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POMC Antibody [B13A5]

Cat.No.: F3420

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IHC1:4000 IF1:100

Application
WB, IHC, IF

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
29 kDa 16 kDa,35 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
POMC Antibody [B13A5] detects endogenous levels of total POMC protein.

Clone
B13A5

Synonym(s)
Pro-opiomelanocortin; POMC; Corticotropin-lipotropin

Background
Pro-opiomelanocortin (POMC) is a 241-amino-acid polyprotein precursor encoded by the POMC gene on chromosome 2p23, serving as the common progenitor for a spectrum of bioactive peptides, including ACTH, α/β/γ-MSH, β-endorphin, β-LPH, and N-POMC, through tissue-specific posttranslational processing by prohormone convertases PC1/3 and PC2 within regulated secretory granules of pituitary corticotrophs, hypothalamic arcuate nucleus neurons, and skin melanocytes. The precursor features a cleavable 26-residue N-terminal signal peptide followed by three principal domains, an N-terminal region (residues 1–61 containing γ-MSH), an ACTH domain (138–176), and a β-LPH domain (236–265), separated by pairs of dibasic residues (KR, KK, RR) recognized by PCs, with an intervening unstructured glycine loop spacer that enables precise endoproteolytic excision, C-terminal trimming by carboxypeptidase E, and N-terminal amidation of MSH peptides by peptidylglycine α-amidating monooxygenase for full receptor activity. In pituitary corticotrophs, dominant PC1/3 activity produces ACTH1-39, which stimulates adrenal glucocorticoid release via MC2R, while hypothalamic neurons preferentially express PC2, yielding α-MSH for MC3R/MC4R-mediated appetite suppression and energy expenditure by antagonizing AgRP/NPY signaling; leptin and insulin activate POMC neurons through PI3K, enhancing α-MSH secretion, white-to-brown fat conversion, and co-release of CART for synergistic anorexigenic effects. Meanwhile, β-endorphin, generated from full β-LPH cleavage, acts as an endogenous opioid analgesic via MOR. This compartmentalized processing integrates stress (CRH/AVP-induced POMC transcription via Nur77/Nr4a), circadian (CLOCK/BMAL1), and metabolic cues, maintaining HPA axis homeostasis and energy balance. POMC deficiency leads to early-onset obesity and adrenal insufficiency, whereas ectopic expression contributes to Cushing's disease and hyperpigmentation.

Background

Pro-opiomelanocortin (POMC) is a 241-amino-acid polyprotein precursor encoded by the POMC gene on chromosome 2p23, serving as the common progenitor for a spectrum of bioactive peptides, including ACTH, α/β/γ-MSH, β-endorphin, β-LPH, and N-POMC, through tissue-specific posttranslational processing by prohormone convertases PC1/3 and PC2 within regulated secretory granules of pituitary corticotrophs, hypothalamic arcuate nucleus neurons, and skin melanocytes. The precursor features a cleavable 26-residue N-terminal signal peptide followed by three principal domains, an N-terminal region (residues 1–61 containing γ-MSH), an ACTH domain (138–176), and a β-LPH domain (236–265), separated by pairs of dibasic residues (KR, KK, RR) recognized by PCs, with an intervening unstructured glycine loop spacer that enables precise endoproteolytic excision, C-terminal trimming by carboxypeptidase E, and N-terminal amidation of MSH peptides by peptidylglycine α-amidating monooxygenase for full receptor activity. In pituitary corticotrophs, dominant PC1/3 activity produces ACTH1-39, which stimulates adrenal glucocorticoid release via MC2R, while hypothalamic neurons preferentially express PC2, yielding α-MSH for MC3R/MC4R-mediated appetite suppression and energy expenditure by antagonizing AgRP/NPY signaling; leptin and insulin activate POMC neurons through PI3K, enhancing α-MSH secretion, white-to-brown fat conversion, and co-release of CART for synergistic anorexigenic effects. Meanwhile, β-endorphin, generated from full β-LPH cleavage, acts as an endogenous opioid analgesic via MOR. This compartmentalized processing integrates stress (CRH/AVP-induced POMC transcription via Nur77/Nr4a), circadian (CLOCK/BMAL1), and metabolic cues, maintaining HPA axis homeostasis and energy balance. POMC deficiency leads to early-onset obesity and adrenal insufficiency, whereas ectopic expression contributes to Cushing's disease and hyperpigmentation.

References
https://pubmed.ncbi.nlm.nih.gov/30156493/ https://pubmed.ncbi.nlm.nih.gov/18601691/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%