Recombinant Human Unconventional Myosin-Viia (MYO7A) Protein (His-SUMO)

Name: Recombinant Human Unconventional Myosin-Viia (MYO7A) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08868P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Unconventional Myosin-Viia (MYO7A) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13402
Target Symbol	MYO7A
Synonyms	MYO7A; USH1B; Unconventional myosin-VIIa
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	WAVLTVQAYARGMIARRLHQRLRAEYLWRLEAEKMRLAEEEKLRKEMSAKKAKEEAERKHQERLAQLAREDAERELKEKEAARRKKELLEQMERARHEPVNHSDMVDKMFGFLGTSGGLPGQEGQAPSGFE
Expression Range	838-968aa
Protein Length	Partial
Mol. Weight	31.3kDa
Research Area	Signal Transduction
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	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. In the retina, plays an important role in the renewal of the outer photoreceptor disks. Plays an important role in the distribution and migration of retinal pigment epithelial (RPE) melanosomes and phagosomes, and in the regulation of opsin transport in retinal photoreceptors. In the inner ear, plays an important role in differentiation, morphogenesis and organization of cochlear hair cell bundles. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity. Motor 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 hearing.
Subcellular Location	Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell junction, synapse.
Protein Families	TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
Database References	HGNC: 7606 OMIM: 276900 KEGG: hsa:4647 STRING: 9606.ENSP00000386331 UniGene: PMID: 29400105 We report here novel homozygous mutations in various genes causing USH, extending the spectrum of causative mutations. We also prove combined sequencing techniques as useful tools to identify novel disease-causing mutations. To the best of our knowledge, this is the largest report of a genetic analysis of Israeli and Palestinian families (n = 74) with different USH subtypes. PMID: 29490346 This study extends the spectrum of known MYO7A mutations and proves next generation sequencing as a valuable tool in molecular diagnosis of Usher syndrome. PMID: 29605349 These findings broaden the phenotype spectrum of the MYO7A gene, and may facilitate understanding of the molecular pathogenesis of the disease, and genetic counseling for the family. PMID: 28731162 a novel stop gained variant c.4513G > T (p.Glu1505Ter) in MYO7A was found in an Iranian pedigree with two affected members with USH type 1 PMID: 29287847 Two pathogenic variations (c.849+2T>C and c.5994G>A) in MYO7A were successfully identified and individually separated from parents PMID: 29287864 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 Patients carrying mutations in MYO7A had a younger age of onset of hearing and visual impairments than those carrying mutations in USH2A, leading to an earlier diagnosis of the disease in the former patients. PMID: 27828912 We suggest that this new mutation named c.6079_6081del (p.H2027del) is the main cause of deaf-blindness found in this family clinically diagnosed as USH1B. PMID: 26864046 Results show the structures of Myo7a IQ5-SAH (single a helix) lever arm extension in complex with apo- and Ca2+-CaM, respectively, reveal that the motor contains an extended and rigid lever arm at low Ca2+ concentration conditions. Increased cellular Ca2+ concentration induces conformational flexibility of the motor and thus regulates its activity. PMID: 28262393 novel mutation c.3847_3848insTCTG (p. N1285LfsX24) in compound heterozygosity with c.2239_2240delAG in the MYO7A gene is the main cause of USH1 in the proband PMID: 28688563 report the results of genetic analyses performed on Moroccan families with autosomal recessive non syndromic hearing loss that identified two families with compound heterozygous MYO7A mutations PMID: 28472130 myosin VIIa movement appears to be suitable for translocating USH1 proteins on stereocilia actin bundles in inner-ear hair cells PMID: 28507101 In USH1B-MYO7A, constriction rate of EZ extent depends on the initial eccentricity of the transition. Ellipsoid zone edges in the macula correspond to large local changes in cone vision, but extramacular EZ edges show more pronounced losses on rod-based vision tests. PMID: 27409480 An unreported splice site mutation c.3924+1G > C compound with c.6028G > A in the MYO7A gene were detected to cosegregate with Usher syndrome type 2 in a Han Chinese family. PMID: 27729122 There are more than 39 deafness genes reported to cause non-syndromic hereditary hearing loss (HHL) in Iran, of which the most prevalent causative genes include GJB2, SLC26A4, MYO15A, and MYO7A. In addition, we highlight some of the more common genetic causes of syndromic HHL in Iran. [review] PMID: 27743438 This study showed that Mendelian sensorineural hearing loss exhibits vestibular dysfunction, including DFNA9, DFNA11, DFNA15 and DFNA28. PMID: 27083884 The novel compound heterozygous mutations (c.3671C>A and c.390_391insC) in MYO7A gene identified in this study were responsible for the autosomal recessive sensorineural hearing loss of this Chinese family PMID: 26968074 MYO7A binds to and impinges on CASPASE-8, revealing a new regulatory axis affecting RIPK1>CASPASE-8 signaling. Results expose a conserved