Recombinant Human NRN1L Protein (C-6His)

Name: Recombinant Human NRN1L Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0918NP
Availability: InStock

BL-0918NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Cytokines, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Neuritin-like Protein is produced by our Mammalian expression system and the target gene encoding Ala36-Ala139 is expressed with a 6His tag at the C-terminus.
Accession	Q496H8
Synonym	Neuritin-like protein; NRN1L; UNQ2446/PRO5725
Gene Background	Neuritin-like protein belongs to the neuritin family. Neuritin is a GPI-anchored protein that promotes neurite outgrowth and branching of neuritic processes in primary hippocampal and cortical cells. Neuritin expression also enhances the development of motor neuron axon arbors by promoting neuromuscular synaptogenesis and by stimulating the addition of new axon branches. Neuritin is induced by neuronal activity and by the neurotrophins, BDNF and NT3. NRN1L contains a consensus cleavage signal found in glycosylphoshatidylinositol (GPI)-anchored proteins.
Molecular Mass	12.3 KDa
Apmol Mass	14&16 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.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.