Analytical Data
-
Gene name
LDHD
- Application
-
Alternative Names
LDH-D; DLD; Probable D-lactate dehydrogenase, mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q86WU2
-
Expression Region
Arg62~Ala265
-
Molecular Weight
52kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
LDHD, or lactate dehydrogenase D, is a critical enzyme that plays a significant role in cellular metabolism, particularly in the conversion of lactate to pyruvate, which is essential for energy production in cells. It is part of a larger family of lactate dehydrogenases that are involved in various metabolic processes. Research into LDHD has gained momentum due to its potential implications in physiological and pathological conditions, such as cancer metabolism, where altered lactate levels can affect tumor growth and adaptation to hypoxic environments. Additionally, studies have suggested a link between LDHD and metabolic disorders, including diabetes and ischemic diseases. The recombinant production of LDHD protein allows for detailed structural and functional studies that can elucidate its role in metabolic pathways. This research is vital for developing targeted therapies and understanding the biochemical mechanisms underpinning various diseases. Furthermore, the application of LDHD in biotechnology and synthetic biology holds promise for developing metabolic engineering strategies. Overall, investigations into the recombinant LDHD protein are critical for advancing our understanding of metabolic regulation and its implications in health and disease.
