Biotinylated Human BTN1A1/Butyrophilin Protein
Catalog No: BTN1A1-HB002
- Species
- Human
- Expression System
- HEK293
- Tag
- His, Avi
Product overview
Recombinant Biotinylated Human BTN1A1/Butyrophilin Protein is expressed in HEK293 cells with a His tag and Avi tag at the C-terminus. It contains amino acid residues Ala27-Arg242 (UniProt accession: Q13410).
Product Details
- Molecular Aliases
- BT; BTN1A1; BTN; Butyrophilin
- Protein Length
- Ala27-Arg242
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 26.9 kDa. Due to glycosylation, the protein migrates to 30-40 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display
Biotinylated Human BTN1A1 on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Biotinylated Human BTN1A1 is greater than 95% as determined by SEC-HPLC.
Background
Butyrophilin 1A1 (BTN1A1) is one of the membrane proteins that surrounds LD,BTN1A1 plays an important role in regulating LD synthesis via a mechanism involving membrane phospholipid composition.
References
- Han L, Zhang M, Xing Z, Coleman DN, Liang Y, Loor JJ, Yang G. Knockout of butyrophilin subfamily 1 member A1 (BTN1A1) alters lipid droplet formation and phospholipid composition in bovine mammary epithelial cells. J Anim Sci Biotechnol. 2020 Jul 3;11:72. doi: 10.1186/s40104-020-00479-6. PM
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