Email: info@neweastbio.com   |  Call: 6109452007

Human CA12 Protein, hFc Tag

Recombinant human CA12 protein with C-terminal human Fc tag
5/5

$550.00

Cat.#:  11574

   Size:   100 μg

In Stock

          Product Description          
Cat.#:     11574
Product Name:   Human CA12 Protein
Size :    10 µg, 50 µg and 100 µg
Synonyms:   CA-XII
Target:    CA12
UNIPROT ID:    O43570
Description:    Recombinant human CA12 protein with C-terminal human Fc tag
Background:     Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. This gene product is a type I membrane protein that is highly expressed in normal tissues, such as kidney, colon and pancreas, and has been found to be overexpressed in 10% of clear cell renal carcinomas. Three transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jun 2014]
Species/Host:    HEK293
Molecular Weight:    The protein has a predicted molecular mass of 57.3 kDa after removal of the signal peptide. The apparent molecular mass of CA12-hFc is approximately 55-70 kDa due to glycosylation.
Molecular Characterization:    CA12(Ala25-Ser301) hFc(Glu99-Ala330)
Purity:    The purity of the protein is greater than 95% 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 CA12 Protein, hFc Tag on SDS-PAGE under reducing condition.
          Publications