ACTH Monoclonal / Biotin / REA296
Product Details
Description | Clone REA296 recognizes MHC class II-associated invariant chain (Ii)-derived peptide (CLIP) complexes. MHC class II alphabeta heterodimers associate early during biosynthesis with a type II membrane protein, the invariant chain (Ii). The invariant chain serves as a chaperone for MHC II molecules and mediates trafficking to the endosomal pathway. In the endosomal pathway Ii is sequentially degraded, leaving a residual CLIP in the peptide-binding groove of MHC II. In presence of antigen peptide fragments, HLA-DM then binds to the MHC II molecule, releasing CLIP and allowing peptides to bind. REA296 detects HLA class II-positive cells which have impaired HLA-DM activity, and tumor cells that have escaped immuno-surveillance by CD4-positive T cells. | Additional information: Clone REA296 displays negligible binding to Fc receptors. | |
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Conjugate | Biotin | |
Clone | REA296 | |
Target Species | Human | |
Applications | FC | |
Supplier | Miltenyi Biotec | |
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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]
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]
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Validation References
PMID 2121367 | |
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PMID 9207120 | |
PMID 24293164 | |
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