Analytical Data
-
Gene name
bioA
- Application
-
Alternative Names
bioA；Lyl-1；Protein lyl-1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P12995
-
Expression Region
1-429aa
-
AA Sequence
MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVRVLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMPPYIILPQQLQRLTAAVNRAVQDETFFCQ
-
Molecular Weight
54.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
BioA, an enzyme involved in the biosynthesis of biotin (vitamin B7), has garnered significant attention in the field of recombinant protein research due to its essential role in cellular metabolism and its potential applications in biotechnology and medicine. Biotin is a crucial cofactor for carboxylase enzymes, which participate in critical metabolic pathways, including fatty acid synthesis and gluconeogenesis. Investigating the structure and function of BioA can provide insights into biotin biosynthesis mechanisms, potentially leading to advancements in metabolic engineering and synthetic biology. Furthermore, understanding the enzymatic properties of BioA can facilitate the development of therapeutic strategies for conditions related to biotin deficiency and may inform agricultural practices that enhance crop yields through improved nutrient biosynthesis. The recombinant expression of BioA in various host systems has enabled extensive studies on its catalytic activity, structural dynamics, and interaction with substrates and inhibitors. These studies aim to optimize BioA for industrial applications, such as the production of biotin and biotinylated biomolecules. Consequently, the research on BioA not only enhances our comprehension of fundamental biological processes but also paves the way for innovative developments in health and agricultural sectors. As the demand for biotin and biotin-related compounds continues to rise, the exploration of bioA through recombinant protein techniques remains a pivotal area of study, linking fundamental enzymology with practical applications.
