Analytical Data
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Gene name
L
- Application
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Alternative Names
L2HGDH；C14orf160；L-2-hydroxyglutarate dehydrogenase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H9P8
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Expression Region
52-463aa
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AA Sequence
VIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFVFDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL
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Molecular Weight
61.3kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
L protein, an essential component of the viral replication machinery, has garnered significant attention in the field of virology and molecular biology due to its crucial role in the life cycle of negative-strand RNA viruses, particularly the rabies virus and other members of the Rhabdoviridae family. This protein is involved in the formation of ribonucleoprotein complexes (RNPs) that are vital for viral transcription and replication. Studies have shown that L protein interacts with other viral proteins, such as the nucleoprotein (N) and phosphoprotein (P), to facilitate the synthesis of viral RNA. Its multifunctional nature, encompassing RNA polymerase activity, binding to the viral genome, and modulation of host immune responses, makes L protein a prime target for antiviral drug development and vaccine design. Recent advancements in structural biology, such as cryo-electron microscopy and X-ray crystallography, have provided insights into the molecular architecture of L protein, enhancing our understanding of its mechanisms of action. Moreover, the ongoing research aims to delineate its functional domains and regulatory interactions, paving the way for novel therapeutic strategies against infections caused by L protein-expressing viruses. Overall, the comprehensive study of L protein not only contributes to our understanding of viral pathogenesis but also opens new avenues for the development of effective countermeasures against some of the world’s most challenging viral diseases.
