BHMT Antibody (Mouse mAb) [M13A7]

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000-1:20000 IHC1:2000 IF1:50 FCM1:50-1:100

Application
WB, IHC, IF, FCM

Reactivity
Human, Mouse, Rat

Source
Mouse 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
45 kDa

Datasheet & SDS

Biological Description

Specificity
BHMT Antibody (Mouse mAb) [M13A7] detects endogenous levels of total BHMT protein.

Clone
M13A7

Synonym(s)
Betaine--homocysteine S-methyltransferase 1, BHMT

Background
BHMT (betaine–homocysteine S-methyltransferase) is a zinc-dependent cytosolic methyltransferase of the one-carbon metabolism network that catalyzes the transfer of a methyl group from the osmolyte betaine (trimethylglycine), derived largely from choline oxidation, to homocysteine, generating methionine and dimethylglycine and thereby providing a folate- and vitamin B12-independent route for homocysteine remethylation and methionine regeneration in liver and kidney. The enzyme functions as a homotetramer with each subunit contributing to a central active site pocket that coordinates a catalytic zinc ion via conserved cysteine and histidine residues; this zinc center activates the thiol of homocysteine for nucleophilic attack on the methyl group of betaine, and enzyme activity requires a reduced thiol environment, as short-term oxidation or removal of reducing agents inactivates BHMT without gross structural disruption. At the pathway level, BHMT works in parallel with methionine synthase (MTR) to remethylate homocysteine, but uses betaine rather than 5-methyltetrahydrofolate as the methyl donor, so its flux is responsive to dietary choline/betaine supply and hepatic osmotic status rather than folate or B12 levels, and it supports maintenance of methionine and S-adenosylmethionine (SAM) pools when folate-dependent remethylation is limited, while its product dimethylglycine enters a dehydrogenase cascade that feeds back into the folate cycle. Expression is highest in hepatocytes and renal cortex, where BHMT contributes substantially to whole-body homocysteine clearance and to the irreversible oxidation arm of choline metabolism, but immunolocalization and fractionation studies also detect BHMT in the nuclear compartment, where it participates in a nuclear branch of the methionine cycle that supports local homocysteine remethylation and potentially influences chromatin methylation in situ, indicating that BHMT is not restricted to bulk cytosolic sulfur amino acid metabolism. Human genetic and biochemical data highlight BHMT as a modulator of homocysteine homeostasis and methylation capacity: common variants and interindividual differences in hepatic BHMT expression alter enzyme activity and betaine-dependent remethylation, and severe loss of function would be predicted to raise homocysteine and reduce methionine/SAM availability, although population studies to date have not identified BHMT deficiency as a major isolated cause of hyperhomocysteinemia or vascular disease compared with other enzymes in the pathway.

Background

BHMT (betaine–homocysteine S-methyltransferase) is a zinc-dependent cytosolic methyltransferase of the one-carbon metabolism network that catalyzes the transfer of a methyl group from the osmolyte betaine (trimethylglycine), derived largely from choline oxidation, to homocysteine, generating methionine and dimethylglycine and thereby providing a folate- and vitamin B12-independent route for homocysteine remethylation and methionine regeneration in liver and kidney. The enzyme functions as a homotetramer with each subunit contributing to a central active site pocket that coordinates a catalytic zinc ion via conserved cysteine and histidine residues; this zinc center activates the thiol of homocysteine for nucleophilic attack on the methyl group of betaine, and enzyme activity requires a reduced thiol environment, as short-term oxidation or removal of reducing agents inactivates BHMT without gross structural disruption. At the pathway level, BHMT works in parallel with methionine synthase (MTR) to remethylate homocysteine, but uses betaine rather than 5-methyltetrahydrofolate as the methyl donor, so its flux is responsive to dietary choline/betaine supply and hepatic osmotic status rather than folate or B12 levels, and it supports maintenance of methionine and S-adenosylmethionine (SAM) pools when folate-dependent remethylation is limited, while its product dimethylglycine enters a dehydrogenase cascade that feeds back into the folate cycle. Expression is highest in hepatocytes and renal cortex, where BHMT contributes substantially to whole-body homocysteine clearance and to the irreversible oxidation arm of choline metabolism, but immunolocalization and fractionation studies also detect BHMT in the nuclear compartment, where it participates in a nuclear branch of the methionine cycle that supports local homocysteine remethylation and potentially influences chromatin methylation in situ, indicating that BHMT is not restricted to bulk cytosolic sulfur amino acid metabolism. Human genetic and biochemical data highlight BHMT as a modulator of homocysteine homeostasis and methylation capacity: common variants and interindividual differences in hepatic BHMT expression alter enzyme activity and betaine-dependent remethylation, and severe loss of function would be predicted to raise homocysteine and reduce methionine/SAM availability, although population studies to date have not identified BHMT deficiency as a major isolated cause of hyperhomocysteinemia or vascular disease compared with other enzymes in the pathway.

References
https://pubmed.ncbi.nlm.nih.gov/18457970/ https://pubmed.ncbi.nlm.nih.gov/28288879/

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

Tech Support

Handling Instructions

Tel: +1-832-582-8158 Ext:3

If you have any other enquiries, please leave a message.

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%