Recombinant Human Carbonic Anhydrase 2 (CA2) Protein (His-SUMO)

Name: Recombinant Human Carbonic Anhydrase 2 (CA2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04331P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Carbonic Anhydrase 2 (CA2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00918
Target Symbol	CA2
Synonyms	CA 2; CA II; CA-II; Ca2; CAC; CAH2_HUMAN; CAII; Car 2; Car2; Carbonate dehydratase II; Carbonic anhydrase 2; Carbonic anhydrase B; Carbonic anhydrase C; Carbonic anhydrase C; formerly; Carbonic anhydrase II; Carbonic dehydratase; epididymis luminal protein 76; Epididymis secretory protein Li 282; HEL-76; HEL-S-282
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFAARGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Expression Range	2-260aa
Protein Length	Full Length of Mature Protein
Mol. Weight	45.1 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.
Subcellular Location	Cytoplasm. Cell membrane. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells.
Protein Families	Alpha-carbonic anhydrase family
Database References	HGNC: 1373 OMIM: 259730 KEGG: hsa:760 STRING: 9606.ENSP00000285379 UniGene: Hs.155097
Associated Diseases	Osteopetrosis, autosomal recessive 3 (OPTB3)

Gene Functions References

CAII, CAIX, and CAXII all have characteristic expression patterns in esophageal adenocarcinoma (EAC), its precursors and normal squamous epithelium. In EAC, CAII downregulation is associated with metastatic disease. CAIX expression is lost towards the more malignant lesions, but in lymph node positive disease, expression seems to be higher. CAXII is only expressed in normal esophageal epithelium. PMID: 30066203
present results suggest that CA2 serves as a suppressor of hepatocellular carcinoma metastasis and epithelial-mesenchymal transition and is correlated with favorable overall survival (OS) in hepatocellular carcinoma patients. PMID: 29309535
The LC/MS analysis of platelet proteome between groups revealed that out of all identified proteins, the only discriminatory protein, affecting aspirin responsiveness, is platelet carbonic anhydrase II (CA II). PMID: 29090039
Study presented a detailed analysis of how protein dynamics (specifically the motions of nonreactive residues in the active site and coupled solvent dynamics) influence the rate limiting proton transfer/transport event in HCA II. PMID: 27063577
This study provides the first evidence that extra-platelet nitrite and erythrocytic CAII may modulate platelet function in a cGMP-dependent manner. PMID: 27129464
CA II and CA XII, but not CA VII or CA IX, could be useful in predicting survival in colorectal carcinomas PMID: 27688658
compute the hydration free energy of Zn(2+), the characteristics of hCAII-Zn(2+) complexation, and the absolute free energy of binding acetazolamide to the hCAII-Zn(2+) co PMID: 27232456
This article presents different classes of structures of the mutant His-107-Tyr of human CA-II by harvesting molecular dynamics trajectories at low and high temperatures. Identified are putative unfolding intermediates of the mutant His-107-tyr of human carbonic anhydrase II in a multidimensional property space. PMID: 26756542
The levels of expression of carbonic anhydrase 2, catalase, and PRDX2 in the nipple discharge were significantly increased in breast ductal carcinoma patients as compared to controls. PMID: 26970563
This study suggests that the expression of CA II acts as independent prognostic biomarker for survival in pseudomyxoma peritonei PMID: 28233447
Changes in membrane composition may affect the erythrocyte membranes' capacity to increase in vitro hCA II activity PMID: 26698855
identified 2 novel mutations in 2 Chinese families with CAII deficiency syndrome; a nonsense mutation in exon 4 in both families; a splice mutation at the splice donor site of intron 3 in 1 family; the splice-site mutation causes exon 3 skipping in patient's mRNA resulting in an in-frame deletion and a novel premature stop codon PMID: 25720518
binding of dorzolamide to bovine and human carbonic anhydrase II PMID: 26093313
Using paramagnetic NMR techniques and X-ray absorption spectroscopy we identified an N-terminal Cu(2+) binding site in carbonic anhydrase II. PMID: 26010488
CAII increases water conductance through AQP1 by a physical interaction between the two proteins. PMID: 25609088
carbonic anhydrase catalytic cycle for natural and promiscuous substrates PMID: 25849760
Suggest an association between CAII and NHE3 that alters the transporter's activity in kidney cell line. PMID: 26041446
The down-regulation of CA II expression was observed in gastric cancer and may serve as an independent prognostic factor for the overall survival of gastric cancer patients. PMID: 25400751
Binding of cyanate to CA II is directly to the zinc, displacing the zinc-bound solvent molecule, and not in a site that overlaps with the CO2 substrate-binding site. PMID: 25286933
Carbonic anhydrase II may play a critical role in neuroendocrine tumor lung tumor growth PMID: 25019941
the pHi of cells with low CAi activity was less responsive to pCO2 fluctuations. Such low pass filtering would "buffer" cancer cell pHi from non-steady-state extracellular pCO2. Thus PMID: 25059669
Our study suggests that the exposed hydrophobic surface and/or the disruption of the structural features protecting a beta-sheet protein might be the major reason(s) for the high aggregation propensity of non-native intermediate conformation of HCAII. PMID: 24813993
sclerostin upregulated osteocyte expression of carbonic anhydrase 2. PMID: 23737439
