Recombinant Human KLK14 protein (rFc Tag)(HPLC verified)

Species

Human

Purity

>90 %, SDS-PAGE
>90 %, SEC-HPLC

Tag

rFc Tag

Activity

not tested

Cat no : Eg2472



Product Information

Purity >90 %, SDS-PAGE
>90 %, SEC-HPLC
Endotoxin <0.1 EU/μg protein, LAL method
Activity
Not tested
Expression HEK293-derived Human KLK14 protein Gln35-Lys267 (Accession# Q9P0G3) with a rabbit IgG Fc tag at the C-terminus.
GeneID 43847
Accession Q9P0G3
PredictedSize 51.5 kDa
SDS-PAGE 13 kDa, 28-32 kDa and 55 kDa, reducing (R) condition
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

KLK14, or Kallikrein-14, is a protein-coding gene that belongs to the kallikrein family of secreted serine proteases. Activation of KLK14 is mediated by KLK5, and once activated, KLK14 further amplifies the activity of KLK proteases through a positive feedback loop by cleaving pro-KLK5, which is a central player in the KLK cascade. One of the most notable substrates of KLK14 is PAR2 (Protease-Activated Receptor 2). KLK14 has been implicated in various physiological functions and is suggested to be involved in carcinogenesis, with potential as a novel biomarker for diseases such as cancer and skin disorders. It is associated with diseases like Netherton Syndrome and Ovarian Cancer. Moreover, KLK14 may play a role in the activation of membrane-type matrix metalloproteinases (MT-MMPs), which are involved in the proteolytic processing of components of the extracellular matrix, modulating the pericellular environment in physiology and pathologies.

References:

1. Katherine Falkowski . et al. (2020). Int J Mol Sci. 21(12):4383. 2. Hyesook Yoon. et al. (2007). J Biol Chem.282(44):31852-31864. 3. Hyun-Jeong Ra. et al. (2007). Matrix Biol. 26(8):587-596.

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