Recombinant Human CANT1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0540

Recombinant Human CANT1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0540
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Product Overview

Tag His
Host Species Human
Accession Q8WVQ1
Synonym DBQD, SCAN-1, SCAN1, SHAPY
Background CANT1(calcium activated nucleotidase 1) belongs to the apyrase family. Apyrase is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP: ADP and another with no selectivity. It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate. CANT1 functions as a calcium-dependent nucleotidase with a preference for UDP. Defects in CANT1 are the cause of desbuquois dysplasia.
Description A DNA sequence encoding the human CANT1 (Q8WVQ1-1) extracellular domain (Gly 80-Ile 401) was fused with His tag at the N-terminus.
Source HEK293
Predicted N Terminal His
AA Sequence Gly 80-Ile 401
Molecular Weight The recombinant human CANT1 consists of 342 a.a. and has a calculated molecular mass of 38 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh CANT1 is approximately 40kDa.
Purity >88% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.
Subcellular Location Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Cell membrane. Note=Processed form: Secreted.
Protein Families Apyrase family
Database References
Associated Diseases Desbuquois dysplasia 1 (DBQD1); Epiphyseal dysplasia, multiple, 7 (EDM7)
Tissue Specificity Widely expressed.

Gene Functions References

  1. CANT1 long non-coding RNA triggers efficient therapeutic efficacy by correcting aberrant long non-coding cascade in malignant uveal melanoma. PMID: 28330694
  2. The Multiple Epiphyseal Dysplasia (MED)phenotype is thus allelic to the more severe Desbuquois dysplasia phenotype and the results identify CANT1 as a second locus for recessively inherited MED PMID: 28742282
  3. a novel mutation of CANT1, c.467C>T (p.Ser156Phe) in 3 Indian patients with Desbuquois dysplasia, Kim type from 2 families PMID: 25486376
  4. Data studied proteoglycan synthesis in CANT1 mutated patient fibroblasts, and found significant reduced GAG synthesis in presence of beta-D-xyloside, suggesting that CANT1 plays a role in proteoglycan metabolism. PMID: 22539336
  5. Novel mutations in the CANT1 gene are reported in three cases of Desbuquois dysplasia type I and fetal hydrops. PMID: 21654728
  6. estimated the age of the founder mutation as approximately 1420 years PMID: 21412251
  7. CANT1 is commonly overexpressed in the vast majority of primary prostate carcinomas and in the precursor lesion PIN and may represent a novel prognostic biomarker PMID: 21435463
  8. The clinical-radiographic spectrum produced by CANT1 mutations must be extended to include Desbuquois dysplasia type 2 and Kim variant. PMID: 21037275
  9. Cloning, expression, and characterization of this calcium-acdtivated enzyme, a human enzyme belonging to a new family of extracellular nucleotidases. PMID: 12234496
  10. This soluble apyrase is a calcium-binding protein, as evident from saturable Ca2+-dependent changes in intrinsic tryptophan fluorescence, UV difference absorption spectra, and Ca2+-triggered transition from enzymatically inactive form to active enzyme. PMID: 12600208
  11. The importance of the dimeric state for enzymatic activity and biological function in this nucleotidase by mutating isoleucine 170, is investigated. PMID: 18067325
  12. human soluble calcium-activated nucleotidase inhibits coagulation in vitro and thrombosis in vivo PMID: 18222531
  13. The two novel ETV4 fusion partners possess as predominant common characteristics androgen-induction and prostate-specific expression. PMID: 18451133
  14. Mutations in CANT1 in Desbuquois dysplasia are identified. PMID: 19853239

FAQs

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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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