Recombinant Human Centrin-2 (CETN2) Protein (His-SUMO)

Name: Recombinant Human Centrin-2 (CETN2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10003P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Centrin-2 (CETN2) 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	P41208
Target Symbol	CETN2
Synonyms	20kD calcium binding protein; CALT; caltractin; Caltractin isoform 1; CEN2; centrin; centrin; EF hand protein; 2 ; Centrin-2; Centrin2; CETN2; CETN2_HUMAN; EF hand protein 2; EF-hand protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY
Expression Range	1-172aa
Protein Length	Full Length
Mol. Weight	35.7kDa
Research Area	Cell Cycle
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	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	HGNC: 1867 OMIM: 300006 KEGG: hsa:1069 STRING: 9606.ENSP00000359300 UniGene: Hs.82794

Gene Functions References

Multidisciplinary approach showed that HsPrp40Ap interacts with centrin in vitro, supporting a coupled functional role for these proteins in pre-mRNA splicing. PMID: 28636910
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
Centrin2 regulates primary ciliogenesis through controlling CP110 levels. PMID: 25753040
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
Data indicate that overexpression of the centrin interactor POC5 leads to the assembly of linear, centrin-dependent structures. PMID: 23844208
Cen2 influences the binding of RPA and XPA with damaged DNA. PMID: 22809153
xeroderma pigmentosum complementation group C expression correlates with a decreased amount of CENTRIN 2 transcript and protein PMID: 21676658
The stability of centrin is regulated in part by Aurora A. PMID: 21731694
Mps1-dependent phosphorylation of Cetn2 stimulates the canonical centriole assembly pathway. PMID: 20980622
oxidative radicals induce high proportions of irreversible damages (polymerisation) centrin 2 is highly sensitive to ionising radiation. PMID: 20586543
required for centriole duplication in mammalian cells PMID: 12176356
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
structural characterization of the complex formed by the C-terminal domain of Cen2 with a peptide of xeroderma pigmentosum group C protein PMID: 12890685
Results describe the self-assembly properties of purified human centrin-2 in vitro. PMID: 15356003
Centrin 2 stimulates nucleotide excision repair by interacting with XPC. PMID: 15964821
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
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
A complex formed by a Ca2+-bound human centrin 2 with a 17-mer peptide derived from the XPC sequence was crystallized. PMID: 16820684
Centrin 2 is highly sensitive to ionizing radiation, which could have important consequences on its biological functions. PMID: 17603931
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
CETN2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export. PMID: 18172010
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
lower centrin levels in oligoasthnozoospermic males resulted in lower pregnancy percentage in this group after ICSI. PMID: 19179680
The nucleocytoplasmic shuttling of centrin-2 depends on the SUMO system. PMID: 19706679
The structure of C-HsCen2 [the C-terminal domain of HsCen2 (T94-Y172)] in complex with R17-hSfi1-20 was determined. PMID: 19857500

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.