| Reactivity | HuSpecies Glossary |
| Applications | WB |
| Clonality | Polyclonal |
| Host | Goat |
| Conjugate | Biotin |
| Concentration | LYOPH |
| Immunogen | E. coli-derived recombinant human Carbonic Anhydrase I/CA1 Ala2-Phe261 Accession # P00915 |
| Specificity | Detects human Carbonic Anhydrase I/CA1 in Western blots. In Western blots, less than 2% cross-reactivity with recombinant human (rh) CA2, rhCA3, rhCA4, rhCA8, rhCA9, rhCA10, rhCA12, rhCA13, and rhCA14 is observed. |
| Source | N/A |
| Isotype | IgG |
| Clonality | Polyclonal |
| Host | Goat |
| Gene | CA1 |
| Purity Statement | Antigen Affinity-purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Preservative | No Preservative |
| Concentration | LYOPH |
| Reconstitution Instructions | Reconstitute at 0.2 mg/mL in sterile PBS. |
Carbonic Anhydrase (CA) catalyzes the reversible reaction of CO2 + H2O = HCO3- + H+, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption (1). Topics in a CA meeting (6th International Conference on the CAs, June 20‑25, 2003, Slovakia) ranged from use of CAs as markers for tumor and hypoxia in clinic, as nutritional supplement in milk, and as a tool for CO2 removal and mosquito control in industry. CA1 is a cytosolic enzyme with the highest levels in erythrocytes and is a very early marker for erythroid differentiation (2). The activity of CA1 can also be measured by its ability to catalyze the reaction CO2 + H2O → HCO3- + H+, using a published method (3).
Secondary Antibodies |
Isotype Controls |
The concentration calculator allows you to quickly calculate the volume, mass or concentration of your vial. Simply enter your mass, volume, or concentration values for your reagent and the calculator will determine the rest.
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