Recombinant Human APRT Protein

Name: Recombinant Human APRT Protein
Brand: Beta LifeScience
SKU: BLA-12187P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P07741
Synonym	Adenine phosphoribosyltransferase AMP AMP diphosphorylase AMP pyrophosphorylase APRT APT_HUMAN DKFZp686D13177 MGC125856 MGC125857 MGC129961 Transphosphoribosidase
Description	Recombinant Human APRT Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHL KATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWAS YSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEV LECVSLVELTSLKGREKLAPVPFFSLLQYE
Molecular Weight	20 kDa including tags
Purity	Greater than 90% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Please see notes section.

Target Details

Target Function	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Subcellular Location	Cytoplasm.
Protein Families	Purine/pyrimidine phosphoribosyltransferase family
Database References	HGNC: 626 OMIM: 102600 KEGG: hsa:353 STRING: 9606.ENSP00000367615 UniGene: Hs.28914
Associated Diseases	Adenine phosphoribosyltransferase deficiency (APRTD)

Gene Functions References

A long TA repeat in the promoter region of IL28B was associated with spontaneous HCV clearance. PMID: 25735432
A new mutation, p.Gln147X, in APRT gene, was found in a patient with adenine phosphoribosyltransferase deficiency. PMID: 24986359
Case study of 2 year old Japanese boy with APRT deficiency. Genetic analysis showed compound heterozygote APRT*J and missense mutation L33P. APRT deficiency should be suspected in patients with radiolucent kidney stones and urinary 2,8-DHA crystals. PMID: 21635362
kinetic, regulatory and thermostability properties of APRT from erythrocytes of HGPRT deficient patients PMID: 14674717
determination of structure and examination of role of deficiency in DHA-urolithiasis PMID: 15196008
two novel mutations, G133D and V84M, were found in the APRT gene in Japanese patients with APRT deficiency PMID: 15571218
APRT assay in a sample of patient hemolysate showed no detectable activity of the enzyme (25.56+/-9.55 U/L red blood cells in control healthy subjects). PMID: 17126311
Data indicates that the flexible loop structure adopts an open conformation before and after binding of both substrates adenine and phosphoribosyl pyrophosphate. PMID: 18399692
The phosphorylation status of membrane-bound nucleoside diphosphate kinase in epithelia and the role of AMP are reported. PMID: 19399589

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.