Recombinant Human HPRT1 Protein, Active

Beta LifeScience SKU/CAT #: BL-1992PS

Recombinant Human HPRT1 Protein, Active

Beta LifeScience SKU/CAT #: BL-1992PS
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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag N/A
Host Species Human
Synonym Hypoxanthine Phosphoribosyltransferase 1, EC 2.4.2.8, HGPRTase, HGPRT, HPRT , Hypoxanthine-Guanine Phosphoribosyltransferase 1, Hypoxanthine-Guanine Phosphoribosyltransferase, Testicular Tissue Protein Li 89, Lesch-Nyhan Syndrome, HPRT1.
Background HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.
Description HPRT1 Human Recombinant expressed in E.Coli is a single, non-glycosylated polypeptide chain containing 238a.a. (1-218 a.a) and having a molecular weight of 26.7kDa. HPRT1 is fused to a 20a.a. His-tag at N-terminus and purified by unique purification methods.
Source E.coli
AA Sequence MGSSHHHHHH SSGLVPRGSH MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV
Purity >95.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Bioactivity Specific activity is > 15 units/mg and is defined as the amount of enzyme that catalyze the formation of 1 umole of guanosine 5'-monophosphate (GMP) per minute from guanine and phosphoribosyl pyrophosphate at pH 7.5 at 37C.
Formulation HPRT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed