Recombinant Mouse UCHL1 Protein

Beta LifeScience SKU/CAT #: BL-4887PS

Recombinant Mouse UCHL1 Protein

Beta LifeScience SKU/CAT #: BL-4887PS
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 Mouse
Synonym Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1,Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Background UbiquitinCarboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose productshydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer.UCHL1 is a part of the ubiquitin system, which regulates many biologicalactivities. UCHL1 is a thiol protease that distinguishes and hydrolyzes apeptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitinand avoids its degradation in lysosomes.
Description UCHL1 Mouse Recombinant expressed in E.Coli is a single,non-glycosylated polypeptide chain containing 246a.a. (1-223a.a) andhaving a molecular weight of 27.2kDa.UCHL1 is fused to a 23a.a. His-tag at N-terminusand purified by unique purification methods.
Source E.coli
AA Sequence MGSSHHHHHH SSGLVPRGSH MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPACALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQFLSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGASSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.
Purity Greaterthan 90.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation UCHL1 protein solution (1mg/ml) containing Phosphatebuffered saline, 10% glycerol 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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