role for unconventional myosins in transducing caspase-dependent regulation of kinases. PMID: 26960254 The genetic correction of MYO7A mutation resulted in morphologic and functional recovery of hair cell-like cells derived from induced pluripotent stem cells from a deaf patient. PMID: 27013738 c.6377delC mutation in significant proportion of Usher syndrome in indigenous South Africans PMID: 26469752 Ten variants in the MYO7A gene and 34 variants in the USH2A gene were detected in Italian patients with Usher syndrome at a high detection rate. PMID: 25558175 concluded that the USH1 in this family was caused by compound heterozygous mutations in MYO7A PMID: 25080338 Electron microscopy revealed that myosin VIIA is a monomer in which the tail domain bends back toward the head-neck domain to form a compact structure. This compact structure is extended at high ionic strength or in the presence of Ca(2+). PMID: 26001786 Clinical phenotypes of Usher syndrome associated with MYO7A mutations. PMID: 24831256 The MYO7A gene is responsible for two distinct diseases and gives evidence that the p.P1887L mutation in a homozygous state may be responsible for nonsyndromic hearing loss. PMID: 24194196 new variants in genes such as MYO7A is associated with nonsyndromic deafness and vestibular dysfunction PMID: 24275721 Data indicate that that CIB2 localizes to stereocilia and interacts with the USH proteins myosin VIIa and whirlin, suggesting CIB2 is a Ca2+-buffering protein essential for calcium homeostasis in the mechanosensory stereocilia of inner ear hair cells. PMID: 24022220 Data show that AAV-mediated hMYO7A gene transfer to the mice sh1(-/-) retina is effective. PMID: 23991031 MYO7A-related ocular disease is variable. Central vision typically remains preserved at least until the third decade of life, with 50% of affected individuals reaching legal blindness by 40 years of age. PMID: 24199935 Hearing loss was found to co-segregate with locus-specific STR markers for MYO7A in 32 Pakistani families. PMID: 23770805 Our results show that MYO7A therapy with AAV2 or AAV5 single vectors is efficacious; however, the dual AAV2 approach proved to be less effective. PMID: 23344065 Possible digenism could not be excluded in two families segregating genomic variations in both MYO7A and USH2A, and two families with CLRN1 and USH2A. PMID: 22681893 Two novel mutations, c.3742G>A (p.E1248K) and c.6051+1G>A (donor splice site mutation in intron 44), of MYO7A in a Chinese non-consanguineous family with Usher syndrome type 1, were identified. PMID: 23559863 A new missense mutation (Arg668His) in the motor head domain of myosin VIIA in a family with autosomal dominant hearing impairment (DFNA11). PMID: 23383098 in a set of consanguineous patient families with Leber congenital amaurosis study identified five putative disease-causing mutations, including four novel alleles, in six families; These five mutations are located in four genes, ALMS1, IQCB1, CNGA3, and MYO7A PMID: 21901789 A previously reported mutation (c.52C>T; p.Q18X) in the myosin VIIA (MYO7A) gene was found in the homozygous state in the affected siblings. PMID: 22690115 Pathogenic mutations in MYO7A, USH1C, and USH1G have been found in four consanguineous Israeli Arab families with Usher syndrome type 1. PMID: 22219650 The results suggested that in a cellular environment, compartment-specific fluctuations in free Mg2+ ions can mediate the conditional switching of myosin-7a between cargo moving and tension bearing modes. PMID: 21687988 The authors speculate that null MYO7A alleles could be associated with milder dysfunction and fewer photoreceptor structural losses at ages when other genotypes show more severe phenotypes. PMID: 21873662 Significant linkage in DFNA11 markers was found in hereditary deafness. PMID: 17702415 a single nucleotide polymorphism (SNP) T/C at position -4128 in the wild-type MYO7A promoter allele that sorts with the degree of hearing loss severity in the pedigree PMID: 21378158 association of myosin VIIA monomers with membrane via the MyRip/Rab27a complex facilitates the cargo-transporting activity of myosin VIIA, which is achieved by cluster formation on the membrane PMID: 21482763 Novel missense mutations in MYO7A underlying postlingual high- or low-frequency non-syndromic hearing impairment in two large families. PMID: 21150918 Five mutations (three in MYO7A and two in CDH23) were identified in four of five unrelated patients with Usher syndrome type 1. PMID: 20844544 The molecular determinant of a mild form of retinopathy in association with a subtle splicing modulation of MYO7A mRNA, was investigated. PMID: 21031134 Variable hearing impairment in a DFNB2 family with a novel MYO7A missense mutation PMID: 20132242 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 Expressed in retina. Domain structure. Carrier proteins determine cellular function. PMID: 15180257 A new heterozygous missense mutation (c.2557C>T; p.R853C) was found in autosomal dominant non-syndromic hearing loss that changes an invariant residue of the fifth IQ motif, a putative calmodulin (CaM) binding domain. PMID: 15300860

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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.

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