Recombinant Human Harmonin Protein (His Tag)

Name: Recombinant Human Harmonin Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2371
Availability: InStock

Collections: Other recombinant proteins, 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.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Human
Accession	Q9Y6N9
Synonym	AIE-75, DFNB18, DFNB18A, NY-CO-37, NY-CO-38, PDZ-45, PDZ-73, PDZ-73/NY-CO-38, PDZ73, PDZD7C, ush1cpst
Background	Harmonin, also known as Antigen NY-CO-38 / NY-CO-37, Autoimmune enteropathy-related antigen AIE-75, Protein PDZ-73, Renal carcinoma antigen NY-REN-3, Usher syndrome type-1C protein and USH1C, is a protein which is expressed in small intestine, colon, kidney, eye and weakly in pancreas. USH1C is expressed also in vestibule of the inner ear. USH1C contains 3PDZ (DHR) domains. USH1C may be involved in protein-protein interaction. Defects in USH1C are the cause of Usher syndrome type 1C (USH1C), also known as Usher syndrome type I Acadian variety. USH is a genetically heterogeneous condition characterized by the association of retinitis pigmentosa and sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). Defects in USH1C are also the cause of deafness autosomal recessive type 18 (DFNB18) which is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Description	A DNA sequence encoding the native human USH1C (Q9Y6N9-1) (Met 1-Phe 552) was expressed, with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1-Phe 552
Molecular Weight	The recombinant human USH1C consisting of 563 a.a. and migrates as an 63.7 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity	>92% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tris, 20% glycerol, pH 7.7.
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.

Target Details

Target Function	Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles. As part of the intermicrovillar adhesion complex/IMAC plays a role in brush border differentiation, controlling microvilli organization and length. Probably plays a central regulatory role in the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B to the microvilli tips.
Subcellular Location	Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell projection, microvillus.
Database References	HGNC: 12597 OMIM: 276900 KEGG: hsa:10083 STRING: 9606.ENSP00000005226 UniGene: Hs.502072
Associated Diseases	Usher syndrome 1C (USH1C); Deafness, autosomal recessive, 18A (DFNB18A)
Tissue Specificity	Expressed in small intestine, colon, kidney, eye and weakly in pancreas. Expressed also in vestibule of the inner ear.

Gene Functions References

Mutations of USHIC can cause both Usher syndrome type IC and nonsyndromic recessive deafness DFNB18. PMID: 12107438
The structure of the Myo7b CMF/USH1C PDZ complex provides mechanistic explanations for >20 deafness-causing mutations in Myo7a CMF. Taken together, these findings suggest that binding to PDZ domains, such as those from USH1C, PDZD7, and Whirlin, is a common property of CMFs of Myo7a, Myo7b, and Myo15a. PMID: 28439001
We found a remarkable genetic heterogeneity in the studied families with USH1 with a variety of mutations, among which three were novel. These novel mutations will be included in the NADf mutation screening chip that will allow a higher diagnosis efficiency of this extremely genetically heterogeneous disease. PMID: 27440999
Harmonin can adopt two different structural states, 'open' and 'closed', as a result of the self-interaction between its domains. PMID: 28653419
In summary, our studies provide novel insight into the functional relationship between USH1 and USH2 proteins in the cochlea and the retina as well as the disease mechanisms underlying USH1 and USH2. PMID: 28031293
ANKS4B, and MYO7B form a stable ternary complex for anchoring microvilli tip-link cadherins PMID: 26812017
harmonin and villin autoantibodies are sensitive and specific markers of IPEX, differentiate IPEX, including atypical cases, from other early childhood disorders associated with enteropathy PMID: 24250806
We localized proteins encoded by the top two regulated genes, TBL1X and USH1C, using immunohistochemistry to placental stem and anchoring villi associated with active contractile function. PMID: 23665419
Description of the spectrum of mutations in USHIC in 374 families with autosomal recessive, non-syndromic hearing loss from India. PMID: 24416283
This is the first report of a mutation in a known USH1 gene that causes late onset rather than congenital sensorineural hearing loss. PMID: 23251578
The data highlight the ability of ZFNs to induce targeted homologous recombination and mediate gene repair in USH. PMID: 22661463
Large protein assemblies formed by multivalent interactions between cadherin23 and harmonin suggest a stable anchorage structure at the tip link of stereocilia PMID: 22879593
Pathogenic mutations in MYO7A, USH1C, and USH1G have been found in four consanguineous Israeli Arab families with Usher syndrome type 1. PMID: 22219650
We report a novel molecular cause of sector retinitis pigmentosa associated with hearing loss representing a new phenotype associated with mutations in the USH1C gene. PMID: 21487335
Mutations in USH1C are responsible for 1.5% of Usher syndrome type I disease in patients of Spanish origin. PMID: 21203349
Mutations in harmonin and Sans found in USH1 patients are shown to destabilize the complex formation of the two proteins PMID: 20142502
USH1C 216G-->A mutation and the 9-repeat VNTR(t,t) allele are in complete linkage disequilibrium in the Acadian population PMID: 11810303
Mutations in the alternatively spliced exons of USH1C cause non-syndromic recessive deafness. PMID: 12136232
the shaping of the hair bundle relies on a functional unit composed of myosin VIIa, harmonin b and cadherin 23 that is essential to ensure the cohesion of the stereocilia PMID: 12485990
the instability of the USH1C mRNA is explained by the 216G-->A out-of-frame splice site mutation. PMID: 15578223
The c.216G>A mutation within the USH1C gene has been linked to a founder effect within the French Canadian population of Quebec associated with deafblindness. PMID: 17407589
The structures of the harmonin N-domain alone and in complex with the cadherin 23 internal peptide fragment uncovered the detailed binding mechanism of this interaction between harmonin and cadherin 23. PMID: 19297620
Observational study of gene-disease association and genetic testing. (HuGE Navigator) PMID: 19683999

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.