Recombinant Human RBM8A Protein

Beta LifeScience SKU/CAT #: BL-4556PS

Recombinant Human RBM8A Protein

Beta LifeScience SKU/CAT #: BL-4556PS
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag N/A
Host Species Human
Synonym RNA-binding protein 8A, Binder of OVCA1-1, BOV-1, RNA-binding motif protein 8A, RNA-binding protein Y14, Ribonucleoprotein RBM8A, RBM8A, RBM8, Y14, ZNRP, RBM8B, ZRNP1, BOV-1A, BOV-1B, BOV-1C, MDS014.
Background RBM8A belongs to the EJC (The exon junction complex) which is involved in mRNA export, cytoplasmic localization and nonsense mediated mRNA decay. RBM8A is able to communicate to the cytoplasm the processing history of the mRNA, including the position of the removed introns. Even though RBM8A shuttles to the cytoplasm, it is mostly detected in the nucleus and is colocalized with oskar mRNA at the posterior pole of the cell.
Description RBM8A expressed in E.Coli is a single, non-glycosylated polypeptide chain containing 182a.a. (1-174 a.a.) and having a molecular weight of 20.9kDa.RBM8A is fused to an 8a.a. His-tag at C-terminus and purified by unique purification methods.
Source E.coli
AA Sequence MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRRLEHHHH HH.
Purity >90.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation The RBM8A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

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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