Analytical Data
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Gene name
HMGCL
- Application
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Alternative Names
HMGCL;Hydroxymethylglutaryl-CoA lyase. 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
P35914
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Expression Region
28-325aa
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AA Sequence
MTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSF VSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVI FGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPY EGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVP LAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNL ATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKLH HHHHH
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Molecular Weight
33 kDa
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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
Related Products
Protein Description
HMGCL (3-hydroxy-3-methylglutaryl-CoA lyase) is an essential enzyme in the ketogenesis and leucine catabolism pathways, facilitating the conversion of HMG-CoA to acetoacetate and acetyl-CoA. Deficiencies in HMGCL can lead to significant metabolic disorders, including organic acidemia and severe hypoketotic hypoglycemia, which pose serious health risks, particularly in neonates. The necessity for a robust understanding of HMGCL both in terms of its structure and function has spurred research efforts into recombinant protein production. Recombinant HMGCL allows for the detailed study of enzyme kinetics, structure-function relationships, and potential therapeutic interventions. Furthermore, the production of this enzyme in a controlled system can facilitate the development of diagnostic tools and therapeutic strategies for managing related metabolic disorders. Advances in molecular biology techniques, such as CRISPR and gene cloning, have enabled researchers to produce recombinant HMGCL in various host systems, including bacteria and yeast, thereby enhancing its availability for both basic and applied research. The insights gained from the study of recombinant HMGCL not only contribute to our understanding of metabolic pathways but also provide a foundation for potential clinical applications in treating metabolic diseases associated with HMGCL deficiency.
