MLX Antibody [N17K22] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Usage Information

Dilution
WB1:1000 IP1:100 CHIP1:100

Application
WB, IP, ChIP

Reactivity
Human, Mouse, Rat, Monkey

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
30 kDa

Datasheet & SDS

Biological Description

Specificity
MLX Antibody [N17K22] detects endogenous levels of total MLX protein.

Clone
N17K22

Synonym(s)
Max-like protein X, Class D basic helix-loop-helix protein 13 (bHLHd13), Max-like bHLHZip protein, Protein BigMax, Transcription factor-like protein 4, MLX, BHLHD13, TCFL4

Background
MLX, a basic helix-loop-helix leucine zipper transcription factor in the Myc/Max/Mad superfamily, heterodimerizes obligatorily with tissue-specific partners MLXIP (MondoA) or MLXIPL (ChREBP) to sense glucose metabolites and regulate metabolic gene expression. Both complexes feature bHLHZip domains for E-box (CACGTG) DNA binding and N-terminal activation domains responsive to glucose-6-phosphate via hexokinase-catalyzed phosphorylation, with cytoplasmic-mitochondrial retention in low glucose shifting to nuclear accumulation upon metabolite elevation. MLX/MLXIP heterodimers translocate rapidly to the nucleus following 2-deoxyglucose exposure, binding ChoRE promoters of thioredoxin-interacting protein (TXNIP), ARRDC4, and glycolytic enzymes like HK2, PFKFB3, LDH-A to drive >75% of glucose-induced transcription, while promoting histone H4 acetylation for open chromatin. MLX/MLXIPL similarly activates lipogenic targets in the liver, with MLX phosphorylation stabilizing heterotetramers on DNA for sustained activity. Glucose sensing integrates hexokinase activity, as inhibitors like 3-bromopyruvate block nuclear import, and MondoA mutations disrupting MLX dimerization abolish response. MLX orchestrates glucose homeostasis by inducing glycolysis/lipogenesis genes and repressing uptake via TXNIP, balancing nutrient flux in muscle, liver, and proliferating cells. MLX-null impairs myokine secretion, including IGF2 for myoblast fusion/Akt activation, blunts muscle regeneration, and disrupts sugar tolerance/lipid balance. Dysregulation contributes to diabetes through failed TXNIP induction and cancer via Myc cooperation, reprogramming metabolism.

Background

MLX, a basic helix-loop-helix leucine zipper transcription factor in the Myc/Max/Mad superfamily, heterodimerizes obligatorily with tissue-specific partners MLXIP (MondoA) or MLXIPL (ChREBP) to sense glucose metabolites and regulate metabolic gene expression. Both complexes feature bHLHZip domains for E-box (CACGTG) DNA binding and N-terminal activation domains responsive to glucose-6-phosphate via hexokinase-catalyzed phosphorylation, with cytoplasmic-mitochondrial retention in low glucose shifting to nuclear accumulation upon metabolite elevation. MLX/MLXIP heterodimers translocate rapidly to the nucleus following 2-deoxyglucose exposure, binding ChoRE promoters of thioredoxin-interacting protein (TXNIP), ARRDC4, and glycolytic enzymes like HK2, PFKFB3, LDH-A to drive >75% of glucose-induced transcription, while promoting histone H4 acetylation for open chromatin. MLX/MLXIPL similarly activates lipogenic targets in the liver, with MLX phosphorylation stabilizing heterotetramers on DNA for sustained activity. Glucose sensing integrates hexokinase activity, as inhibitors like 3-bromopyruvate block nuclear import, and MondoA mutations disrupting MLX dimerization abolish response. MLX orchestrates glucose homeostasis by inducing glycolysis/lipogenesis genes and repressing uptake via TXNIP, balancing nutrient flux in muscle, liver, and proliferating cells. MLX-null impairs myokine secretion, including IGF2 for myoblast fusion/Akt activation, blunts muscle regeneration, and disrupts sugar tolerance/lipid balance. Dysregulation contributes to diabetes through failed TXNIP induction and cancer via Myc cooperation, reprogramming metabolism.

References
https://pubmed.ncbi.nlm.nih.gov/26584623/ https://pubmed.ncbi.nlm.nih.gov/18458340/

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%