Reactivity | HuSpecies Glossary |
Applications | IP, B/N |
Clone | 337903 |
Clonality | Monoclonal |
Host | Mouse |
Conjugate | Unconjugated |
Concentration | LYOPH |
Immunogen | Mouse myeloma cell line NS0-derived recombinant human Kallikrein 14 Gln19-Met248 Accession # AAD50773 |
Specificity | Detects human Kallikrein 14 in direct ELISAs. |
Source | N/A |
Isotype | IgG1 |
Clonality | Monoclonal |
Host | Mouse |
Gene | KLK14 |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. |
Human tissue kallikreins refer to a group of secreted serine proteases that are encoded by homologous genes clustering on chromosome 19q13.3-4. As a member of this family, human tissue Kallikrein 14 (hKLK14) is present in many tissues, with high levels in breast, skin, prostate, and brain. The 251 amino acid hKLK14 precursor consists of a signal peptide (residues 1 to 18), a pro peptide (residues 19 to 24) and an active protein (residues 25 to 251) (1). Its enzymatic activity has been shown to be mainly trypsin-like (2). However, its physiological substrates and functions are still unclear. Several studies have suggested that hKLK14 may have clinical utility as a biomarker for cancer of the breast, ovary, and prostate (3, 4). In addition, it may be the initiator of a kallikrein proteolytic cascade responsible for the degradation of the adhesion structures in the stratum corneum (2). The purified, secreted rhKLK14 corresponds to the pro form (residues 19 to 248) with a replacement of the last three residues with a His tag at the C-terminus. When activated by thermolysin, it displays enzymatic activity towards a fluorogenic peptide described above. This activity can be inhibited by rhSerpin A4, E1, and F2 (R&D Systems, Catalog # 1669-PI, 1786-PI, and 1470-PI, respectively).
Secondary Antibodies |
Isotype Controls |
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