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These results show that aberrant KLK7 expression leads to a switch from proliferative to invasive phenotype, suggesting a potential role of KLK7 in melanoma progression.
KLK7 is differentially expressed in lesional biopsy specimens from patients with atopic eczema relative to normal skin
impaired KLK7 secretion from lamellar granules and increased LEKTI expression could underlie the insufficient activation of KLK in atopic dermatitis.
Epigenetic regulation of KLK7 gene expression in pancreatic and cervical cancer cells
Korean X-linked ichthyosis patients exhibited unimpaired skin barrier function and frequent association with the KLK7 gene polymorphism, which may differentiate them from Western X-linked ichthyosis patients.
This report demonstrates that concurrent loss of KLK5 and KLK7 associates with a poor clinical outcome in Squamous-Cell Carcinoma and could therefore serve as prognostic marker in this disease.
Data demonstrate that elevated levels of KLK6, KLK7 and KLK9 proteins are associated with poor glioblastoma patients survival.
Our findings suggest that serum KLK7 may be a valuable diagnostic biomarker for cervical cancer, and may help to determine the individual prognosis of these patients.
KLK6 and KLK7 mRNA and protein overexpression is directly associated with early-stage ovarian tumors.
Proteolytic cleavage of midkine, CYR61, and tenascin-C govern the pathophysiological roles of KLK7.
Early-stage oral squamous cell carcinoma and high KLK7 mRNA levels were correlated with the rs10581213(wt/ins + ins/ins) genotypes
These results demonstrate the aberrant expression of KLK7 in colon cancer cells and tissues and its involvement in cell proliferation in vitro and in vivo.
Daata indicate that the peptide Abz-NLY( downward arrow)RVE-Q-EDDnp is the best synthetic substrate for Kallikrein-related peptidase 7 (KLK7) [kcat/Km=455 (mMs)(-1)].
KLK7 and KLK14 gene expression can be regarded as markers of poor prognosis for colorectal cancer patients with discriminating power between CC and adenoma patients.
Prochemerin processing protease converts prochemerin into active chemerinF; the activating truncation by the protease may trigger a structural C-terminal rearrangement leading to increased affinity of chemerin to chemokine-like receptor (CMKLR)1.
High KLK7 expression is associated with pancreatic ductal adenocarcinoma.
regulation of procaspase-14 maturation during terminal differentiation is a unique two-step process involving KLK7 and an activation intermediate of caspase-14.
The enhancement of protease activity through increased KLK7 expression by the TH2 cytokines IL-4 and IL-13 might be an important factor for mechanical and chemical epidermal barrier dysfunction in patients with atopic dermatitis.
Stromal cells can suppress the expression of the KLK7 gene in the epithelial cells in benign prostate hyperplasia.
Significant co-expression of KLKs 5 and 7 was observed in the same cancer samples. Increased KLK5 expression was a statistically significant independent prognostic factor for DFS and OS of patients
This gene encodes a member of the kallikrein subfamily of serine proteases. These enzymes have diverse physiological functions and many kallikrein genes are biomarkers for cancer. The encoded protein has chymotrypsin-like activity and plays a role in the proteolysis of intercellular cohesive structures that precedes desquamation, the shedding of the outermost layer of the epidermis. The encoded protein may play a role in cancer invasion and metastasis, and increased expression of this gene is associated with unfavorable prognosis and progression of several types of cancer. Polymorphisms in this gene may play a role in the development of atopic dermatitis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, which is one of fifteen kallikrein subfamily members located in a gene cluster on chromosome 19.
kallikrein 7 (chymotryptic, stratum corneum)
, protease, serine, 6
, serine protease 6
, stratum corneum chymotryptic enzyme
, kallikrein related-peptidase 7 (chymotryptic, stratum corneum)
, signal protein