Phospho-ACTH(S168) Antibody Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P01189 |
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Clone Names | 80118204 |
Gene ID | 5443 |
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Other Names | Pro-opiomelanocortin, POMC, Corticotropin-lipotropin, NPP, Melanotropin gamma, Gamma-MSH, Potential peptide, Corticotropin, Adrenocorticotropic hormone, ACTH, Melanotropin alpha, Alpha-MSH, Corticotropin-like intermediary peptide, CLIP, Lipotropin beta, Beta-LPH, Lipotropin gamma, Gamma-LPH, Melanotropin beta, Beta-MSH, Beta-endorphin, Met-enkephalin, POMC |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | POMC |
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Function | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production in melanocytes. [Met-enkephalin]: Endogenous opiate. |
Cellular Location | Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms {ECO:0000250|UniProtKB:P01193} |
Tissue Location | ACTH and MSH are produced by the pituitary gland. |
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Background
This gene encodes a polypeptide hormone precursor thatundergoes extensive, tissue-specific, post-translational processingvia cleavage by subtilisin-like enzymes known as prohormoneconvertases. There are eight potential cleavage sites within thepolypeptide precursor and, depending on tissue type and theavailable convertases, processing may yield as many as tenbiologically active peptides involved in diverse cellularfunctions. The encoded protein is synthesized mainly incorticotroph cells of the anterior pituitary where four cleavagesites are used; adrenocorticotrophin, essential for normalsteroidogenesis and the maintenance of normal adrenal weight, andlipotropin beta are the major end products. In other tissues,including the hypothalamus, placenta, and epithelium, all cleavagesites may be used, giving rise to peptides with roles in pain andenergy homeostasis, melanocyte stimulation, and immune modulation.These include several distinct melanotropins, lipotropins, andendorphins that are contained within the adrenocorticotrophin andbeta-lipotropin peptides. Mutations in this gene have beenassociated with early onset obesity, adrenal insufficiency, and redhair pigmentation. Alternatively spliced transcript variantsencoding the same protein have been described. [provided byRefSeq].
References
This gene encodes a polypeptide hormone precursor thatundergoes extensive, tissue-specific, post-translational processingvia cleavage by subtilisin-like enzymes known as prohormoneconvertases. There are eight potential cleavage sites within thepolypeptide precursor and, depending on tissue type and theavailable convertases, processing may yield as many as tenbiologically active peptides involved in diverse cellularfunctions. The encoded protein is synthesized mainly incorticotroph cells of the anterior pituitary where four cleavagesites are used; adrenocorticotrophin, essential for normalsteroidogenesis and the maintenance of normal adrenal weight, andlipotropin beta are the major end products. In other tissues,including the hypothalamus, placenta, and epithelium, all cleavagesites may be used, giving rise to peptides with roles in pain andenergy homeostasis, melanocyte stimulation, and immune modulation.These include several distinct melanotropins, lipotropins, andendorphins that are contained within the adrenocorticotrophin andbeta-lipotropin peptides. Mutations in this gene have beenassociated with early onset obesity, adrenal insufficiency, and redhair pigmentation. Alternatively spliced transcript variantsencoding the same protein have been described. [provided byRefSeq].
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