Glutamate ELISA Kit

Name: Glutamate ELISA Kit
SKU: DEIA3517
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Urine and various biological samples.

Detection Method

cELISA

Intended Use

Glutamate ELISA Kit is an enzyme immunoassay for the quantitative measurement of glutamate in urine and various biological samples.

Contents of Kit

1. Adhesive Foil: Ready to use, in a resealable pouch. 4 slides
2. Reaction Plate: Ready to use, empty in a resealable pouch. 96 well plate × 1
3. Extraction Plate: Ready to use, precoated with cation exchanger in a resealable pouch. 48 well plate × 2
4. Wash Buffer Concentrate (50×): Concentrated buffer with a non-ionic detergent and physiological pH. 20 mL
5. Enzyme Conjugate: Ready to use, goat anti-rabbit immunoglobulins conjugated with peroxidase. 12 mL
6. Substrate: Ready to use, chromogenic substrate containing tetramethylbenzidine, substrate buffer and hydrogen peroxide. 12 mL
7. Stop Solution: Ready to use, containing 0.25 M sulfuric acid. H290 May be corrosive to metals. 12 mL
8. Glutamate Microtiter Strips: Ready to use, antigen precoated microwell plate in a resealable foil pouch with desiccant. 96 (8×12) wells
9. Glutamate Antiserum: Ready to use, rabbit anti-glutamate antibody, blue coloured. 6 mL
10. Assay Buffer: Ready to use, buffer with alkaline pH. 20 mL
11. Equalizing Reagent: Lyophilized protein. 1 vial
12. D-Reagent: Ready to use, crosslinking agent in dimethylsulfoxide. H317 May cause an allergic skin reaction. 4 mL
13. Q-Buffer: Ready to use, TRIS buffer. 20 mL
14. Diluent: Ready to use, buffer with sodium acetate. 20 mL
15. NaOH: Ready to use, sodium hydroxide solution. H290 May be corrosive to metals. H315 Causes skin irritation. H319 Causes serious eye irritation. 2 mL
16. Standards and Controls: Ready to use
Standard A: 0μg/mL (0μmol/L). 4 mL
Standard B: 0.6μg/mL (4.08μmol/L). 4 mL
Standard C: 2μg/mL (13.6μmol/L). 4 mL
Standard D: 6μg/mL (40.8μmol/L). 4 mL
Standard E: 20μg/mL (136μmol/L). 4 mL
Standard F: 60μg/mL (408μmol/L). 4 mL
Control 1: Refer to QC-Report for expected value and acceptable range. 4 mL
Control 2: Refer to QC-Report for expected value and acceptable range. 4 mL
Conversion: Glutamate (μg/mL) × 6.8 = Glutamate (μmol/L)
Contents: Acidic buffer with non-mercury preservative, spiked with defined quantity of Glutamate.

Storage

Store the unopened reagents at 2-8 °C until expiration date. Do not use components beyond the expiry date indicated on the kit labels. Once opened the reagents are stable for 1 month when stored at 2-8°C. Once the resealable pouch has been opened, care should be taken to close it tightly with desiccant again.

Precision

Detection Range

0.26-60 μg/mL

Sensitivity

Various biological samples can be used for L-Glutamate determination. The assay was validated for urine samples.

Citations

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Dodecafluoropentane Improves Neurological Function Following Anterior Ischemic Stroke

