as variants are linked to the risk of oral and esophageal squamous cell carcinomas (9-11) and TMPRSS11a was identified as a putative tumor suppressor in human esophageal cancers (12,13). TMPRSS11a is upregulated in aged skin and gingival tissue, inhibits cell migration through binding to integrin beta 1 via a putative RGD motif contained within the C-terminal trypsin-like serine proteinase domain to play a role in inducing cellular senescence and attenuate wound healing capacity (3,13) making it a target for skin wound healing during aging (3). 
  1. Wu, Q. et al. (2023) Biomedicines 11:1794. 
  2. Su, T. et al. (1998) Zhonghua Zhong Liu Za Zhi 20:254.
  3. Fernandez, C. et al. (2021) FASEB J. 35:e21597.
  4. Zhang, C. et al. (2020) J. Biol. Chem. 295:12686.
  5. Fuentes-Prior, P. (2021) J. Biol. Chem. 296:100135.
  6. Kam, Y.W. et al. (2009) PLoS ONE 4:e7870.
  7. Zmora, P. et al. (2018) J. Biol. Chem. 293:13863.
  8. Cekin, N. et al. (2025) Mol. Biol. Rep. 53:51.
  9. Li, Y. et al. (2006) Carcinogenesis 27:798.
  10. Bachmann, K. et al. (2009) J. Gastrointest. Surg. 13:181.
  11. Rasool S, et al. (2013) Onkologie. 36:213.
  12. Zhao, N. et al. (2004) J. Cell. Biochem. 92:65.
  13. Zhao, N. et al. (2006) Exp. Biol. Med. 231:84.

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