Recombinant Human Centrin 2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1218

Recombinant Human Centrin 2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1218
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Product Overview

Tag His
Host Species Human
Accession P41208
Synonym CALT, CEN2
Description A DNA sequence encoding the human CETN2 (P41208) (Met1-Tyr171) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal His
AA Sequence Met1-Tyr171
Molecular Weight The recombinant human CETN2 consists of 187 a.a. and predicts a molecular mass of 21.6 KDa. It migrates as an approximately 21 KDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
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 Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.; Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.; As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores.
Subcellular Location Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus envelope. Nucleus, nuclear pore complex. Nucleus.
Protein Families Centrin family
Database References

Gene Functions References

  1. Multidisciplinary approach showed that HsPrp40Ap interacts with centrin in vitro, supporting a coupled functional role for these proteins in pre-mRNA splicing. PMID: 28636910
  2. Cetn3 inhibits Mps1 autophosphorylation at Thr-676, a known site of T-loop autoactivation, and interferes with Mps1-dependent phosphorylation of Cetn2. The cellular overexpression of Cetn3 attenuates the incorporation of Cetn2 into centrioles and centrosome reduplication, whereas depletion of Cetn3 generates extra centrioles. PMID: 26354417
  3. Centrin2 regulates primary ciliogenesis through controlling CP110 levels. PMID: 25753040
  4. co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export, indicating the dominance of the centrin 2 phenotype. PMID: 24291146
  5. Data indicate that overexpression of the centrin interactor POC5 leads to the assembly of linear, centrin-dependent structures. PMID: 23844208
  6. Cen2 influences the binding of RPA and XPA with damaged DNA. PMID: 22809153
  7. xeroderma pigmentosum complementation group C expression correlates with a decreased amount of CENTRIN 2 transcript and protein PMID: 21676658
  8. The stability of centrin is regulated in part by Aurora A. PMID: 21731694
  9. Mps1-dependent phosphorylation of Cetn2 stimulates the canonical centriole assembly pathway. PMID: 20980622
  10. oxidative radicals induce high proportions of irreversible damages (polymerisation) centrin 2 is highly sensitive to ionising radiation. PMID: 20586543
  11. required for centriole duplication in mammalian cells PMID: 12176356
  12. The solution structure of the long C-terminal fragment of centrin 2 exhibits an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. PMID: 12578356
  13. structural characterization of the complex formed by the C-terminal domain of Cen2 with a peptide of xeroderma pigmentosum group C protein PMID: 12890685
  14. Results describe the self-assembly properties of purified human centrin-2 in vitro. PMID: 15356003
  15. Centrin 2 stimulates nucleotide excision repair by interacting with XPC. PMID: 15964821
  16. an 18-residue peptide, from the N-terminal unstructured fragment, has a significant affinity for the isolated C-terminal domain, suggesting an active role in the self-assembly of centrin molecules. PMID: 16411764
  17. the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide; a novel binding motif for centrin PMID: 16627479
  18. A complex formed by a Ca2+-bound human centrin 2 with a 17-mer peptide derived from the XPC sequence was crystallized. PMID: 16820684
  19. Centrin 2 is highly sensitive to ionizing radiation, which could have important consequences on its biological functions. PMID: 17603931
  20. The present data confirm that the in vitro structural features of the centrin/XPC peptide complex are highly relevant to the cellular context. PMID: 17897675
  21. CETN2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export. PMID: 18172010
  22. NMR analysis indicates that the physical interaction between C-XPC and centrin 2 induces only minor conformational changes into XPC, localized around the 17-mer segment (847-863), showed to be critically involved in the centrin binding. PMID: 18177054
  23. lower centrin levels in oligoasthnozoospermic males resulted in lower pregnancy percentage in this group after ICSI. PMID: 19179680
  24. The nucleocytoplasmic shuttling of centrin-2 depends on the SUMO system. PMID: 19706679
  25. The structure of C-HsCen2 [the C-terminal domain of HsCen2 (T94-Y172)] in complex with R17-hSfi1-20 was determined. PMID: 19857500


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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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