Recombinant Human Myosin-9 (MYH9) Protein (GST)

Name: Recombinant Human Myosin-9 (MYH9) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02386P
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 Myosin-9 (MYH9) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P35579
Target Symbol	MYH9
Synonyms	BDPLT 6; BDPLT6; Cellular myosin heavy chain; Cellular myosin heavy chain type A; DFNA 17; DFNA17; EPSTS; FTNS; MGC104539; MHA; MYH 2A; MYH 9; MYH2A; MYH9; MYH9_HUMAN; MYHas8; MyHC 2A; MyHC IIa; MyHC2A; MyHCIIa; MYHSA 2; MYHSA2; Myosin 9; Myosin heavy chain 9; Myosin heavy chain 9 non muscle; Myosin heavy chain; Myosin heavy chain non muscle IIa; Myosin heavy chain nonmuscle IIa; Myosin heavy polypeptide 2; Myosin heavy polypeptide 9 non muscle; Myosin-9; Myosin9; NMHC II A; NMMHC A; NMMHC II a; NMMHC II-a; NMMHC IIA; NMMHC-A; NMMHC-IIA; NMMHCA; Non muscle myosin heavy chain A; Non muscle myosin heavy chain; Non muscle myosin heavy chain II A; Non muscle myosin heavy polypeptide 9; non-muscle IIa; Non-muscle myosin heavy chain A; Non-muscle myosin heavy chain IIa; Nonmuscle myosin heavy chain A; Nonmuscle myosin heavy chain II A; type A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	AQQAADKYLYVDKNFINNPLAQADWAAKKLVWVPSDKSGFEPASLKEEVGEEAIVELVENGKKVKVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI
Expression Range	2-241aa
Protein Length	Partial
Mol. Weight	54.2kDa
Research Area	Cell Cycle
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	Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis. Promotes cell motility in conjunction with S100A4. During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10.
Subcellular Location	Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Cytoplasmic vesicle, secretory vesicle, Cortical granule.
Protein Families	TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
Database References	HGNC: 7579 OMIM: 153640 KEGG: hsa:4627 STRING: 9606.ENSP00000216181 UniGene: PMID: 29956586 In neutrophilic leucocytes from MYH9-related disease patients NMIIa inclusions are accompanied by increased lipid storage in droplets, suggesting that NMIIa dysfunction may contribute to lipid imbalance in man. PMID: 28361956 A missense mutation (c.1124C>T:p.S375F) was found in a congenital thrombocytopenia patient and his affected mother. It was associated with abnormal neutrophil NMMHC-IIA localization. PMID: 28293712 Our results suggest that MYH9 rs3752462 is significantly associated with an increased risk of diabetic kidney disease in Chinese Han individuals. PMID: 29862302 Results suggest that coupling between actin and microtubule cytoskeletons driven by Myosin II and KIF20A ensures the spatial coordination between RAB6-positive vesicles fission from Golgi/trans-Golgi network membranes and their exit along microtubules. PMID: 29093437 These results suggest that cytoplasmic multimolecular protein complexes containing myosin-9 and tropomyosin are involved in the regulation of cellular response to LYSOPHOSPHATIDIC ACID. PMID: 30199160 miR-647 functions as a tumor metastasis suppressor in gastric cancer by targeting SRF/MYH9 axis. PMID: 28900514 MYO18A has the potential to form a multiprotein complex that links the Golgi apparatus to F-actin, which regulates muscle integrity and function during early development PMID: 27824130 Report that PTCSC2 binds myosin-9 (MYH9). In a bidirectional promoter shared by FOXE1 and PTCSC2, MYH9 inhibits the promoter activity in both directions. This inhibition can be reversed by PTCSC2, which acts as a suppressor. PMID: 28049826 demonstrated that though the targeted integration site for exogenous genes is shifted to MYH9 intron 2 (about 500bp downstream exon 2), the high HR efficiency and the endogenous MYH9 gene integrity are not only preserved, but the expected expression of the inserted gene(s) is observed in a pre-designed set of experiments conducted in mouse ES cells PMID: 29438440 These distinct functions of NMIIA and NMIIB might promote intrinsic and directed migration of normal human fibroblasts. PMID: 29486156 ALPK1 is a kinase that participates in the regulation of Golgi-derived TNF-alpha trafficking through myosin IIA phosphorylation in the inflammation of gout. PMID: 27169898 we present high MYH9 expression as a reliable and powerful prognostic factor for patients with AML. PMID: 27437869 Mutations of MYH9 cause MYH9-RD, a form of congenital thrombocytopenia characterized by giant platelets and no platelet functional abnormalities. PMID: 28368695 Findings suggest that the tumor suppressor capability of wtp53 is dependent upon functional NMIIA and that the invasive phenotype of high-risk mutp53 is independent of NMIIA. PMID: 28160562 Heterozygous deletional mutation (c.5803delG) in exon 41 of the MYH9 gene is associated with inherited thrombocytopenia. PMID: 28604953 cytokinesis failure in megakaryocytes is the consequence of both the absence of NMIIB and a low RhoA activity that impairs NMIIA localization at the cleavage furrow through increased actin turnover. PMID: 27737892 The loss of junctional NMIIA, upon Coronin 1B knockdown, perturbed RhoA signaling. PMID: 27650961 Results identified nonsynonymous variants in MYH9 and ABCA4 to be the most frequent risk loci in nonsyndromic orofacial clefts in the Taiwanese population. PMID: 27527345 Our study is the first to identify genetic predisposition to transplant renal