GLUD1 Recombinant Monoclonal Antibody

Code: CSB-RA938641A0HU

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Size:

50μl100μl

US$210

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Species Reactivity: Human

Application: ELISA, IHC, FC

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Product Details
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Target Background

Product Details

Uniprot NO.

P00367

Target Names

GLUD1

Alternative Names

Glutamate dehydrogenase 1, mitochondrial (GDH 1) (EC 1.4.1.3), GLUD1, GLUD

Species Reactivity

Human

Immunogen

A synthesized peptide from human GLUD1 protein

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

16B7

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol Immunohistochemistry (IHC) Protocol Flow Cytometry (FC) Protocol

Recommended Dilution

Application	Recommended Dilution
IHC	1:50-1:200
FC	1:50-1:200

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

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Images

IHC image of CSB-RA938641A0HU diluted at 1:100 and staining in paraffin-embedded human liver cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
IHC image of CSB-RA938641A0HU diluted at 1:100 and staining in paraffin-embedded human stomach tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
Overlay Peak curve showing PC-3 cells stained with CSB-RA938641A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/1*10⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/1*10⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.

Description

Glutamate dehydrogenase 1 (GLUD1) serves as a critical metabolic enzyme in mitochondria, catalyzing the reversible oxidative deamination of glutamate to α-ketoglutarate. This reaction sits at a key intersection of amino acid and energy metabolism, linking glutamate catabolism to the tricarboxylic acid cycle. GLUD1 has emerged as a significant focus in cancer metabolism research, where altered glutamine utilization supports rapid tumor growth, as well as in studies of hyperinsulinism-hyperammonemia syndrome and neurodegenerative conditions where glutamate homeostasis is disrupted.

This recombinant monoclonal antibody, generated against a synthetic peptide derived from human GLUD1, offers the reproducibility and consistency that demanding experimental workflows require. As a sequence-defined recombinant clone, it eliminates the lot-to-lot variability inherent in traditional hybridoma-derived antibodies, ensuring that your optimized protocols remain reliable across extended studies and collaborative projects.

Validation across multiple platforms demonstrates this antibody's experimental versatility. Immunohistochemical staining has been successfully performed in paraffin-embedded human liver cancer and stomach tissue sections using citrate buffer antigen retrieval, with effective detection at 1:100 dilution. Flow cytometry analysis in PC-3 prostate cancer cells confirms robust intracellular detection of GLUD1, showing clear signal separation from isotype control when cells are fixed and permeabilized.

Whether you are investigating metabolic reprogramming in tumor microenvironments, characterizing mitochondrial enzyme expression patterns across tissue types, or exploring GLUD1's role in cellular bioenergetics, this antibody provides a dependable tool for immunohistochemistry and flow cytometry applications in human samples.

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Target Background

Function(From Uniprot)

Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. Plays a role in insulin homeostasis. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.

