Recombinant Human PMM2 Protein (C-6His)

Name: Recombinant Human PMM2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1297NP
Availability: InStock

BL-1297NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Phosphomannomutase 2 is produced by our E.coli expression system and the target gene encoding Met1-Ser246 is expressed with a 6His tag at the C-terminus.
Accession	O15305
Synonym	Phosphomannomutase 2; PMM 2; PMM2
Gene Background	Phosphomannomutase 2 (PMM2) is an enzyme that is a member of the highly variable methyltransferase superfamily. PMM2 is a cytoplasmic protein and catalyzes the isomerization of mannose 6-phosphate to mannose 1-phosphate.In addition, PMM2 involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose that required for a number of critical mannosyl transfer reactions. Defects in PMM2 can results in congenital disorder of glycosylation type 1A (CDG1A). Congenital disorders of glycosylation are metabolic deficiencies in glycoprotein biosynthesis that usually cause severe mental and psychomotor retardation.
Molecular Mass	29.1 KDa
Apmol Mass	29 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Subcellular Location	Cytoplasm.
Protein Families	Eukaryotic PMM family
Database References	HGNC: 9115 OMIM: 212065 KEGG: hsa:5373 STRING: 9606.ENSP00000268261 UniGene: Hs.625732
Associated Diseases	Congenital disorder of glycosylation 1A (CDG1A)

Gene Functions References

The biochemical analysis of mutants does not allow a precise genotypephenotype correlation for PMM2-Type I disorders of glycosylation. PMM2 is very tolerant to missense and loss of function mutations, suggesting that a partial deficiency of activity might be beneficial under certain circumstances. PMID: 30061496
clinical variables to detect risk factors for Stroke-like episodes in a series of 43 phosphomannomutase deficiency patients. PMID: 29470411
PMM2-CDG clinical phenotype is heterogeneous in terms of clinical course, with no clear division between neurological and visceral presentations. PMID: 28954837
Four patients were diagnosed with PMM2-CDG at the age of 8 years or later as their neurological symptoms were quite mild and they had been able to participate in regular school programs. We report patients with p.Val231Met/p.Arg239Trp and p.Ile120Thr/p.Gly228Cys genotypes which may cause milder variants of PMM2-CDG PMID: 28425223
This functional mouse model of PMM2-CDG, in vitro assays and identification of the novel gp130 biomarker all shed light on the human disease, and moreover, provide the essential tools to test potential therapeutics for this untreatable disease. PMID: 27053713
We propose that the PMM2 promoter mutation alters tissue-specific chromatin loop formation, with consequent organ-specific deficiency of PMM2 leading to the restricted phenotype of HIPKD. Our findings extend the spectrum of genetic causes for both HI and PKD and provide insights into gene regulation and PMM2 pleiotropy PMID: 28373276
work describes the functional analysis of 9 PMM2 mutant proteins frequently found in congenital disorder of glycosylation type Ia(PMM2-CDG)patients; results suggest that some loss-of-function mutations detected in PMM2-CDG patients could be destabilizing PMID: 26014514
the activity of phosphomannomutase2 R141H/F119L heterodimers in vitro, which reproduces the protein found in patients, has the same activity of wild type/R141H, which reproduces the protein found in healthy carriers. PMID: 26488408
A mild neurological phenotype of PMM2-CDG marked by preserved ambulatory ability and autonomy and associated with L32R mutation is particularly frequent in Italy. PMID: 25355454
conformational response to ligand binding in phosphomannomutase2 PMID: 25324542
Data indicate genome-wide significant association at multiple single nucleotide polymorphism (SNPs) near ATP binding cassette transporter 1 (ABCA1) at 9q31.1 and suggestive evidence of association in phosphomannomutase 2 (PMM2) at 16p13.2. PMID: 25173107
We conclude that electroretinogram signs of on-pathway dysfunction can be detected in the early stages of PMM2-Congenital disorder of glycosylation. PMID: 23430200
Two young sisters are compound heterozygous for mutations p.Leu32Arg and p.Arg141His, while two paternal great-aunts are compound heterozygosity for p.Leu32Arg and p.Thr237Met, with congenital disorder of glycosylation. PMID: 23988505
Hypertrophic cardiomyopathy with cardiac rupture and tamponade caused by congenital disorder of glycosylation type Ia with PMM2 mutations in two siblings. PMID: 22374380
Identification of exclusively catalytic protein change, catalytic protein changes affecting protein stability, two protein changes disrupting the dimer interface and several misfolding changes . PMID: 21541725
When non-immune hydrops fetalis remains unexplained despite exhaustive obstetrical screening, analysis of PMM activity in the parents' leucocytes is possible and might be performed easily during pregnancy PMID: 20638314
The presence of this deletion-insertion mutation at cDNA position 565 suggests that this site in the PMM2 gene may be a hotspot for chromosomal breakage. PMID: 11891694
Congenital disorder of glycosylation type Ia: benign clinical course in a new genetic variant. a new, previously undescribed, combination of mutations of the PMM gene locus on chromosome 16p13 (647,691). PMID: 11935250
A Japanese patient with congenital disorder of glycosylation type Ia had a novel nonsense mutation (R194X) in the PMM2 gene. PMID: 13129599
enzymatic activity of PMM2 is upregulated by insulin treatment and that Sgk1 completely inhibits PMM2 activity both in the absence and in the presence of insulin stimulation. PMID: 15342340
11 novel mutations in the PMM2 gene are described as associated with Congenital disorder of Glycosylation type Ia. PMID: 15844218
Based on SNP and STR genotypic analysis, we ascertained an association between the R141H substitution and a particular haplotype, suggesting a common origin for all the mutated chromosomes. PMID: 17166182
We describe the characterization of two unusual truncating PMM2 mutations in two CDG-Ia patients. PMID: 17307006
three siblings of congenital disorder of glycosylation type 1a are compound heterozygotes for R141H and L32R mutations in the PMM2 gene. PMID: 17451957
Two CDG-Ia patients,who presented with ataxia and cerebellar hypoplasia and with a normal or only slightly abnormal transferrin but the activity of the corresponding enzyme phosphomannomutase was clearly deficient in leucocytes and fibroblasts. PMID: 17694350
Val231Met and Arg148Met heterozygosity can present as primary skeletal dysplasia with congenital glycosylation type Ia disorder. PMID: 18203160
This work reports the study of two new nucleotide changes (c.256-1G>C and c.640-9T>G) identified in the PMM2 gene in congenital disorders of glycosylation type 1a patients, and of a previously described deep intronic nucleotide change in intron 7. PMID: 19235233

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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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