protein

Recombinant Human Alpha-L-iduronidase

MBS717919

0.05 mg (E-Coli)

185 USD

Recombinant Protein

Recombinant Human Alpha-L-iduronidase

Alpha-L-iduronidase

alpha-L-iduronidase; Alpha-L-iduronidase; alpha-L-iduronidase; iduronidase, alpha-L-

IDUA

IDUA; IDUA; IDA; MPS1

IDUA_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

28-653

653

APHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVL
SWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGR
GLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFE
DKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEP
DHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPG
DSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISL
HRKGARSSISILEQEKVVAQQ

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Metabolism

Human alpha-L-iduronidase cDNA isolation and expression.Scott H.S., Anson D.S., Orsborn A.M., Nelson P.V., Clements P.R., Morris C.P., Hopwood J.J.Proc. Natl. Acad. Sci. U.S.A. 88:9695-9699(1991) Structure and sequence of the human alpha-L-iduronidase gene.Scott H.S., Guo X.H., Hopwood J.J., Morris C.P.Genomics 13:1311-1313(1992) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Molecular genetics of mucopolysaccharidosis type I diagnostic, clinical, and biological implications.Scott H.S., Bunge S., Gal A., Clarke L.A., Morris C.P., Hopwood J.J.Hum. Mutat. 6:288-302(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) Insights into mucopolysaccharidosis I from the structure and action of alpha-L-iduronidase.Bie H., Yin J., He X., Kermode A.R., Goddard-Borger E.D., Withers S.G., James M.N.Nat. Chem. Biol. 9:739-745(2013) Human alpha-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.Maita N., Tsukimura T., Taniguchi T., Saito S., Ohno K., Taniguchi H., Sakuraba H.Proc. Natl. Acad. Sci. U.S.A. 110:14628-14633(2013) Mutation analysis of 19 North American mucopolysaccharidosis type I patients identification of two additional frequent mutations.Clarke L.A., Nelson P.V., Warrington C.L., Morris C.P., Hopwood J.J., Scott H.S.Hum. Mutat. 3:275-282(1994) Two novel mutations causing mucopolysaccharidosis type I detected by single strand conformational analysis of the alpha-L-iduronidase gene.Clark L.A., Scott H.S.Hum. Mol. Genet. 2:1311-1312(1993) Identification of mutations in the alpha-L-iduronidase gene (IDUA) that cause Hurler and Scheie syndromes.Scott H.S., Litjens T., Nelson P.V., Thompson P.R., Brooks D.A., Hopwood J.J., Morris C.P.Am. J. Hum. Genet. 53:973-986(1993) Molecular analysis of Hurler syndrome in Druze and Muslim Arab patients in Israel multiple allelic mutations of the IDUA gene in a small geographic area.Bach G., Moskowitz S.M., Tieu P.T., Matynia A., Neufeld E.F.Am. J. Hum. Genet. 53:330-338(1993) Alpha-L-iduronidase mutations (Q70X and P533R) associate with a severe Hurler phenotype.Scott H.S., Litjens T., Nelson P.V., Brooks D.A., Hopwood J.J., Morris C.P.Hum. Mutat. 1:333-339(1992) Mucopolysaccharidosis type I identification of 8 novel mutations and determination of the frequency of the two common alpha-L-iduronidase mutations (W402X and Q70X) among European patients.Bunge S., Kleijer W.J., Steglich C., Beck M., Zuther C., Morris C.P., Schwinger E., Hopwood J.J., Scott H.S., Gal A.Hum. Mol. Genet. 3:861-866(1994) PCR detection of two RFLPs in exon I of the alpha-L-iduronidase (IDUA) gene.Scott H.S., Litjens T., Hopwood J.J., Morris C.P.Hum. Genet. 90:327-327(1992) Multiple polymorphisms within the alpha-L-iduronidase gene (IDUA) implications for a role in modification of MPS-I disease phenotype.Scott H.S., Nelson P.V., Litjens T., Hopwood J.J., Morris C.P.Hum. Mol. Genet. 2:1471-1473(1993) Four novel mutations underlying mild or intermediate forms of alpha-L-iduronidase deficiency (MPS IS and MPS IH/S) .Tieu P.T., Bach G., Matynia A., Hwang M., Neufeld E.F.Hum. Mutat. 6:55-59(1995) Mucopolysaccharidosis type I identification of 13 novel mutations of the alpha-L-iduronidase gene.Bunge S., Kleijer W.J., Steglich C., Beck M., Schwinger E., Gal A.Hum. Mutat. 6:91-94(1995) Molecular genetic defect underlying alpha-L-iduronidase pseudodeficiency.Aronovich E.L., Pan D., Whitley C.B.Am. J. Hum. Genet. 58:75-85(1996) A novel missense mutation in the human IDUA gene associated with a severe Hurler's phenotype.Bartholomew D.W., McClellan J.M.Hum. Mutat. 12:291-291(1998) Mucopolysaccharidosis type I characterization of novel mutations affecting alpha-L-iduronidase activity.Lee-Chen G.J., Lin S.P., Tang Y.F., Chin Y.W.Clin. Genet. 56:66-70(1999) Identification and characterization of -3c-g acceptor splice site mutation in human alpha-L-iduronidase associated with mucopolysaccharidosis type IH/S.Teng Y.N., Wang T.R., Hwu W.L., Lin S.P., Lee-Chen G.J.Clin. Genet. 57:131-136(2000) Identification and characterization of 13 new mutations in mucopolysaccharidosis type I patients.Matte U., Yogalingam G., Brooks D., Leistner S., Schwartz I., Lima L., Norato D.Y., Brum J.M., Beesley C., Winchester B., Giugliani R., Hopwood J.J.Mol. Genet. Metab. 78:37-43(2003) Identification and molecular characterization of alpha-L-iduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy.Yogalingam G., Guo X.H., Muller V.J., Brooks D.A., Clements P.R., Kakkis E.D., Hopwood J.J.Hum. Mutat. 24:199-207(2004) Mucopolysaccharidosis type I in 21 Czech and Slovak patients mutation analysis suggests a functional importance of C-terminus of the IDUA protein.Vazna A., Beesley C., Berna L., Stolnaja L., Myskova H., Bouckova M., Vlaskova H., Poupetova H., Zeman J., Magner M., Hlavata A., Winchester B., Hrebicek M., Dvorakova L.Am. J. Med. Genet. A 149A:965-974(2009) IDUA mutational profiling of a cohort of 102 European patients with mucopolysaccharidosis type I identification and characterization of 35 novel alpha-L-iduronidase (IDUA) alleles.Bertola F., Filocamo M., Casati G., Mort M., Rosano C., Tylki-Szymanska A., Tuysuz B., Gabrielli O., Grossi S., Scarpa M., Parenti G., Antuzzi D., Dalmau J., Di Rocco M., Vici C.D., Okur I., Rosell J., Rovelli A., Furlan F., Rigoldi M., Biondi A., Cooper D.N., Parini R.Hum. Mutat. 32:E2189-E2210(2011) p.L18P a novel IDUA mutation that causes a distinct attenuated phenotype in mucopolysaccharidosis type I patients.Pasqualim G., Ribeiro M.G., da Fonseca G.G., Szlago M., Schenone A., Lemes A., Rojas M.V., Matte U., Giugliani R.Clin. Genet. 0:0-0(2014) +Additional computationally mapped references. p>Provides general information on the entry.

