Anti-Kallikrein 6/KLK6 Antibody Picoband®

KLK6 (Kallikrein-related peptidase 6), also called KALLIKREIN 6, NEUROSIN, PROTEASE M, ZYME or PRSS9, is a protein that in humans is encoded by the KLK6 gene. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. The encoded enzyme is regulated by steroid hormones. Northern blot analysis revealed that the PRSS9 mRNA was expressed in several primary tumors and cell lines from mammary, prostate, and ovarian cancers, but was not detected in any metastases of these cancers. The KLK6 gene is mapped on 19q13.41. In tissue culture, the enzyme has been found to generate amyloidogenic fragments from the amyloid precursor protein, suggesting a potential for involvement in Alzheimer's disease. Upon cellular stress, neurosin was released from mitochondria to the cytosol, which resulted in the increase of degraded alpha-synuclein species. Neurosin may play a significant role in physiologic alpha-synuclein degradation and also in the pathogenesis of synucleinopathies.

In fluids, highest levels found in milk of lactating women followed by cerebrospinal fluid, nipple aspirate fluid and breast cyst fluid. Also found in serum, seminal plasma and some amniotic fluids and breast tumor cytosolic extracts. Not detected in urine. At the tissue level, highest concentrations found in glandular tissues such as salivary glands followed by lung, colon, fallopian tube, placenta, breast, pituitary and kidney. Not detected in skin, spleen, bone, thyroid, heart, ureter, liver, muscle, endometrium, testis, pancreas, seminal vesicle, ovary, adrenals and prostate. In brain, detected in gray matter neurons (at protein level) . Colocalizes with pathological inclusions such as Lewy bodies and glial cytoplasmic inclusions. Overexpressed in primary breast tumors but not expressed in metastatic tumors.

Apoptosis, Associated Proteins, Cell Biology, Developmental Biology, Intracellular, Neurogenesis, Neurology Process, Neuroscience, Organogenesis, Protein Phosphorylation, Ser/Thr Kinases, Signal Transduction

Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.

1. Anisowicz, A., Sotiropoulou, G., Stenman, G., Mok, S. C., Sager, R. A novel protease homolog differentially expressed in breast and ovarian cancer. Molec. Med. 2: 624-636, 1996. 2. Elliott, M. B., Irwin, D. M., Diamandis, E. P. In silico identification and Bayesian phylogenetic analysis of multiple new mammalian kallikrein gene families. Genomics 88: 591-599, 2006. 3. Iwata, A., Maruyama, M., Akagi, T., Hashikawa, T., Kanazawa, I., Tsuji, S., Nukina, N. Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Secreted. Nucleus, nucleolus. Cytoplasm. Mitochondrion. Microsome. In brain, detected in the nucleus of glial cells and in the nucleus and cytoplasm of neurons. Detected in the mitochondrial and microsomal fractions of HEK-293 cells and released into the cytoplasm following cell stress.