CBS Antibody [J23E1] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Mouse, Rat

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
61 kDa

Positive Control	MCF7 cells; HeLa cells; Hs578T cells; LNCaP cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
CBS Antibody [J23E1] detects endogenous levels of total CBS protein.

Clone
J23E1

Synonym(s)
Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; CBS

Background
Cystathionine beta-synthase (CBS) is the rate-limiting pyridoxal 5'-phosphate (PLP)-dependent enzyme in the transsulfuration pathway. It catalyzes the β-replacement of serine's hydroxyl group by homocysteine to form cystathionine, channeling sulfur from methionine to cysteine biosynthesis, and generates hydrogen sulfide (H₂S) via alternative cysteine-dependent reactions. Human CBS forms a homotetramer with an N-terminal heme-binding domain that binds Fe-porphyrin to sense redox and CO changes, a central PLP catalytic domain containing the active site where Lysine 47 forms Schiff base intermediates and stabilizes carbanion or aminoacrylate species through electrostatic interactions, and C-terminal tandem CBS domains that bind S-adenosylmethionine (AdoMet) for allosteric activation by rigidifying the tetramer and enhancing PLP site accessibility. CBS maintains homocysteine homeostasis, which is essential for vascular health, with AdoMet-induced activation boosting flux under high-methionine conditions. Heme modulates activity by shifting PLP tautomerism to inhibit the enzyme under oxidative stress, while H₂S production acts as a gasotransmitter regulating vasodilation, neuromodulation, and cytoprotection through sulfhydration of targets such as K(ATP) channels and protein kinases. The enzyme's tetrameric assembly positions regulatory CBS domains away from the catalytic core, transmitting conformational changes that reposition active site residues such as lysine and arginine to stabilize zwitterionic intermediates during β-replacement. CBS deficiency causes homocystinuria, leading to hyperhomocysteinemia, thromboembolism, lens dislocation, skeletal abnormalities, and cognitive impairment due to toxic homocysteine accumulation and impaired H₂S and glutathione synthesis. Pathogenic mutations often disrupt tetramerization, heme or PLP binding, or AdoMet responsiveness.

Background

Cystathionine beta-synthase (CBS) is the rate-limiting pyridoxal 5'-phosphate (PLP)-dependent enzyme in the transsulfuration pathway. It catalyzes the β-replacement of serine's hydroxyl group by homocysteine to form cystathionine, channeling sulfur from methionine to cysteine biosynthesis, and generates hydrogen sulfide (H₂S) via alternative cysteine-dependent reactions. Human CBS forms a homotetramer with an N-terminal heme-binding domain that binds Fe-porphyrin to sense redox and CO changes, a central PLP catalytic domain containing the active site where Lysine 47 forms Schiff base intermediates and stabilizes carbanion or aminoacrylate species through electrostatic interactions, and C-terminal tandem CBS domains that bind S-adenosylmethionine (AdoMet) for allosteric activation by rigidifying the tetramer and enhancing PLP site accessibility. CBS maintains homocysteine homeostasis, which is essential for vascular health, with AdoMet-induced activation boosting flux under high-methionine conditions. Heme modulates activity by shifting PLP tautomerism to inhibit the enzyme under oxidative stress, while H₂S production acts as a gasotransmitter regulating vasodilation, neuromodulation, and cytoprotection through sulfhydration of targets such as K(ATP) channels and protein kinases. The enzyme's tetrameric assembly positions regulatory CBS domains away from the catalytic core, transmitting conformational changes that reposition active site residues such as lysine and arginine to stabilize zwitterionic intermediates during β-replacement. CBS deficiency causes homocystinuria, leading to hyperhomocysteinemia, thromboembolism, lens dislocation, skeletal abnormalities, and cognitive impairment due to toxic homocysteine accumulation and impaired H₂S and glutathione synthesis. Pathogenic mutations often disrupt tetramerization, heme or PLP binding, or AdoMet responsiveness.

References
https://pubmed.ncbi.nlm.nih.gov/32365821/ https://pubmed.ncbi.nlm.nih.gov/10338090/

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%