protein

Kallikrein-7 Protein, Human (HEK293, His, solution)

HY-P70163

10 μg;50 μg

160;450 USD

Kallikrein-7 Protein, Human (HEK293, His, solution)

proteins

HEK293

10 μg;50 μg

160;450 USD

Kallikrein-7 Protein (KLK7), a member of the tissue kallikrein family, is a first protease target of vaspin inhibited by classical serpin mechanism with high specificity in vitro. KLK7 cleaves human insulin in the A- and B-chain. KLK7 a serine protease with chymotrypsin-like activity which was involved in the regulated desquamation of terminally differentiated keratinocytes. KLK7 mediates the disruption of corneodesmosomes, the cell–cell adhesion junctions of corneocyites, by hydrolyzing the two mayor cadherins (corneodesmosin and desmocollin 1) in the extracellular region of these junctions. KLK7 overexpression and/or increased activity result in over-desquamation [1] [2] [3] . Kallikrein-7 Protein, Human (HEK293, His, solution) is the recombinant human-derived Kallikrein-7 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of Kallikrein-7 Protein, Human (HEK293, His, solution) is 230 a.a., with molecular weight of ~30.0 kDa.

Human

The molecular mass of full-length mature KLK7 is predicted to be ~25 kDa, and KLK7 has one predicted glycosylation site at 246NDT, which is located away from the KLK7 catalytic triad and substrate binding pocket [1] . KLK7 is a member of the tissue kallikrein family that comprises 15 chymotrypsin- or trypsin-like serine proteases in humans. KLK7 is predominantly expressed in the skin where it is involved in the desquamation process. Aberrant KLK7 activity is a major underlying pathogenic mechanism of inflammatory skin diseases such as psoriasis, acne rosacea and Netherton syndrome [1] . KLK7 is initially characterized as an enzyme implicated in the degradation of intercellular cohesive structures in the stratum corneum of stratified squamous epithelia, preceding desquamation in the skin. It catalyzes the degradation of desmosomes in the outermost layer of skin and permits cell shedding to take place at the skin surface. Overexpression of KLK7 in tumor cells has been reported to significantly enhance the invasive potential in intracranial malignancies and ovarian cancer cells. Thus, KLK7 can contribute to the degradation of extracellular matrices in oral squamous cell carcinoma (OSCC) tissues, promoting invasion of neoplastic cells locally and facilitating metastasis to regional lymph nodes [2] .

rHuKallikrein 7/KLK7, His ; Kallikrein-7; hK7; Serine Protease 6; Stratum Corneum Chymotryptic Enzyme; hSCCE; KLK7; PRSS6; SCCE

Greater than 95% as determined by reducing SDS-PAGE.

Supplied as a 0.2 μm filtered solution of 20 mM HEPES, 150 mM NaCl, pH 7.5.

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