Gene References into Functions

This study provides insight into the molecular mechanism by which GDH1-mediated metabolic reprogramming of glutaminolysis mediates lung cancer metastasis and offers a therapeutic strategy for patients with LKB1-deficient lung cancer. PMID:29249655
Phenotypic heterogeneity of GDH-hyperinsulinemia patients was observed within the Chinese cohort in the present study. The fact that most patients had a GLUD1 p. S445L mutation implies that this site could be a hotspot in Chinese patients. PMID:30306091
structural model of a complex of human Sirt4 and GDH in order to elucidate the molecular mechanism underlying the ADP-ribosylation of GDH by Sirt4 PMID:29571013
Upregulation of GLUD1 and SLC25A13 was associated with tumor aggressiveness and poorer prognosis in colorectal cancer patients. PMID:27924922
This study showed that SIRT5 supports the anaplerotic entry of glutamine into the TCA cycle in malignant phenotypes of CRC via activating GLUD1. PMID:29416026
the present study shows that the GDHS445L enzyme is highly sensitive to the allosteric activator ADP, explaining the hyperactivity of this mutant. INS-1E beta-cells expressing GDHS445L responded to glutamine stimulation by increasing the mitochondrial respiration and ATP production, as well as by a rise in cytosolic calcium. PMID:28911206
We have shown that alpha-ketoglutarate substrate inhibition kinetics of GDH, which include both random and obligatory ordered association/dissociation reactions, robustly control the ratio between glutamate and ammonium under a wide range of intracellular substrate variation. Dysregulation of this activity under pericentral nitrogen insufficiency contributes to the breaking down of ammonia homeostasis and thereby can s... PMID:27747338
mRNA and protein levels of GluD1 were increased in iPSC-derived neurons from FOXG1(+/-) patients. PMID:26443267
Hypoxia-induced expression of GDH relies on the up-regulation of HIF1alpha but not HIF2alpha. HIF1alpha binds the promoter of GDH and promotes the transcription of GDH gene in lung cancer cells. PMID:28065856
Results indicate that it is possible to use high-throughput screening methods to find activators for glutamate dehydrogenase (GDH) that might be useful as pharmaceutical agents. PMID:27808506
Missense mutation of GLUD1 is associated with Hyperinsulinism-hyperammonemia syndrome. PMID:27383869
Analysis of Serbian patients with Hyperinsulinism/hyperammonemia syndrome confirms the association of p.S445L and p.R221C mutations with hypoglycaemic seizures noted within the first three months of life and with subsequent risk for cognitive impairment and/or epilepsy. PMID:26759084
GLUD1 is differentially expressed in the cellular and subcellular compartments of numerous tissues. PMID:27422263
GLUD1 mutation is associated with congenital hyperinsulinism-hyperammonemia. PMID:26656609
Study of the expression of the GDH1/2 in human steroidogenic organs revealed that, while GDH2 was expressed specifically in steroid-synthesizing cells, GDH1 was expressed both in the cells that produce steroids and in those that lack endocrine function. PMID:26241911
GDH plays a critical role in colorectal cancer progression PMID:25947346
Mutation in the GLUD1 gene is associated with hyperinsulinism/hyperammonemia. PMID:25781533
side-chain interactions between 409 and 443 positions in the 'antenna' region of GDH are crucial for basal catalytic activity, allosteric regulation, and relative resistance to thermal inactivation PMID:25620628
argeting GDH1 by shRNA or a small molecule inhibitor R162 resulted in imbalanced redox homeostasis, leading to attenuated cancer cell proliferation and tumor growth. PMID:25670081
SIRT3 and glutamate dehydrogenase are altered in follicular cells of women with reduced ovarian reserve or advanced maternal age PMID:24771001
The GDH1 is a key metabolic enzyme with emerging roles in insulin regulation. MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. PMID:24295216
The data suggest a dual mechanism by which glutamate dehydrogenase activity modulates autophagy, i.e., by activating MTORC1 and by limiting the formation of reactive oxygen species. PMID:23575388
first N-terminal alpha helical structure is crucial for the mitochondrial import of hGDH2 and these findings may have implications in understanding the evolutionary mechanisms that led to the large mitochondrial targeting signals of human GDHs PMID:22658952
Lack of Glud1 in transgenic mouse brain inhibits GDH activity regardless of enzymatic direction, modified glutamate handling, decreased glutamate catabolism and increased glutamine levels without affecting synaptic transmission. PMID:22924626
Transgenic mice are useful in defining the molecular pathways affected by the over-activation of GLUD transgene in glutamatergic neurons of the brain and spinal cord. PMID:21397652
Human GDH1 appears to act like bovine GDH1, but human GDH2 does not show the same enhancement of branched chain alpha-keto acid dehydrogenase complex enzyme activities. PMID:21621574
[review] Hyperinsulinemic hypoglycemia and hyperammonemia demonstrate the important role of GDH in insulin regulation and illustrate unexpectedly important reasons for the unusually complex allosteric regulation of GDH. PMID:21130127
GDH interactions with aristolochic acid induce apoptosis of renal tubular epithelial cells. PMID:21901531
Report glutamate dehydrogenase mutations in Japanese patients with congenital hyperinsulinism and hyperammonemia syndrome. PMID:22106762
Green tea polyphenols control dysregulated glutamate dehydrogenase in transgenic mice by hijacking the ADP activation site. PMID:21813650
In Chinese, R269H, S445L mutation of the GLUD1 leads to congenital hyperinsulinism. PMID:20931523
Gradual decrease in leukocyte GLDH activity may be a key factor for neurodegenerative aging processes. PMID:20197649
Two missense mutations give rise to two different forms of congenital hyperinsulinism/hyperammonemia. PMID:11840195
increased glutamate dehydrogenase activity confers on beta-cells the ability to secrete insulin in response to glutamine PMID:11872671
Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations PMID:11903050
identify the structural basis for allosteric differences of GlUD1 and GLUD2 PMID:11950837
Tyr187 is responsible for the efficient base binding of ADP to human GDH. PMID:12022886
site-directed mutagenesis showing involvement of Glu(279)in NAD+ binding PMID:12193607
substitution of Ser for Arg-443 (but not substitution of Thr for Ser-331, Leu for Met-370, or Leu for Met-415) virtually abolished basal activity and totally abrogated the activation of the enzyme by l-leucine (1-10 mm) in the absence of other effectors PMID:12324473
These results suggest that the Ser443 residue plays an important role in the different thermal stability of human glutamate dehydrogenase isozymes (hGDH1 and hGDH2). PMID:15044002
inhibition of glutamate dehydrogenase results in sulfite neurotoxicity PMID:15273247
GLUD2 originated by retroposition from GLUD1 in the hominoid ancestor less than 23 million years ago. PMID:15378063
results suggest that cysteine 323 plays an important role in catalysis by human GDH isozymes; C323 is not directly involved in allosteric regulation. PMID:15750346
GLUD1 may have a role in hyperinsulinism/hyperammonaemia syndrome PMID:16151898
Results describe the electrophysiological mechanisms underlying the dysregulated insulin secretion in pancreatic beta cells with glutamate dehydrogenase mutations. PMID:16492972
we describe a family with a dominantly inherited mutation in GDH in Myoclonic absence epilepsy with photosensitivity. PMID:18321734
GLUD1 parental protein localizes to mitochondria and the cytoplasm, GLUD2 is specifically targeted to mitochondria. PMID:18688271
Although GDH activity is also highly expressed in the brain, central nervous system (CNS) manifestations of GLUD1 activating mutations have remained relatively unexplored. PMID:19046183
Neurological disorders in HHS are more frequent than previously thought and might suggest that mutations in the GTP binding site of GDH could be associated with more frequent epilepsy. PMID:19046187
Hence, while most of the hGDHs translocate into the mitochondria (a process associated with cleavage of the signal sequence), part of the protein localizes to the endoplasmic reticulum, probably serving additional functions PMID:19448744