Serine racemase Antibody [A1N23]

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:100-1:1000 IP1:100-1:200 IHC1:50-1:500 IF1:50-1:500

Application
WB, IP, IHC, IF, ELISA

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
37 kDa

Datasheet & SDS

Biological Description

Specificity
Serine racemase Antibody [A1N23] detects endogenous levels of total Serine racemase protein.

Clone
A1N23

Synonym(s)
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR

Background
Serine racemase is a pyridoxal 5′‑phosphate–dependent dimeric enzyme in the fold‑type II family that catalyzes the reversible racemization of L‑serine to D‑serine and also performs β‑elimination to generate pyruvate and ammonia, making it the principal biosynthetic source of D‑serine in the mammalian brain and a regulator of local serine flux between signaling and metabolic pools. The enzyme contains a PLP‑binding lysine in its active site and conserved catalytic residues that support both racemase and β‑lyase chemistry, arranged in a dynamic homodimer whose conformational flexibility underlies substrate binding, catalysis, and modulation by allosteric ligands such as divalent cations and Mg‑ATP. D‑serine produced by serine racemase serves as an essential co‑agonist at the glycine site of NMDA receptors, and the enzyme is enriched in forebrain regions where glutamatergic neurotransmission and long‑term potentiation are prominent; genetic and pharmacologic manipulation of serine racemase alters D‑serine levels, NMDA receptor activation, synaptic plasticity, and neuronal migration, positioning this enzyme as a key upstream control point in glutamate‑dependent signaling networks. Regulation of serine racemase activity integrates multiple inputs: ATP and divalent cations stimulate racemase function, while post‑translational mechanisms such as S‑nitrosylation, phosphorylation, and protein–protein interactions at the N‑ and C‑termini tune activity and stability, and the competing β‑elimination reaction provides a mechanism to drain L‑serine away from D‑serine production under conditions where dampening NMDA co‑agonist tone is advantageous. Expression and activity of serine racemase and D‑serine levels change across aging and neurodegenerative disease: hippocampal SR and D‑serine decline with normal aging in association with impaired cognition, whereas SR is upregulated in Alzheimer’s disease brain and elevated D‑serine has been reported in brain, CSF, or serum in subsets of AD patients, consistent with a shift from NMDA hypofunction in aging to hyperactivation and excitotoxicity in dementia. Abnormal SR–D‑serine–NMDA coupling in ischemic stroke, ALS, schizophrenia, and other neuropsychiatric disorders, with both excessive and deficient D‑serine linked to pathology, and the detailed characterization of SR’s catalytic mechanism and conformational energy landscape has spurred efforts to develop selective inhibitors and modulators as potential therapeutics to normalize NMDA receptor co‑agonist tone.

Background

Serine racemase is a pyridoxal 5′‑phosphate–dependent dimeric enzyme in the fold‑type II family that catalyzes the reversible racemization of L‑serine to D‑serine and also performs β‑elimination to generate pyruvate and ammonia, making it the principal biosynthetic source of D‑serine in the mammalian brain and a regulator of local serine flux between signaling and metabolic pools. The enzyme contains a PLP‑binding lysine in its active site and conserved catalytic residues that support both racemase and β‑lyase chemistry, arranged in a dynamic homodimer whose conformational flexibility underlies substrate binding, catalysis, and modulation by allosteric ligands such as divalent cations and Mg‑ATP. D‑serine produced by serine racemase serves as an essential co‑agonist at the glycine site of NMDA receptors, and the enzyme is enriched in forebrain regions where glutamatergic neurotransmission and long‑term potentiation are prominent; genetic and pharmacologic manipulation of serine racemase alters D‑serine levels, NMDA receptor activation, synaptic plasticity, and neuronal migration, positioning this enzyme as a key upstream control point in glutamate‑dependent signaling networks. Regulation of serine racemase activity integrates multiple inputs: ATP and divalent cations stimulate racemase function, while post‑translational mechanisms such as S‑nitrosylation, phosphorylation, and protein–protein interactions at the N‑ and C‑termini tune activity and stability, and the competing β‑elimination reaction provides a mechanism to drain L‑serine away from D‑serine production under conditions where dampening NMDA co‑agonist tone is advantageous. Expression and activity of serine racemase and D‑serine levels change across aging and neurodegenerative disease: hippocampal SR and D‑serine decline with normal aging in association with impaired cognition, whereas SR is upregulated in Alzheimer’s disease brain and elevated D‑serine has been reported in brain, CSF, or serum in subsets of AD patients, consistent with a shift from NMDA hypofunction in aging to hyperactivation and excitotoxicity in dementia. Abnormal SR–D‑serine–NMDA coupling in ischemic stroke, ALS, schizophrenia, and other neuropsychiatric disorders, with both excessive and deficient D‑serine linked to pathology, and the detailed characterization of SR’s catalytic mechanism and conformational energy landscape has spurred efforts to develop selective inhibitors and modulators as potential therapeutics to normalize NMDA receptor co‑agonist tone.

References
https://pubmed.ncbi.nlm.nih.gov/29413527/ https://pubmed.ncbi.nlm.nih.gov/30918891/

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%