Alpha-galactosidase A, Recombinant Protein

Alpha-D-galactosidase A; Alpha-D-galactoside galactohydrolase; Melibiase; INN: Agalsidase

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

Greater than 90% as determined by SDS-PAGE. (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of GLA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Cardiovascular

(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)

49.4kD

galactosidase alpha

alpha-galactosidase A

Alpha-galactosidase A

AGAL_HUMAN

This gene encodes a homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties. [provided by RefSeq, Jul 2008]

GLA: Defects in GLA are the cause of Fabry disease (FD). FD is a rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Heterozygous females may exhibit the disorder in an attenuated form, they are more likely to show corneal opacities. Belongs to the glycosyl hydrolase 27 family.

Protein type: Lipid Metabolism - sphingolipid; Glycan Metabolism - glycosphingolipid biosynthesis - globo series; Lipid Metabolism - glycerolipid; EC 3.2.1.22; Carbohydrate Metabolism - galactose; Hydrolase

Chromosomal Location of Human Ortholog: Xq22

Cellular Component: cytoplasm; extracellular region; Golgi apparatus; lysosomal lumen; lysosome

Molecular Function: alpha-galactosidase activity; catalytic activity; galactoside binding; hydrolase activity; protein binding; protein homodimerization activity; receptor binding

Biological Process: glycosphingolipid catabolic process; glycosphingolipid metabolic process; glycosylceramide catabolic process; negative regulation of nitric oxide biosynthetic process; negative regulation of nitric-oxide synthase activity; oligosaccharide metabolic process; sphingolipid metabolic process