Expression of carbonic anhydrase II in SaOS-2 cells after incubation with bicarbonate increased. PMID: 23953824
these data suggest that CA II may be a potential biomarker for early diagnosis of colorectal cancer and the results may contribute to a better understanding of the molecular mechanism of colorectal cancer and colorectal cancer treatment. PMID: 23727877
Carbonic anhydrase II and Ki-67 are significant prognostic factors for gastrointestinal stromal tumors. PMID: 23674848
role of aromatic cluster in stability and function PMID: 24036123
An interactive human carbonic anhydrase-II (hCA-II) receptor--pharmacophore molecular model & anti-convulsant activity of the designed and synthesized 5-amino-1,3,4-thiadiazole-2-thiol conjugated imine derivatives. PMID: 23360090
Molecular modeling of the structure and possible proton transfer pathways from the surface of the protein to the zinc-bound water molecule in the active site of the mutant His-107-Tyr of human carbonic anhydrase, is presented. PMID: 22878862
The rate constants for transfer of a proton from His64 to the zinc-bound hydroxide during catalysis were 4 and 9 mus(-1) for Y7F and Y7F/N67Q, respectively, compared with a value of 0.8 mus(-1) for wild-type CAII. PMID: 23215152
reconstitution of the zinc active site of human CA II PMID: 23030313
data suggest that the Ile substitution at position 143 reduced the catalytic efficiency, likely due to steric crowding resulting in destabilization of the transition state for conversion of CO(2) into bicarbonate and a decreased product dissociation rate. PMID: 23098192
A significant correlation was found between positive carbonic anhydrase II 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
pKa shifts of zinc-bound water due to mutations of CA II active site support conclusion that changes in conformation and electronic polarization of mutated active sites account for altered deprotonation behavior of zinc-bound water. PMID: 22732064
study reports the catalytic properties of three hCA II mutants (Asn67Ile, Gln92Val and Leu204Ser) and the inhibition of these enzymes; small perturbations within the active site architecture have influences on the catalytic efficiency but dramatically change affinity for inhibitors among the CA enzymes PMID: 22386980
Studies indicate that cytosolic isoform carbonic anhydrase II (hCA II) was very weakly inhibited by the aliphatic, C1-C5 carboxylates as well as by branched aliphatic ones. PMID: 22192857
The apparent values of the pK(a) of the zinc-bound water and the proton shuttle residue suggest that different active-site conformations influence the two stages of catalysis, the proton transfer stage and the interconversion of CO(2) and bicarbonate. PMID: 22001224
Detailed analysis and comparison to the previously determined structure of CAII at pH 10.0 show important differences in protonation of key catalytic residues in the active site as well as a rearrangement of the hydrogen-bonded water network. PMID: 21988105
The expression of CA2 is significantly increased in the spermatozoa of asthenozoospermic men, which might be responsible for low sperm motility. PMID: 21243755
data suggest that extracellular membrane-bound CAIV, but not cytosolic CAII, augments transport activity of MCT2 in a non-catalytic manner, possibly by facilitating a proton pathway other than His-88 PMID: 21680735
Data suggest that association of functional CAII with AE1 increases Cl(-)/HCO(3)(-) exchange activity, consistent with the HCO(3)(-) transport metabolon model. PMID: 21543742
The H(+) shuttle in CAII not only facilitates CAII catalytic activity but also can enhance activity of acid-/base-transporting proteins such as MCT1/4 in a direct, noncatalytic manner, possibly by acting as an "H(+)-collecting antenna." PMID: 21282642
The side chain of Tyr7 in CA II extends into the active-site cavity about 7 A from the catalytic zinc atom. Replacement of Tyr7 with eight other amino acids had no effect on the interconversion of bicarbonate and CO2. PMID: 21145876
plasma level of CAII was significantly increased in Alzheimer disease patients, providing further evidence that changes in CAII level may play a role in the pathogenesis of Alzheimer disease. PMID: 20634585
The visible absorption of crystals of Co(II)-substituted carbonic anhydrase II were measured over a pH range of 6.0-11.0 giving an estimate of pK(a) 8.4 for the ionization of the metal-bound water in the crystal. PMID: 20637176
structure of Car2 has been redetermined, with the coordinates of both pseudo-symmetrically related molecules in the crystallographic asymmetric unit translated by x' = x +/- 1/4, and no rotational disorder is observed PMID: 20693695
our results imply that CA2 and CA12 are highly over-expressed in advanced atherosclerosis by osteoclast-like cells of monocytic origin PMID: 20509747
the active site of HCA II is extended to include residues that, at first glance, appear to be too far from the zinc to exert any catalytic effects PMID: 20578724
Report carbonic anydrase II expression in medulloblastomas and supratentorial primitive neuroectodermal tumours. PMID: 20398423
CA II is overexpressed in most gastrointestinal stromal tumors, is quite selective to this tumor type among mesenchymal tumors, and therefore might be a useful biomarker in diagnostics PMID: 20081808

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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.

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