Recombinant Human Kallikrein 2 His-tag Protein, CF New
Recombinant Human Kallikrein 2 His-tag Protein, CF Summary
- R&D Systems CHO-derived Recombinant Human Kallikrein 2 His-tag Protein (11691-SE)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
Ile25-Pro261, with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11691-SE
| Formulation | Supplied as a 0.2 μm filtered solution in Sodium Citrate and NaCl. |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Assay Procedure
- Assay Buffer: 50 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.05% (w/v) Brij-35, pH 7.5 (TCNB)
- Recombinant Human Kallikrein 2 (rhKLK2) (Catalog # 11691-SE)
- Substrate: Pro-Phe-Arg-AMC, 10 mM stock in DMSO
- Black 96-well plate
- Plate Reader with Fluorescence Read Capability
- Dilute rhKLK2 to 4 µg/mL in Assay Buffer.
- Dilute Substrate to 200 µM in Assay Buffer.
- In a plate, load 50 µL of 4 µg/mL rhKLK2, and start the reaction by adding 50 µL of the 200 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 200 µM Substrate.
- Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
- Calculate specific activity:
Specific Activity (pmol/min/µg) = | Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU) |
| amount of enzyme (µg) |
- rhKLK2: 0.2 µg
- Substrate: 100 µM
Scientific Data
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Recombinant Human Kallikrein 2 His-tag (Catalog # 11691-SE) is measured by its ability to cleave the fluorogenic peptide substrate Pro-Phe-Arg-7-amido-4-methylcoumarin (PFR-AMC).
Reconstitution Calculator
Background: Kallikrein 2
Recombinant human Kallikrein 2 (KLK2) is also known as glandular kallikrein or the prostate-specific glandular kallikrein as it is structurally related to KLK3, the prostate-specific antigen (PSA). KLK2 is a secreted serine protease member of the tissue kallikrein subfamily family of the peptidase S1 family (1). It is highly expressed in the human prostate gland (2) and synthesized as a pre-proenzyme like other kallikriens. Removal of the propeptide occurs through cleavage by trypsin-like activity to activate the protein (1). KLK2 also contains a catalytic domain with an extended 99 or kallikrein loop (3) and glycan that regulate its activity (4). KLK2 is highly specific for cleavage after arginine residues and is able to autoactivate and play a role in activation of KLK cascades (5). In addition, KLK2 has been reported to activate other key proteins including the urokinase-type plasminogen activator (6), IGFBPs (7), and IL10 (8). Its activity is highly regulated by activation cascades, endogenous inhibitors such as serpins protein C inhibitor, antichymotrypsin, and plasminogen activator inhibitor 1 (9-11), pH, and metal dependency (1). It is heavily implicated to play a role in prostate cancer and is attractive as a biomarker and therapeutic target (12-15).
- Prassas, I. et al. (2015) Nat. Rev. 14:183.
- Chapdelaine, P. et al. (1988) FEBS Lett. 236:205.
- Skala, W. et al. (2014) J. Biol. Chem. 289:34267.
- Guo, S. et al. (2016) J. Biol. Chem. 291:593.
- Yoon, H. et al. (2007) J. Biol. Chem. 282:31852.
- Frenette, G. et al. (1997) Int. J. Cancer 71:897.
- Emami, N. and E.P. Diamandis (2007) Mol. Oncol. 1:269.
- Oliveira, J.R. et al. (2024) Biochemistry 63:2023.
- Deperthes, D. et al. (1995) Biochim. Biophys. Acta 1245:311.
- Grauer, L.S. et al. (1998) J. Androl. 19:407.
- Mikolajczyk S.D. et al. (1999) Cancer Res. 59:3927.
- Sardana, G. et al. (2008) Clin. Chem. 54:1951.
- Shang, Z. et al. (2014) Tumor Biol. 35:1881.
- Bonk, S. et al. (2020) Prostate 80:1097.
- Zhang, J. and J.S. Chadha (2024) Cancers 16:3098.
FAQs
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