Analytical Data
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Gene name
HIBCH
- Application
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Alternative Names
HIBCH;3-hydroxyisobutyryl-CoA hydrolase. 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
Q6NVY1
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Expression Region
33-386aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDAAEE VLLEKKGCTG VITLNRPKFL NALTLNMIRQ IYPQLKKWEQ DPETFLIIIK GAGGKAFCAG GDIRVISEAE KAKQKIAPVF FREEYMLNNA VGSCQKPYVA LIHGITMGGG VGLSVHGQFR VATEKCLFAM PETAIGLFPD VGGGYFLPRL QGKLGYFLAL TGFRLKGRDV YRAGIATHFV DSEKLAMLEE DLLALKSPSK ENIASVLENY HTESKIDRDK SFILEEHMDK INSCFSANTV EEIIENLQQD GSSFALEQLK VINKMSPTSL KITLRQLMEG SSKTLQEVLT MEYRLSQACM RGHDFHEGVR AVLIDKDQSP KWKPADLKEV TEEDLNNHFK SLGSSDLKF
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Molecular Weight
42 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
HIBCH (3-Hydroxyisobutyryl-CoA hydrolase) is an essential enzyme involved in the metabolism of branched-chain amino acids and plays a critical role in the mitochondrial dehydrogenation pathways. Research has increasingly focused on HIBCH due to its implications in various metabolic disorders, including ketotic hypoglycemia and neurological conditions. Mutations in the HIBCH gene can lead to a deficiency of the enzyme, affecting cellular energy production and metabolite balance. The study of HIBCH recombinant proteins has become vital for understanding its structure-function relationships and enzyme kinetics, which are essential for developing therapeutic interventions aimed at correcting metabolic imbalances caused by HIBCH-related deficiencies. Moreover, the recombinant form of HIBCH is utilized in high-throughput screening for potential small-molecule regulators that could modulate its activity, providing insights into novel therapeutic approaches for related metabolic diseases. This research not only enhances our understanding of HIBCH's physiological roles but also opens avenues for biotechnological applications in metabolic engineering and synthetic biology.
