BBOX1 Protein, Human (sf9, His-GST)
Based on 1 Customer Validation
The BBOX1 protein plays a central role in cellular processes as it catalyzes the formation of L-carnitine from gamma-butybetaine. This enzyme activity is essential for the biosynthesis of L-carnitine, an important compound involved in fatty acid metabolism and energy production. BBOX1 Protein, Human (sf9, His-GST) is the recombinant human-derived BBOX1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.
- Species: Human
- Source: Sf9 insect cells
-
Storage:Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Biological Activity
Description
The BBOX1 protein plays a central role in cellular processes as it catalyzes the formation of L-carnitine from gamma-butybetaine. This enzyme activity is essential for the biosynthesis of L-carnitine, an important compound involved in fatty acid metabolism and energy production. BBOX1 Protein, Human (sf9, His-GST) is the recombinant human-derived BBOX1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.
Background
BBOX1 (gamma-butyrobetaine dioxygenase 1) is an enzyme that catalyzes the formation of L-carnitine from gamma-butyrobetaine. This enzymatic process is a key step in the biosynthesis of L-carnitine, an essential compound involved in the transport of fatty acids into mitochondria for beta-oxidation. By converting gamma-butyrobetaine into L-carnitine, BBOX1 contributes to the regulation of carnitine levels, which play a crucial role in energy metabolism. L-carnitine serves as a cofactor in the transport of long-chain fatty acids across the mitochondrial membrane, facilitating their utilization as a source of energy. It has to succinctly outline BBOX1's specific role in the biosynthesis of L-carnitine, emphasizing its importance in cellular metabolism and energy homeostasis.
Verified Bioactivity
The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.
Technical Parameters
-
Species Human
-
Source Sf9 insect cells
-
Tag N-His;N-GST
-
Accession
O75936 (M1-N387)
-
Molecular Construction
-
N-term
-
His-GST
-
BBOX1 (M1-N387)
Accession # O75936 -
C-term
-
-
Protein Length
Full Length
-
Synonyms
BBOX1; Butyrobetaine (Gamma), 2-Oxoglutarate Dioxygenase (Gamma-Butyrobetaine Hydroxylase) 1; Prev. BBOX; Gamma-Butyrobetaine Hydroxylase; Gamma-BBH; Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase 1; BBH; Gamma-Butyrobetaine,2-Oxoglutarate Dioxygenase; G-
-
AA Sequence
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVENGN
-
Predicted Molecular Mass
72.5 kDa
-
Molecular Weight
Approximately 65 kDa, based on SDS-PAGE under reducing conditions.
-
Purity
≥ 85%, as determined by reducing SDS-PAGE.
Product Properties
Solution
Supplied as a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, 10% glycerol, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.
Shipping with dry ice.
Documentation
-
Data Sheet (261 KB)
-
SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
-
Handling Instructions (2659 KB)
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)