artery stenosis in patients with MYH9 risk allelic variants (rs4821480, rs4821481, rs3752462, rs11089788, rs136211, rs5756168, rs2032487, and rs2239784) PMID: 27496447 The hearing impairment associated with MYH9 disorder in this family was characterized as adult onset, progressive, and high-frequency dominant. Hematological manifestations of MYH9 disorder show complete penetrance, whereas extra-hematological manifestations show incomplete penetrance and variable expressivity in this family. PMID: 26942920 mass spectrum followed by immunoprecipitation identified non-muscle myosin heavy chain-IIA (NMMHC-IIA) as the CXCR4-interacting protein. Furthermore, pharmaceutical inhibition of NMMHC-IIA by blebbistatin dampened the nuclear translocation of CXCR4 as well as the metastatic capacity of RCC cells PMID: 27634189 The rs3752462 polymorphism of MYH9 is associated with high systolic blood pressure in patients with CKD. The T allele in the dominant model was associated with an elevated risk for high systolic blood pressure . PMID: 27924804 The Raf-ERK1/2 signaling pathway is involved in regulation of NMIIA by DT-13. PMID: 27374701 The tumor microenvironment can regulate NMIIA in cancer cells. PMID: 27350172 HhnRNP-K-mediated regulation of NMHC IIA mRNA translation contributes to the control of enucleation in erythropoiesis. PMID: 26823606 Data show that a heterozygous missense mutation c.4270G>A (p.Aspl841Asn) in exon 30 of the non-muscle myosin heavy chain 9 (MYH9) gene was identified in all affected members from thE family. PMID: 27577209 the present study indicated that knockdown of NMIIA inhibited the migration and invasion of gastric cancer cells, which may be, at least in part, mediated via the JNK signaling pathway. PMID: 26719067 Knocking down myosin-9 or promoting protein S-glutathionylation by knocking down glutaredoxin-1 inhibited the death of airway smooth muscle cells by heating to simulate bronchial thermoplasty PMID: 26499037 Severity and progression of sensorineural hearing loss appeared to depend on the specific NMMHC-IIA mutation in patients with MYH9-related disease. PMID: 26226608 7 members in 3 generations of a family had macrothrombocytopenia without Alport syndrome, and they all had a p.A95V mutation in exon 1 of MYH9. This affects the motor domain. PMID: 26861218 heterozygotic form (allele A) of the MYH9 gene could be considered a very early marker, a new risk factor for the appearance of CKD, or a sign of renal frailty in elderly people. PMID: 26152646 concordant with the genetic interaction observed in sickle cell disease patients, APOL1 G2 reduces myh9 expression in vivo, suggesting a possible interaction between the altered APOL1 and myh9. PMID: 26147622 myosin IIA and IIB heavy chains play distinct and non-redundant roles in matrix remodeling PMID: 26136073 Inhibition of NMMHC IIA impedes TF expression and venous thrombosis via Akt/GSK3beta-NF-kappaB signalling pathways in the endothelium both in vitro and in vivo. PMID: 25881103 revealed that MYH9 is expressed in a subset of NSCLC with a more malignant nature, and its expression is an indicator of a poorer survival probability PMID: 25826333 R705H mutation of MYH9 is associated with MYH9-related disease characterized by hearing impairment, thrombocytopenia, giant platelets, leukocyte inclusions, and mild to moderate elevation of some liver enzymes PMID: 24890873 Data show that myosin II supports a stable Rho zone at the at E-cadherin junctions. PMID: 26368311 MYH9 gene polymorphisms may be associated with multiple cerebrovascular blood flow phenotypes in Chinese patients with type 2 diabetes PMID: 25730040 High myosin-9 expression is associated with esophageal squamous cell carcinoma. PMID: 25605255 One complicating factor in this case is the diagnosis of MYH9RD in this patient. PMID: 25424224 A novel MYH9 mutation in a patient with MYH9 disorders and platelet size-specific effect of romiplostim on macrothrombocytopenia. PMID: 26051904 MYH9 p.R1165C mutation is associated with MYH9 Disorder. PMID: 26056797 we tested the effect of loss of MYH9 expression in podocytes in vitro, and found that it was necessary for cytoskeletal organization PMID: 24949636 Whereas most nonmuscle myosin IIA (MIIA) at the leading edge assembled into dorsal contractile arcs, a substantial subset assembled in or was captured within maturing focal adhesions, and this behavior was promoted by active Rac1. PMID: 25544611 the role of myosin IIA and its specific kinase, myosin light chain kinase, during Shigella intercellular spreading was investigated in HeLa cells PMID: 24989342 A novel mechanism of regulation of NMHC-IIA activity relying on the phosphorylation of Tyr-158 by Src. PMID: 25635050 These findings indicate that overexpression of NMIIA may contribute to the progression and poor prognosis of GC. PMID: 23203126 Matrix stiffness couples to myosin-II activity to promote lamin-A,C dephosphorylation at Ser22, which regulates turnover, lamina physical properties, and actomyosin expression. Lamin-A,C phosphorylation is low in interphase versus dividing cells. PMID: 25127216 The role of myosin II in shape control of invasive cells migrating in 3D collagen gels, was studied. PMID: 25621949

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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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