Email: info@neweastbio.com   |  Call: 6109452007

Human BTN2A1 Protein, His Tag

Recombinant Human BTN2A1 Protein with C-terminal 6XHis tag
5/5

$415.00

Cat.#:  11868

   Size:   100 μg

In Stock

          Product Description          
Cat.#:     11868
Product Name:   Human BTN2A1 Protein
Size :    10 µg, 50 µg and 100 µg
Synonyms:   BK14H9.1;BT2.1;BTF1;BTN2.1;DJ3E1.1
Target:    BTN2A1
UNIPROT ID:    Q7KYR7
Description:    Recombinant Human BTN2A1 Protein with C-terminal 6xHis tag
Background:     This gene encodes a member of the immunoglobulin superfamily. The gene is located in a cluster of butyrophilin-like genes in the juxta-telomeric region of the major histocompatibility complex on chromosome 6. A pseudogene of this gene has been identified in this cluster. The encoded protein is an integral plasma membrane protein involved in lipid, fatty-acid, and sterol metabolism. Alterations in this gene may be associated with several disease states including metabolic syndrome. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2013]
Species/Host:    HEK293
Molecular Weight:    The protein has a predicted molecular mass of 25.4 kDa after removal of the signal peptide. The apparent molecular mass of BTN2A1-His is approximately 35-55 kDa due to glycosylation.
Molecular Characterization:    BTN2A1(Gln29-Ala248) 6×His tag
Purity:    The purity of the protein is greater than 85% as determined by SDS-PAGE and Coomassie blue staining.
Formulation & Reconstitution:    Lyophilized from nanodisc solubilization buffer (20 mM Tris-HCl, 150 mM NaCl, pH 8.0). Normally 5% – 8% trehalose is added as protectants before lyophilization.
Storage & Shipping:    Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature.

Figure 1. Human BTN2A1 Protein, His Tag on SDS-PAGE under reducing condition.
          Publications