Disease: Fabry Disease

Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A.Tsuji S., Martin B.M., Kaslow D.C., Migeon B.R., Choudary P.V., Stubblefield B.K., Mayor J.A., Murray G.J., Barranger J.A., Ginns E.I.Eur. J. Biochem. 165:275-280(1987) Nucleotide sequence of the human alpha-galactosidase A gene.Kornreich R., Desnick R.J., Bishop D.F.Nucleic Acids Res. 17:3301-3302(1989) Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci.Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A.Mamm. Genome 6:334-338(1995) The DNA sequence of the human X chromosome.Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.Nature 434:325-337(2005) Human alpha-galactosidase A nucleotide sequence of a cDNA clone encoding the mature enzyme.Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M., Desnick R.J.Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986) A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A.Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H.Gene 58:177-188(1987) Structural organization of the human alpha-galactosidase A gene further evidence for the absence of a 3' untranslated region.Bishop D.F., Kornreich R., Desnick R.J.Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988) Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion.Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C.Nucleic Acids Res. 23:2636-2640(1995) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) The molecular defect leading to Fabry disease structure of human alpha-galactosidase.Garman S.C., Garboczi D.N.J. Mol. Biol. 337:319-335(2004) Molecular basis of Fabry disease mutations and polymorphisms in the human alpha-galactosidase A gene.Eng C.M., Desnick R.J.Hum. Mutat. 3:103-111(1994) A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser.Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y., Uchida T.FEBS Lett. 259:353-356(1990) An atypical variant of Fabry's disease with manifestations confined to the myocardium.von Scheidt W., Eng C.M., Fitzmaurice T.F., Erdmann E., Hubner G., Olsen E.G.J., Christomanou H., Kandolf R., Bishop D.F., Desnick R.J.N. Engl. J. Med. 324:395-399(1991) Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease.Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y., Bishop D.F., Desnick R.J., Suzuki Y.Am. J. Hum. Genet. 47:784-789(1990) Fabry disease six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene.Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M., Sakuraba H., Desnick R.J.J. Clin. Invest. 83:1390-1399(1989) Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease.Ishii S., Sakuraba H., Suzuki Y.Hum. Genet. 89:29-32(1992) Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease.Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H., Desnick R.J.Am. J. Hum. Genet. 53:1186-1197(1993) Mutation analysis in patients with the typical form of Anderson-Fabry disease.Davies J.P., Winchester B.G., Malcolm S.Hum. Mol. Genet. 2:1051-1053(1993) Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease.Davies J.P., Christomanou H., Winchester B.G., Malcolm S.Hum. Mol. Genet. 3:667-669(1994) Fabry disease twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene.Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D., Desnick R.J.Hum. Mol. Genet. 3:1795-1799(1994) Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease.Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H., Suzuki Y.Biochem. Biophys. Res. Commun. 214:1219-1224(1995) Alpha-galactosidase gene mutations in Fabry disease heterogeneous expressions of mutant enzyme proteins.Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y.Hum. Genet. 95:557-561(1995) Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease.Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M., Dahl N.Hum. Mutat. 5:277-278(1995) An atypical variant of Fabry's disease in men with left ventricular hypertrophy.Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M., Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H.N. Engl. J. Med. 333:288-293(1995) Point mutation in the alpha-galactosidase A gene of atypical Fabry disease with only nephropathy.Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y., Nishimura K., Kimura M.Clin. Nephrol. 45:289-294(1996) Fabry disease fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries.Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K., Winchester B.G., Desnick R.J.Eur. J. Hum. Genet. 4:219-224(1996) Novel trinucleotide deletion in Fabry's disease.Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A., Tsambaos D.Hum. Genet. 97:468-470(1996) Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease.Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L.Hum. Genet. 98:719-726(1996) A sensitive mutation screening strategy for Fabry disease detection of nine mutations in the alpha-galactosidase A gene.Blanch L.C., Meaney C., Morris C.P.3.0.CO;2-L>Hum. Mutat. 8:38-43(1996) Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene.Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M., Wevers R.A., Salvayre R., Levade T.J. Med. Genet. 33:682-688(1996) Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis.Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K., Utsumi K., Kamei S., Sakuraba H.Brain Dev. 19:111-116(1997) Fabry disease thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes.Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M., Desnick R.J.Mol. Med. 3:174-182(1997) Identification of a novel point mutation (S65T) in alpha-galactosidase A gene in Chinese patients with Fabry disease.Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J., Hsiao K.-J.3.0.CO;2-N>Hum. Mutat. 11:328-330(1998) A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease.Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y., Seo H.Hum. Mutat. Suppl. 1:S139-S140(1998) Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote.Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S., Sakuraba H.Hum. Mutat. Suppl. 1:S213-S216(1998) Mutation analysis in 11 French patients with Fabry disease.Guffon N., Froissart R., Chevalier-Porst F., Maire I.Hum. Mutat. Suppl. 1:S288-S290(1998) Fabry disease identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches.Germain D.P., Poenaru L.Biochem. Biophys. Res. Commun. 257:708-713(1999) The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A.Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K., van Diggelen O.P., Tsvetkova I.V.Clin. Chim. Acta 280:81-89(1999) Characterization of two alpha-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease.Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K., Sandhoff K., Sakuraba H.Biochim. Biophys. Acta 1501:227-235(2000) Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease.Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J.Mol. Med. 5:806-811(1999) Identification of four novel mutations in five unrelated Korean families with Fabry disease.Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W.Clin. Genet. 58:228-233(2000) Fabry disease twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes.Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J.J. Invest. Med. 48:227-235(2000) Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease.Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C., Bernard M.-C., Poenaru L.Hum. Mutat. 17:353-353(2001) Fabry disease 20 novel GLA mutations in 35 families.Blaydon D., Hill J.A., Winchester B.G.Hum. Mutat. 18:459-459(2001) Natural history of Fabry renal disease influence of alpha-galactosidase A activity and genetic mutations on clinical course.Branton M.H., Schiffmann R., Sabnis S.G., Murray G.J., Quirk J.M., Altarescu G., Goldfarb L., Brady R.O., Balow J.E., Austin H.A. III, Kopp J.B.Medicine (Baltimore) 81:122-138(2002) Two novel mutations in the alpha-galactosidase A gene in Chinese patients with Fabry disease.Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C., Lien Y.-H.H.Clin. Genet. 63:205-209(2003) Analysis of splice-site mutations of the alpha-galactosidase A gene in Fabry disease.Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H.Clin. Genet. 63:476-482(2003) Remarkable variability in renal disease in a large Slovenian family with Fabry disease.Verovnik F., Benko D., Vujkovac B., Linthorst G.E.Eur. J. Hum. Genet. 12:678-681(2004) Detection of alpha-galactosidase a mutations causing Fabry disease by denaturing high performance liquid chromatography.Shabbeer J., Robinson M., Desnick R.J.Hum. Mutat. 25:299-305(2005) Later-onset Fabry disease an ***** variant presenting with the cramp-fasciculation syndrome.Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G., McArthur J.C., Rodriguez M., Desnick R.J.Arch. Neurol. 63:453-457(2006) Newborn screening for Fabry disease in Taiwan reveals a high incidence of the later-onset GLA mutation c.936+919G>A (IVS4+919G>A) .Hwu W.L., Chien Y.H., Lee N.C., Chiang S.C., Dobrovolny R., Huang A.C., Yeh H.Y., Chao M.C., Lin S.J., Kitagawa T., Desnick R.J., Hsu L.W.Hum. Mutat. 30:1397-1405(2009) +Additional computationally mapped references.

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