Rat Dihydrolipoyl Dehydrogenase (DLD) Protein

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221€ (10 µg)

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935106861
info@markelab.com
name
Rat Dihydrolipoyl Dehydrogenase (DLD) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx066336
tested applications
WB, SDS-PAGE

Description

Rat Dihydrolipoyl Dehydrogenase (DLD) is a recombinant Rat protein expressed in E. coli.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Dihydrolipoyl Dehydrogenase (DLD)
Host
E. coli
Assay Type
Activity: Not tested
Sequence Fragment: Asp238-Glu466
Tag: N-terminal His tag
Origin
Rat
Conjugation
Unconjugated
Observed MW
Calculated MW: 28.0 kDa
Expression
Recombinant
Purity
> 95%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 5-7 working days.
Storage
Store lyophilized form at 2-8°C for up to 1 month. For longer periods, store lyophilized or liquid at -80°C. Avoid repeated freeze–thaw cycles.
Dry Ice
No
UniProt ID
Q6P6R2
Background
Protein DLD
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.
To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Concentration: Prior to lyophilization: 200 µg/ml

Descripción

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This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. Alternative splicing results in multiple transcript variants.

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