Comparison

Recombinant Human Phosphoacetylglucosamine mutase(PGM3)

Manufacturer Cusabio
Category
Type Proteins
Specific against other
Amount 200ug
Host E.coli
Item no. CSB-EP017869HU-200
Eclass 6.1 34160400
Eclass 9.0 42020190
Available
Alternative Name(s)
Acetylglucosamine phosphomutaseCurated
AA Sequence
MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHL DHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEED NGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRV LIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSV IDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRY GKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKV DCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKL NHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDAD RIVYYYHDADGHFHLIDGDKIATLISSFLKELLVE IGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTK TGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEM KIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAI SDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQ VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKL SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSL AVFQLAGGIGERPQPGF
Research Topic
Metabolism
Uniprot ID
O95394
Gene Names
PGM3
Tag Info
N-terminal 6xHis-SUMO-tagged
Expression Region
1-542aa
MW of Fusion Proten
75, 9
Sequence Info
Full Length
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.
Species
Homo sapiens (Human)
Amount: 200ug
Available: In stock
Listprice: €546.07
Price: €546.07
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