Human CETN2 (Centrin-2) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-00569P
SDS-PAGE analysis of Human CETN2 (Centrin-2) - Recombinant Protein, CAT
SDS-PAGE analysis of Human CETN2 (Centrin-2) - Recombinant Protein, CAT# BLT-00569P, showing >85% purity under 15% SDS-PAGE (Reduced)

Human CETN2 (Centrin-2) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-00569P
Regular price $595.00 Sale price $445.00Save $150
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Pack Size Price (USD)
500 µg $1,030 (Fall Promotion)
1 mg $1,870 (Fall Promotion)

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Product Overview

Product Name Recombinant Human CETN2 Protein
Product Overview This recombinant human CETN2 protein includes amino acids 1-172aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id P41208
Recommended Name Centrin-2
Gene Name CETN2
Synonyms Caltractin, CALT, CEN2, Centrin-2
Species Human
Predicted Molecular Mass 21.9 kDa
Expression System E.coli
Expression Range 1-172aa
Tag N-6His
Purity >85%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 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.
Reconstitution Instruction 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%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Cell Cycle
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 Family Centrin family

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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