Recombinant Mouse Usherin (USH2A) Protein (His)

Name: Recombinant Mouse Usherin (USH2A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07072P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Mouse Usherin (USH2A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q2QI47
Target Symbol	USH2A
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	GRMQDFRLYNVSLTNREILEVFSGDFPHLHIQPHCRCPGSHPRVHPSVQQYCIPNGAGDTPEHRMSRLNPEAHPLSFINDDDVATSWISHVFTNITQLYEGVAISIDLENGQYQVLKVITQFSSLQPVAIRIQRKKADSSPWEDWQYFARNCSVWGMKDNEDLENPNSVNCLQLPDFIPFSHGNVTFDLLTSGQKHRPGYNDFYNSSVLQEFMRATQIRLHFHGQYYPAGHTVDWRHQYYAVDEIIVSGRCQC
Expression Range	265-517aa
Protein Length	Partial
Mol. Weight	33.3 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in hearing and vision as member of the USH2 complex. In the inner ear, required for the maintenance of hair bundle ankle formation, which connects growing stereocilia in developing cochlear hair cells. In retina photoreceptors, the USH2 complex is required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport.
Subcellular Location	Cell projection, stereocilium membrane; Single-pass type I membrane protein. Photoreceptor inner segment.; [Isoform 2]: Secreted.
Database References	KEGG: mmu:22283 STRING: 10090.ENSMUSP00000050454 UniGene: Mm.331238
Tissue Specificity	Present in the testis, epididymis, oviduct, spleen, submaxillary gland, and small and large intestines. Not detected in the brain, skin, lung, skeletal muscle, cardiac muscle, liver or kidney. Expressed in smooth muscle of the colon and the epididymis. Al

Gene Functions References

Expressed in the cells of the outer nuclear layer of the retina and in cochlea. PMID: 12160733
Conservation of usherin is seen at the nucleotide and amino acid level when comparing the mouse and human gene sequences. PMID: 12433396
Binding to fibronectin occurs at the LE domain of usherin. PMID: 16114888
In mouse inner ears usherin is present at the base of the differentiating stereocilia, which make up the mechanosensitive hair bundles receptive to sound PMID: 16301217
Whrn connects to the Usher protein network in the cochlea and retina by direct association with USH2A and VLGR1. PMID: 16434480
usherin in photoreceptors is tethered via its C terminus to the plasma membrane and its large extracellular domain projects into the periciliary matrix, where they may interact with the connecting cilium to fulfill important structural or signaling roles PMID: 17360538

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.