Recombinant Human Harmonin (USH1C) Protein (His-SUMO)

Name: Recombinant Human Harmonin (USH1C) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03090P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Harmonin (USH1C) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y6N9
Target Symbol	USH1C
Synonyms	AIE 75; AIE75; Antigen NY CO 38/NY CO 37; Antigen NY-CO-38/NY-CO-37; Autoimmune enteropathy related antigen AIE 75; Autoimmune enteropathy related antigen AIE75; Autoimmune enteropathy-related antigen AIE-75; Deafness autosomal recessive 18; DFNB 18; DFNB18; Harmonin; NY CO 37; NY CO 38; PDZ 45; PDZ 73; PDZ 73 protein; PDZ 73/NY CO 38; PDZ45; PDZ73; PDZ73 protein; Protein PDZ-73; Renal carcinoma antigen NY REN 3; Renal carcinoma antigen NY-REN-3; USH 1C; USH1C; USH1C_HUMAN; Ush1cpst; Usher syndrome 1C (autosomal recessive severe); Usher syndrome 1C; Usher syndrome type 1C protein; Usher syndrome type-1C protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MDRKVAREFRHKVDFLIENDAEKDYLYDVLRMYHQTMDVAVLVGDLKLVINEPSRLPLFDAIRPLIPLKHQVEYDQLTPRRSRKLKEVRLDRLHPEGLGLSVRGGLEFGCGLFISHLIKGGQADSVGLQVGDEIVRINGYSISSCTHEEVINLIRTKKTVSIKVRHIGLIPVKSSPDEPLTWQYVDQFVSESGGVRGSLGSPGNRENKEKKVFISLVGSRGLGCSISSGPIQKPGIFISHVKPGSLSAEVGLEIGDQIVEVNGVDFSNLDHKEGRELFMTDRERLAEARQRELQRQELLMQKRLAMESNKILQEQQEMERQRRKEIAQKAAEENERYRKEMEQIVEEEEKFKKQWEEDWGSKEQLLLPKTITAEVHPVPLRKPKYDQGVEPELEPADDLDGGTEEQGEQDFRKYEEGFDPYSMFTPEQIMGKDVRLLRIKKEGSLDLALEGGVDSPIGKVVVSAVYERGAAERHGGIVKGDEIMAINGKIVTDYTLAEAEAALQKAWNQGGDWIDLVVAVCPPKEYDDELTFF
Expression Range	1-533aa
Protein Length	Full Length of Isoform 4
Mol. Weight	76.3kDa
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	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: 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

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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.