Comparison

Recombinant Human Phosphoacetylglucosamine mutase(PGM3)

Manufacturer Cusabio
Category
Type Proteins
Specific against other
Amount 10ug
Host E.coli
Item no. CSB-EP017869HU-10
eClass 6.1 34160400
eClass 9.0 42020190
Available
Research Topic
Metabolism
Uniprot ID
O95394
Gene Names
PGM3
Organism
Homo sapiens (Human)
AA Sequence
MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHL DHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEED NGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRV LIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSV IDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRY GKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKV DCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKL NHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDAD RIVYYYHDADGHFHLIDGDKIATLISSFLKELLVE IGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTK TGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEM KIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAI SDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQ VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKL SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSL AVFQLAGGIGERPQPGF
Expression Region
1-542aa
Sequence Info
Full Length
Source
E.coli
Tag Info
N-terminal 6xHis-SUMO-tagged
MW
75.9 kDa
Alternative Name
Acetylglucosamine phosphomutaseCurated
Relevance
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
Reference
The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003)
Purity
Greater than 90% as determined by SDS-PAGE.
Storage Buffer
Tris-based buffer, 50% glycerol
Storage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week.
Function
Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
Involvement in disease
Immunodeficiency 23 (IMD23)
Protein Families
Phosphohexose mutase family
Tissue Specificity
Found in many tissues except lung. Relatively high expression in pancreas, heart, liver, and placenta, and relatively low expression in brain, skeletal muscle and kidney.
Amount: 10ug
Available: In stock
Listprice: €175.45
Price: €175.45
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