M. Christine Arthur, Aliza Brown, Kristen Carlson, John Lowery, Robert D. Skinner & William C. Culp

Molecular Neurobiology2016 AugPubMed ID: 27501802Read Article

Applications: ELISA
Reactive species: Rabbit
"Abstract: Dodecafluoropentane emulsion (DDFPe), an advanced oxygen transport drug, given IV at 90-min intervals maintains viability in the penumbra during cerebral ischemia in the standard rabbit anterior stroke model (STND). This study investigated shortened dosage schedules of DDFPe in nonstandard posterior (NSTND) strokes following occlusions of the posterior cerebral arteries. DDFPe given at shortened schedules of 30 or 60-min injection intervals will reduce neurological deficits, percent stroke volume (%SV), and serum glutamate levels in NSTND ischemic strokes. New Zealand White rabbits (N = 26) were randomly placed into three groups: A (n = 9) controls given saline injections every 60 min, B (n = 9) 2 % DDFPe given IV every 30 min, and C (n = 8) DDFPe every 60 min. Injections began 1 h after embolization. Groups were subdivided into STND and NSTND based on angiographically verified embolization of the cerebral arteries. Neurological assessments and blood samples were done at 0.5–1-h intervals. Rabbits were euthanized at 7 h following embolization. Stained brain slices were measured for %SV. The 30 and 60-min subgroups did not differ and were combined as DDFPe-STND or DDFPe-NSTND groups. In the DDFPe-STND stroke group, the %SV, neurological assessment scores (NAS), and serum glutamate were decreased vs. STND controls (p = 0.0016, 0.008, and 0.016, respectively). In the DDFPe-NSTND stroke group, %SV, NAS, and serum glutamate did not differ statistically compared to NSTND controls (p = 0.82, 0.097, and 0.06, respectively). More frequent dosage schedules provided no additional improvement. In anterior strokes, DDFPe improves recovery but not in the more severe NSTND strokes."
Article snippet: Blood samples were collected via the ear artery (2–3 ml) two times prior to surgery, immediately after occlusion and at 1, 3, and 5 h following embolization. The serum specimens were stored at -8 °C until analysis was performed using the glutamate ELISA kit by Creative Diagnostics® New York, USA.

Serum glutamate levels in STND and NSTND animals. (M. Christine Arthur, <i>et al</i>, 2016)

Figure 1. Serum glutamate levels in STND and NSTND animals.

Documents

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QA & Reviews

Customer Reviews

References

Prediction and Identification of Antioxidant Peptides in Potato Protein Hydrolysate

JOURNAL OF FOOD QUALITY

Authors: Wu, Juan; Mao, Chao; Zhang, Wenli; Cheng, Yu

Abstract

Principal component analysis (PCA) was used to cluster the possible amino acid compositions of antioxidant peptides in potato protein hydrolysate (PPH). The antioxidant peptides exhibiting high ABTS(+center dot)scavenging capacity were isolated with the procedure of ultrafiltration, gel filtration, and preparative RP-HPLC and identified by UPLC-MS/MS. Phe, Tyr, and His were shown to group together with ABTS(+center dot)scavenging capacity in component matrix plot. Three prominent peptides, namely, Phe-Tyr, Tyr-Phe-Glu, and Pro-Pro-His-Tyr-Phe, which matched the sequence of patatin and were made up of Phe and Tyr, were identified. The peptide Tyr-Phe-Glu demonstrated antioxidant activity against Caco-2 cell oxidation induced by H2O2. The results suggested that multivariate analysis could be used to predict the amino acid compositions of antioxidant peptides.

IMPROVING THE CATALYTIC FEATURES OF THE LIPASE FROM Rhizomucor miehei IMMOBILIZED ON CHITOSAN-BASED HYBRID MATRICES BY ALTERING THE CHEMICAL ACTIVATION CONDITIONS

QUIMICA NOVA

Authors: Carneiro, Elizabete Araujo; Pessoa Bastas, Ana Karine; Freire de Oliveira, Ulisses Marcondes; Brandao Lima de Matos, Leonardo Jose; Adriano, Wellington Sabino; de Castro Monteiro, Rodolpho Ramilton; Sousa dos Santos, Jose Cleiton; Barros Goncalves, Luciana Rocha

Abstract

The lipase from Rhizomucor miehei (RML) has been immobilized on chitosan-based hybrid (sodium alginate or carrageenan) matrices activated with glycidol (GLY), epichlorohydrin (EPI) or glutaraldehyde (GLU) groups. Then, the properties of the different biocatalysts have been evaluated and compared with the soluble RML. Thermal stability (at pH 7.0 and 60 degrees C) was significantly increased when compared to the soluble enzyme: 154-fold for chitosan 5.0% - GLU, 80-fold for chitosan 2.5% - carrageenan 2.5% - GLY and 93-fold for chitosan 2.5% - alginate 2.5% - EPI. The best biocatalyst preparation, which was 154-fold more stable than the soluble enzyme, was obtained when RML was immobilized on chitosan activated with glutaraldehyde 5.0% v/v. According to the results, it was concluded that RML immobilization on chitosan-based hybrid matrices using different chemistries greatly produced biocatalysts with different properties.