Recombinant production enables lot-to-lot consistency and is animal-cruelty-free
Western blot analysis of Kallikrein 5 on different lysates. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in PBS for 1 hour at room temperature. The primary antibody (ET7110-90, 1/500) was used in 5% BSA at room temperature for 2 hours. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1:5,000 dilution was used for 1 hour at room temperature.
Lane 1: MCF-7 cell lysate
Lane 2: SK-Br-3 cell lysate
HK5 antibody;Kallikrein 5 antibody;Kallikrein L2 antibody;Kallikrein like 2 antibody;Kallikrein like protein 2 antibody;Kallikrein related peptidase 5 antibody;Kallikrein-5 antibody;Kallikrein-like protein 2 antibody;Kallikrein5 antibody;KLK 5 antibody;KLK L2 antibody;KLK-L2 antibody;KLK5 antibody;KLK5_HUMAN antibody;KLKL 2 antibody;KLKL2 antibody;SCTE antibody;Stratum corneum tryptic enzyme antibody;UNQ570/PRO1132 antibody
Belongs to the peptidase S1 family. Kallikrein subfamily.
Expressed in skin, breast, brain and testis. Expressed at the stratum granulosum of palmar skin.
Kallikrein-related peptidase 5 (KLK5), formerly known as stratum corneum tryptic enzyme (SCTE), is a serine protease expressed in the epidermis. In humans it is encoded by the KLK5 gene. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Its expression is up-regulated by estrogens and progestins. Alternative splicing results in multiple transcript variants encoding the same protein. KLK5 has been suggested to regulate cell shedding (desquamation) in conjunction with KLK7 and KLK14, given its ability to degrade proteins which form the extracellular component of cell junctions in the stratum corneum. It is proposed that KLK5 regulates this process since it is able to self-activate in addition to activating KLK7 and KLK14. Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers.
Just like the interactions between antigens and antibodies, the higher the affinity between you and us the better.