Recombinant Human Carbonic Anhydrase 1 Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0292NP
BL-0292NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-0292NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human Carbonic Anhydrase 1 Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-0292NP
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Product Overview

Description Recombinant Human Carbonic Anhydrase 1 is produced by our E.coli expression system and the target gene encoding Ala2-Phe261 is expressed with a 6His tag at the C-terminus.
Accession P00915
Synonym Carbonic Anhydrase 1; Carbonate Dehydratase I; Carbonic Anhydrase B; CAB; Carbonic Anhydrase I; CA-I; CA1
Gene Background Carbonic Anhydrase 1 (CA1) is a cytosolic enzyme, belonging to the alpha-carbonic anhydrase family. It is highly expressed in erythrocytes and acts as an early marker for erythroid differentiation. Carbonic anhydrase 1 plays a improtant role in many biological processes such as calcification, cellular respiration, bone resorption, acid-base balance. It is activated by imidazole, histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. At the same time, It is inhibited by sulfonamide derivatives and coumarins. In addition, CA1 is a zinc metalloenzyme that has reversible hydration of carbon dioxide. It can hydrate cyanamide to urea.
Molecular Mass 29.93 KDa
Apmol Mass 25-35 KDa, reducing conditions
Formulation Supplied as a 0.2 μm filtered solution of 12.5mM Tris-HCl, 75mM NaCl, pH 7.5.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution
Storage Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.
Subcellular Location Cytoplasm.
Protein Families Alpha-carbonic anhydrase family
Database References

Gene Functions References

  1. Anti-CA I and II antibody levels were investigated using ELISA in serum samples from 30 patients with Acute Myeloid Leukemia (AML) and 30 healthy peers. Anti-CA I and II antibody titers in the AML group were significantly higher compared with the control group (p=0.0001 and 0.018, respectively). PMID: 28270370
  2. These six-membered carbocycles showed nice inhibitory action against AChE and human carbonic anhydrase (hCA) II and I isoforms. The hCA I, II, and AChE were efficiently inhibited by these molecules, with Ki values in the range of 6.70-35.85 nM for hCA I, 18.77-60.84 nM for hCA II, and 0.74-4.60 for AChE, respectively PMID: 28613396
  3. These results showed that flavonoids especially malvin and oenin effectively inhibited hCA I and II isoenzymes. PMID: 28445001
  4. Discovery of potent carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase enzymes inhibitors: The new amides and thiazolidine-4-ones synthesized on an acetophenone base. PMID: 28544359
  5. Here are presented solved the first crystal structures of carbonic anhydrase 1and carbonic anhydrase 2 in complex with polmacoxib, at 2.0 A and 1.8 A, respectively. PMID: 27475498
  6. Neuronal carbonic anhydrase I (CA1) appears to be associated with the endoplasmic reticulum subcellular structure. PMID: 27809276
  7. CA1 is highly expressed in the sera of stage I non-small cell lung cancer patients PMID: 26232327
  8. We demonstrated that resveratrol, caffeic acid, and tannic acid in stored blood could decrease the sensitivity to oxidation of erythrocytes in vitro but did not exhibit such effects on Carbonic Anhydrase activity. PMID: 27413740
  9. CA1 is a potential oncogene and that it contributes to abnormal cell calcification, apoptosis and migration in breast cancer. PMID: 26459317
  10. We report on the competitive zinc metalation of apo-carbonic anhydrase [CA; metal-free CA (apo-CA)] in the presence of apo-metallothionein 1A domain fragments to identify domain specific determinants of zinc binding and zinc donation PMID: 26475450
  11. The gene encoding CA1 is susceptible to ankylosing spondylitis and plays a role in the process of bone formation. PMID: 22838845
  12. Structure-activity relationships study showed that indolylchalcone derivatives have higher inhibitory activities than pyrido[2,3-d]pyrimidine derivatives on hCA I and hCA II. PMID: 25165709
  13. Myocardial carbonic anhydrase 1/2 activation is significantly elevated in diabetic ischemic cardiomyopathy. PMID: 24670789
  14. may be involved in the pathogenesis of Abdominal aortic aneurysm PMID: 23557951
  15. The new prognostic biomarkers GRP78, Fructose-bisphosphate Aldolase A (ALDOA), Carbonic Anhydrase I (CA1) and Peptidyl-prolyl cis-trans isomerase A or Cyclophilin A (PPIA)) provided good survival prediction for TNM stage I-IV patients. PMID: 22996014
  16. A significant correlation was found between positive carbonic anhydrase I staining and oral squamous cell carcinoma for more advanced clinical stage and larger tumor size, but not for positive lymph node metastasis, distal metastasis, and recurrence. PMID: 22416960
  17. carbonic anhydrase I, phosphoglycerate kinase 1 and apolipoprotein A-I appeared to be the most significant variations of proteins in patients with osteopenia and osteoarthritis PMID: 22619369
  18. A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration. PMID: 22360420
  19. Overexpression of CA1 in the synovial tissues of ankylosing spondylitis (AS) patients may promote improper calcification and bone resorption in AS. PMID: 21143847
  20. single mutation of an amino acid not considered essential to catalysis (Phe91Asn) in carbonic anhydrase I, but is near substrate binding pocket, led to increase of catalytic activity; mutant CA I also showed higher affinity for sulfonamide inhibitors PMID: 20624682
  21. The X-ray crystallographic structure of the CA I Michigan 1 variant isozyme is reported, both in the presence and absence of a second bound zinc ion coordinated to His 64, His 200, and Arg 67. PMID: 12009884
  22. concentrations in nondialyzed chronic kidney disease patients, and the relationship with acidosis, zinc, anemia, and iron supplementation PMID: 14675565
  23. cytosolic CA I, II, and XIII are downregulated in neoplastic colorectal mucosa compared to normal colorectal mucosa PMID: 15836783
  24. Isothiocyanato sulfonamide thioureas inhibit this enzyme. PMID: 15837325
  25. X-ray crystallographic structure for the adduct of an activator with hCA I. Binding site interactions of activator L-Histidine with active site amino acids PMID: 16870440
  26. study presents the X-ray structure of the foscarnet adduct with CA1 together with the factors governing recognition of such small molecules by a metalloenzyme active site PMID: 17314045
  27. Decreased levels of carbonic anhydrase 1 isozyme is associated with type II diabetes. PMID: 17464559

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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