A1527
Adrenocorticotropic Hormone Fragment 7-38 human
≥97% (HPLC)
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250 μG
$292.00
0.5 MG
$460.00
1 MG
$798.00
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250 μG
$292.00
0.5 MG
$460.00
1 MG
$798.00
About This Item
Empirical Formula (Hill Notation):
C167H257N47O46
CAS Number:
Molecular Weight:
3659.11
MDL number:
UNSPSC Code:
51111800
NACRES:
NA.77
biological source:
synthetic (organic)
form:
powder
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biological source
synthetic (organic)
Quality Level
sterility
non-sterile
Assay
≥97% (HPLC)
form
powder
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... POMC(5443)
Amino Acid Sequence
Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asn-Gly-Ala-Glu-Asp-Glu-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu
Application
Adrenocorticotropic hormone fragment 7-38 human has been used as astandard in external calibration for mass spectrometry.[1]
Biochem/physiol Actions
Adrenocorticotropic hormone (ACTH) is a polypeptide hormone thatstimulates adrenocortical activity. It is produced by the prohormoneproopiomelanocortin (POMC), which is synthesized in the corticotroph andmelanotroph cells found in the intermediate and anterior lobe of the pituitarygland and the arcuate nucleus of the hypothalamus. ACTH is also synthesized inthe skin. It plays a role in controlling steroidogenesis in the adrenal glandand prevents reactive oxygen species (ROS)-induced cell toxicity. Higher levelsof ACTH lead to skin hyperpigmentation due to the hyperstimulation ofmelanocytes, characteristic of primary adrenal insufficiency (PAI). Deficiencyof ACTH synthesis, receptors, or signaling is associated with adrenalinsufficiency.[2]
Other Notes
ACTH fragment that is a potent inhibitor of ACTH-stimulated adenylate cyclase.
Lyophilized from 0.1% TFA in H2O
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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C H Li et al.
Proceedings of the National Academy of Sciences of the United States of America, 75(9), 4306-4309 (1978-09-01)
A corticotropin-inhibiting peptide (CIP) has been isolated from human pituitary extracts. It consists of 32 amino acids with a proposed sequence identical to residues 7--38 of corticotropin (ACTH). The peptide has been synthesized by the solid-phase method. The melanotropic activity
Min-Jung Kang et al.
Analytical and bioanalytical chemistry, 404(8), 2249-2258 (2012-09-04)
A multireaction monitoring method using high-performance liquid chromatography-tandem mass spectrometry was developed for 12 target peptides for determination of endogenous peptide concentrations in human serum. Chromatographic separation conditions were optimized and recoveries for liquid-liquid extraction, solid-phase extraction (SPE), and ultrafiltration
L K Malendowicz et al.
The Journal of steroid biochemistry and molecular biology, 70(4-6), 185-188 (2000-01-06)
Orexins-A and B are two novel hypothalamic peptides, which, like leptin and neuropeptide-Y (NPY), are involved in the central regulation of feeding. Since leptin and NPY were found to modulate adrenal function, we have examined whether orexins are able to
L K Malendowicz et al.
The Journal of steroid biochemistry and molecular biology, 67(2), 149-152 (1999-01-07)
Corticotropin-inhibiting peptide (CIP), the 7-38 fragment of human ACTH(1-39), is known to act as an antagonist of ACTH receptors. Accordingly, CIP has been found to inhibit ACTH-stimulated glucocorticoid secretion of dispersed rat adrenocortical cells, without per se affecting the basal
V L Clifton et al.
The Journal of clinical endocrinology and metabolism, 81(4), 1406-1410 (1996-04-01)
During human pregnancy, ACTH is produced by both the placenta and fetal pituitary. ACTH has been shown to cause vasodilatation in the adrenal cortex in vitro. In this context we have investigated the vasoactive effects of ACTH in the human
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