ACTH / Alexa Fluor 488 /

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Conjugate Alexa Fluor 488
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Target Species Human, Mouse, Rat
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Supplier Bioss
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About ACTH
This gene encodes a preproprotein that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. There are eight potential cleavage sites within the preproprotein and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. The encoded protein is synthesized mainly in corticotroph cells of the anterior pituitary where four cleavage sites are used; adrenocorticotrophin, essential for normal steroidogenesis and the maintenance of normal adrenal weight, and lipotropin beta are the major end products. In other tissues, including the hypothalamus, placenta, and epithelium, all cleavage sites may be used, giving rise to peptides with roles in pain and energy homeostasis, melanocyte stimulation, and immune modulation. These include several distinct melanotropins, lipotropins, and endorphins that are contained within the adrenocorticotrophin and beta-lipotropin peptides. The antimicrobial melanotropin alpha peptide exhibits antibacterial and antifungal activity. Mutations in this gene have been associated with early onset obesity, adrenal insufficiency, and red hair pigmentation. Alternatively spliced transcript variants encoding the same protein have been described. [provided by RefSeq, Jan 2016]
About Alexa Fluor 488
Alexa Fluor™ 488 (AF488, Alexa 488) has an excitation peak at 488 nm and an emission peak at 496 nm, and is considered a high-performance alternative to FITC. Alexa 488 is one of the most popular Alexa Fluor™ dyes and is widely used in Fluorescence Microscopy, flow cytometry, and for staining low expression markers. It is bright, highly photostable, resistant to pH changes, and less susceptible to photobleaching. Alexa 488 and is similar in size, brightness and application to DyLight™ 488, iFluor® 488 and CF®488A.
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