110611239

NP_000194.2

NM_000203.4

P35475

73.96kD

This gene encodes an enzyme that hydrolyzes the terminal alpha-L-iduronic acid residues of two glycosaminoglycans, dermatan sulfate and heparan sulfate. This hydrolysis is required for the lysosomal degradation of these glycosaminoglycans. Mutations in this gene that result in enzymatic deficiency lead to the autosomal recessive disease mucopolysaccharidosis type I (MPS I). [provided by RefSeq, Jul 2008]

IDUA: Defects in IDUA are the cause of mucopolysaccharidosis type 1H (MPS1H); also known as Hurler syndrome. MPS1H is a severe form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1H usually present, within the first year of life, a combination of hepatosplenomegaly, skeletal deformities, corneal clouding and severe mental retardation. Obstructive airways disease, respiratory infection and cardiac complications usually result in death before 10 years of age. Defects in IDUA are the cause of mucopolysaccharidosis type 1H/S (MPS1H/S); also known as Hurler-Scheie syndrome. MPS1H/S is a form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. MPS1H/S represents an intermediate phenotype of the MPS1 clinical spectrum. It is characterized by relatively little neurological involvement, but most of the somatic symptoms described for severe MPS1 develop in the early to mid-teens, causing considerable loss of mobility. Defects in IDUA are the cause of mucopolysaccharidosis type 1S (MPS1S); also known as Scheie syndrome. MPS1S is a mild form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1S may have little or no neurological involvement, normal stature and life span, but present development of joints stiffness, mild hepatosplenomegaly, aortic valve disease and corneal clouding. Belongs to the glycosyl hydrolase 39 family. Protein type: EC 3.2.1.76; Hydrolase; Glycan Metabolism - glycosaminoglycan degradation. Chromosomal Location of Human Ortholog: 4p16.3. Cellular Component: lysosomal lumen. Molecular Function: L-iduronidase activity; receptor binding. Biological Process: carbohydrate metabolic process; cell morphogenesis; chemical homeostasis; chondroitin sulfate catabolic process; chondroitin sulfate metabolic process; dermatan sulfate catabolic process; disaccharide metabolic process; glycosaminoglycan catabolic process; glycosaminoglycan metabolic process; limb morphogenesis; lysosome organization and biogenesis; skeletal morphogenesis. Disease: Hurler Syndrome; Hurler-scheie Syndrome; Scheie Syndrome

0.05 mg (E-Coli)

185 USD

0.2 mg (E-Coli)

420

0.5 mg (E-Coli)

680

1 mg (E-Coli)

1070