Recombinant Human ADPRH Protein (N-6His)

Name: Recombinant Human ADPRH Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1480NP
Availability: InStock

BL-1480NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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

Description	Recombinant Human ADP-Ribosylarginine Hydrolase is produced by our E.coli expression system and the target gene encoding Met1-Leu357 is expressed with a 6His tag at the N-terminus.
Accession	P54922
Synonym	[Protein ADP-Ribosylarginine] Hydrolase; ADP-Ribosylarginine Hydrolase; ADP-Ribose-L-Arginine Cleaving Enzyme; ADPRH; ARH1
Gene Background	ADP-Ribosylarginine Hydrolase (ADPRH) belongs to the ADP-Ribosylglycohydrolase family. ADPRH catalyzes removal of mono-ADP-ribose from arginine residues of proteins in the ADP-Ribosylation cycle, which is a post-translation modification that includes the addition of one or more ADP-ribose moieties. These reactions are related to cell signaling and the control of many cell processes, such as DNA repair and cell apoptosis. In addition, ADPRH binds with magnesium ion and possess ADP-ribosylarginine hydrolase activity.
Molecular Mass	41.67 KDa
Apmol Mass	39 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 50% Glycerol, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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.