Analytical Data
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Gene name
HMGCLL1
- Application
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Alternative Names
HMGCLL1; 3-hydroxy-3-methylglutaryl-CoA lyase; cytoplasmic; EC 4.1.3.4; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase; er-cHL
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TB92
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Expression Region
1-340aa
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AA Sequence
MGNVPSAVKHCLSYQQLLREHLWIGDSVAGALDPAQETSQLSGLPEFVKIVEVGPRDGLQNEKVIVPTDIKIEFINRLSQTGLSVIEVTSFVSSRWVPQMADHTEVMKGIHQYPGVRYPVLTPNLQGFHHAVAAGATEISVFGAASESFSKKNINCSIEESMGKFEEVVKSARHMNIPARGYVSCALGCPYEGSITPQKVTEVSKRLYGMGCYEISLGDTIGVGTPGSMKRMLESVMKEIPPGALAVHCHDTYGQALANILTALQMGINVVDSAVSGLGGCPYAKGASGNVATEDLIYMLNGLGLNTGVNLYKVMEAGDFICKAVNKTTNSKVAQASFNA
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Molecular Weight
63.14 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
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Protein Description
HMGCLL1 (3-hydroxy-3-methylglutaryl-CoA lyase-like 1) is a protein that has gained attention in the field of molecular biology due to its potential roles in various metabolic pathways and its involvement in cellular processes. This protein is a member of the HMG-CoA lyase family, which is crucial in the metabolism of ketone bodies and cholesterol synthesis. Research has shown that HMGCLL1 participates in the regulation of cellular energy metabolism and may impact conditions related to metabolic disorders, neurodegenerative diseases, and cancer. Its expression levels and functional implications suggest that HMGCLL1 could serve as a significant biomarker or therapeutic target in these diseases. Recent advances in recombinant protein expression techniques have enabled researchers to produce HMGCLL1 in significant quantities, facilitating detailed studies of its biochemical properties and interactions. Investigating the structure-function relationship of HMGCLL1 through site-directed mutagenesis and structural biology approaches has provided insights into its mechanism of action and regulatory roles. Understanding the functional dynamics of HMGCLL1 may lead to novel therapeutic strategies and enhance our knowledge of metabolic regulation, thereby opening new avenues for research in metabolic health and disease management.
