Recombinant Human Anoctamin-5 (ANO5) Protein (His)

Name: Recombinant Human Anoctamin-5 (ANO5) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00777P
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 Anoctamin-5 (ANO5) Protein (His) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q75V66
Target Symbol	ANO5
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-10His
Target Protein Sequence	MGDPDLLEVLAEEGEKVNKHIDYSFQMSEQSLSSRETSFLINEETMPAKRFNLFLRRRLMFQKNQQSKDSIFFRDGIRQIDFVLSYVDDVKKDAELKAERRKEFETNLRKTGLELEIEDKRDSEDGRTYFVKIHAPWEVLVTYAEVLGIKMPIKESDIPRPKHTPISYVLGPVRLPLSVKYPHPEYFTAQFSRHRQELFLIEDQATFFPSSSRNRIVYYILSRCPFGIEDGKKRFGIERLLNSNTYSSAYPLHDGQYWKPSEPPNPTNERYTLHQNWARFSYFYKEQPLDLIKNYYGEK
Expression Range	1-299aa
Protein Length	Partial
Mol. Weight	39.0 kDa
Research Area	Others
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	Does not exhibit calcium-activated chloride channel (CaCC) activity.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Protein Families	Anoctamin family
Database References	HGNC: 27337 OMIM: 166260 KEGG: hsa:203859 STRING: 9606.ENSP00000315371 UniGene: PMID: 29124309 After Ano5 gene knock-down with shRNA in MC3T3-E1 osteoblast precursors the authors saw elevated expression of osteoblast-related genes such as Col1a1, osteocalcin, osterix and Runx2 as well as increased mineral nodule formation in differentiating cells. The data suggest that ANO5 plays a role in osteoblast differentiation. PMID: 28176803 The Limb-girdle muscular dystrophy 2L family was characterized by mild chronic myopathy and bilateral gastrocnemius hypertrophy with obviously increased creatine kinase levels. Pathological changes included atrophy of fibers with interstitial connective tissues hyperplasia. The pathogenic allele was a c.220C> T mutation in the ANO5 gene. PMID: 30235762 A heterozygous mutation in the ANO5 gene c.1067G > A (p.Cys356Tyr) was identified in both affected individuals in a Russian family with giant cementoma and bone fractures consistent with a diagnosis of gnathodiaphyseal dysplasia. PMID: 27216912 Results show that ANO5 is downregulated in thyroid cancer and, negatively associated with lymph node metastasis. Its inhibition promotes the migration and invasion of thyroid cancer cells suggesting it as a tumor marker. PMID: 28902351 Study characterized 12 newly identified and 2 previously identified patients with ANO5 mutations from 11 families. Material was genetically homogeneous with most patients homozygous for the Finnish founder variant c.2272C>T (p.Arg758Cys). In one family, study found a novel p.Met470Arg variant compound heterozygous with p.Arg758Cys. PMID: 27911336 Asymptomatic, sometimes mild hyperCKemia or exercise intolerance is a presentation of ANO5-related myopathy. PMID: 28187523 Here we show that Ano5-deficient mice have reduced capacity to repair the sarcolemma following laser-induced damage, exhibit delayed regeneration after cardiotoxin injury and suffer from defective myoblast fusion necessary for the proper repair and regeneration of multinucleated myotubes. these data suggest that ANO5 plays an important role in sarcolemmal membrane dynamics. PMID: 26911675 Study screened the ANO5 gene in 786 myopathic patients and 52 controls by combining NGS and Sanger sequencing. In the cohort of patients, thirty-three are homozygous or compound heterozygous for causative mutations in ANO5 PMID: 25891276 supervised aerobic exercise training is safe and effective in improving oxidative capacity and muscle function in patients with anoctamin 5 deficiency PMID: 24639367 The present report describes an association between LGMD2L consequent upon mutation in ANO5 and macular dystrophy in one affected person. PMID: 24232312 Dilated cardiomyopathy is associated with mutations in the ANO5 gene. PMID: 23041008 ANO5 mutations can be associated with amyloid deposition in muscle PMID: 23663589 A high prevalence of ANO5 deficiency was found among patients with unclassified recessive limb girdle muscular dystrophy 2 PMID: 23670307 a diagnosis of ANO5 causing Muscular Dystrophy, Limb-Girdle, Type 2L, in 16% of the families (11/68) in a well-defined limb girdle muscular dystrophy cohort in the Netherlands PMID: 23607914 investigated the prevalence and spectrum of ANO5 gene mutations and related clinical phenotypes; study confirmed that ANO5 gene mutations are responsible for about one fourth of cases of undiagnosed muscular dystrophy in the population studied PMID: 23606453 This study showed that TMEM16E possesses distinct function other than chloride channel activity, and another protein-stabilizing machinery toward the TMEM16E proteins should be considered for the on-set regulation of their phenotypes in tissues. PMID: 23843187 By sequencing the entire ANO5 gene coding region and untranslated regions in a large Italian gnathodiaphyseal dyplasia family, a novel missense mutation causing the p.Thr513Ile substitution, was found. PMID: 23047743 occurrence and molecular epidemiology of LGMD2L, caused by mutations in the anoctamin 5 (ANO5) gene, in a Italian cohort differed from those observed in other European countries. PMID: 22742934 This study demonistrayed that anoctamin 5 mutations associate to distal muscular dystrophy. PMID: 22980764 A family is described in which 2 mutations in ANO5 segregate with marked creatine kinase-type hypercreatinemia, demonstrating that recessively inherited ANO5 mutations not only lead to muscular dystrophy but may also cause bone disease. PMID: 23055322 The c.191dupA mutation, already reported as a founder mutation in Caucasian patients with anoctamin myopathies, was found in our family in a heterozygous state. PMID: 22336395 This study identified four novel mutations in the ANO5 gene cause high lever Creatine Kinase and limb girdle muscular weakness and Miyoshi type of muscular dystrophy. PMID: 22499103 Mutations are distributed all over the gene, indicating that muscular dystrophy caused by ANO5 can be expected to occur in all populations PMID: 22402862 mutation in patients with a distal myopathy;(a new separate clinical, genetic and histopathologic entity) PMID: 20692837 A founder mutation in Anoctamin 5 is a major cause of limb-girdle muscular dystrophy. PMID: 21186264 Recessive mutations were identified in ANO5 that result in a proximal limb-girdle muscular dystrophy (LGMD2L) in three French Canadian families and in a distal non-dysferlin Miyoshi myopathy (MMD3) in Dutch and Finnish families. PMID: 20096397

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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.