Recombinant Human NRXN3 Protein (His Tag)

Name: Recombinant Human NRXN3 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3569
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NP_620426.2
Synonym	C14orf60
Background	Neurexin-3-beta, also known as Neurexin III-beta and NRXN3, is a single-pass type I membrane protein which belongs to theneurexin family. It contains onelaminin G-like domain. It is a neuronal cell surface protein that may be involved in cell recognition and cell adhesion. Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two, NRXN1 and NRXN3, are among the largest known human genes. Three of the genes ( NRXN1, NRXN2, NRXN3 ) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain EGF-like sequences and laminin G domains, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins. NRXN3 have been linked to genetic predisposition towards a number of conditions such as alcohol or drug addiction, or obesity.
Description	A DNA sequence encoding the human NRXN3 beta isoform 2 (NP_620426.2) extracellular domain (Met 1-Thr 357) was expressed, with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Ser 36
AA Sequence	Met 1-Thr 357
Molecular Weight	The recombinant human NRXN3 consists of 333 a.a. and predictes a molecular mass of 36 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhNRXN3 is approximately 50-60 kDa due to glycosylation.
Purity	>94% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by the ability of the immobilized protein to support the adhesion of C6 Rat brain glial cells. When 5 x 10E4 cells/well are added to NRXN3 coated plates (0.8 ug/ml and 100 ul/well), approximately 30%-50% will adhere specifically after 60 minutes at 37 °C.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated 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.