protein

Recombinant Human Arylsulfatase B

MBS952564

0.05 mg (E-Coli)

180 USD

Recombinant Protein

Recombinant Human Arylsulfatase B

Arylsulfatase B

N-acetylgalactosamine-4-sulfatase; G4S

arylsulfatase B isoform 1; Arylsulfatase B; arylsulfatase B; arylsulfatase B; N-acetylgalactosamine-4-sulfatase; G4S

ARSB

ARSB; ARSB; ASB; G4S; MPS6; ASB; G4S

ARSB_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

37-533; Mature full length protein

533

SGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDAL
AAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQII
WPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRK
ECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRC
ALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKP
LFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMV
SLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGG
NNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELI
HISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSP
RIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFN
TSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSS
DPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQF
YHKHSVPVYFPAQDPRCDPKATGVWGPWM

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.

Cancer

Roves sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation. Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium. In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels.

Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B.Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuehlsdorf M., Vingron M., Meyer H.E., Pohlmann R., von Figura K.J. Biol. Chem. 265:3374-3381(1990) Human arylsulfatase B MOPAC cloning, nucleotide sequence of a full-length cDNA, and regions of amino acid identity with arylsulfatases A and C.Schuchman E.H., Jackson C.E., Desnick R.J.Genomics 6:149-158(1990) Structure of the human arylsulfatase B gene.Modaressi S., Rupp K., von Figura K., Peters C.Biol. Chem. Hoppe-Seyler 374:327-335(1993) 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) The DNA sequence and comparative analysis of human chromosome 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Human N-acetylgalactosamine-4-sulphatase protein maturation and isolation of genomic clones.Litjens T., Morris C.P., Gibson G.J., Beckmann K.R., Hopwood J.J.Biochem. Int. 24:209-215(1991) Components and proteolytic processing sites of arylsulfatase B from human placenta.Kobayashi T., Honke K., Jin T., Gasa S., Miyazaki T., Makita A.Biochim. Biophys. Acta 1159:243-247(1992) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.Schmidt B., Selmer T., Ingendoh A., von Figura K.Cell 82:271-278(1995) Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency.Cosma M.P., Pepe S., Parenti G., Settembre C., Annunziata I., Wade-Martins R., Domenico C.D., Natale P.D., Mankad A., Cox B., Uziel G., Mancini G.M., Zammarchi E., Donati M.A., Kleijer W.J., Filocamo M., Carrozzo R., Carella M., Ballabio A.Hum. Mutat. 23:576-581(2004) Arylsulfatase B regulates colonic epithelial cell migration by effects on MMP9 expression and RhoA activation.Bhattacharyya S., Tobacman J.K.Clin. Exp. Metastasis 26:535-545(2009) 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) Structure of a human lysosomal sulfatase.Bond C.S., Clements P.R., Ashby S.J., Collyer C.A., Harrop S.J., Hopwood J.J., Guss J.M.Structure 5:277-289(1997) Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome) . An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B.Wicker G., Prill V., Brooks D.A., Gibson G.J., Hopwood J.J., von Figura K., Peters C.J. Biol. Chem. 266:21386-21391(1991) Mucopolysaccharidosis type VI identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity.Jin W.-D., Jackson C.E., Desnick R.J., Schuchman E.H.Am. J. Hum. Genet. 50:795-800(1992) Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome) six unique arylsulfatase B gene alleles causing variable disease phenotypes.Isbrandt D., Arlt G., Brooks D.A., Hopwood J.J., von Figura K., Peters C.Am. J. Hum. Genet. 54:454-463(1994) Four novel mutant alleles of the arylsulfatase B gene in two patients with intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome) .Voskoboeva E., Isbrandt D., von Figura K., Krasnopolskaya X., Peters C.Hum. Genet. 93:259-264(1994) N-acetylgalactosamine-4-sulfatase identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI.Simonaro C.M., Schuchman E.H.Biochim. Biophys. Acta 1272:129-132(1995) Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS6 patients.Litjens T., Brooks D.A., Peters C., Gibson G.J., Hopwood J.J.Am. J. Hum. Genet. 58:1127-1134(1996) Two novel mutations of the arylsulfatase B gene in two Italian patients with severe form of mucopolysaccharidosis.Villani G.R.D., Balzano N., Di Natale P.3.0.CO;2-Q>Hum. Mutat. 11:410-410(1998) Large-scale identification, mapping, and genotyping of single-nucleotide polymorphisms in the human genome.Wang D.G., Fan J.-B., Siao C.-J., Berno A., Young P., Sapolsky R., Ghandour G., Perkins N., Winchester E., Spencer J., Kruglyak L., Stein L., Hsie L., Topaloglou T., Hubbell E., Robinson E., Mittmann M., Morris M.S., Shen N., Kilburn D., Rioux J., Nusbaum C., Rozen S., Hudson T.J., Lipshutz R., Chee M., Lander E.S.Science 280:1077-1082(1998) Maroteaux-Lamy syndrome five novel mutations and their structural localization.Villani G.R.D., Balzano N., Vitale D., Saviano M., Pavone V., Di Natale P.Biochim. Biophys. Acta 1453:185-192(1999) A novel mutation (Q239R) identified in a Taiwan Chinese patient with type VI mucopolysaccharidosis (Maroteaux-Lamy syndrome) .Wu J.-Y., Yang C.-F., Lee C.-C., Chang J.-G., Tsai F.-J.3.0.CO;2-0>Hum. Mutat. 15:389-390(2000) Mucopolysaccharidosis type VI report of two Taiwanese patients and identification of one novel mutation.Yang C.-F., Wu J.-Y., Lin S.-P., Tsai F.-J.J. Formos. Med. Assoc. 100:820-823(2001) Mutational analysis of mucopolysaccharidosis type VI patients undergoing a trial of enzyme replacement therapy.Karageorgos L., Harmatz P., Simon J., Pollard A., Clements P.R., Brooks D.A., Hopwood J.J.Hum. Mutat. 23:229-233(2004) +Additional computationally mapped references. p>Provides general information on the entry.

38569405

NP_000037.2

NM_000046.3

P15848

72kD

CS/DS Degradation Pathway (1269987); Chondroitin Sulfate Degradation Pathway (413376); Chondroitin Sulfate Degradation Pathway (468247); Chondroitin Sulfate/dermatan Sulfate Metabolism Pathway (1269984); Dermatan Sulfate Degradation Pathway (413375); Dermatan Sulfate Degradation Pathway (468240); Gamma Carboxylation, Hypusine Formation And Arylsulfatase Activation Pathway (1268702); Glycosaminoglycan Degradation Pathway (82981); Glycosaminoglycan Degradation Pathway (355); Glycosaminoglycan Metabolism Pathway (1269972)

Arylsulfatase B encoded by this gene belongs to the sulfatase family. The arylsulfatase B homodimer hydrolyzes sulfate groups of N-Acetyl-D-galactosamine, chondriotin sulfate, and dermatan sulfate. The protein is targetted to the lysozyme. Mucopolysaccharidosis type VI is an autosomal recessive lysosomal storage disorder resulting from a deficiency of arylsulfatase B. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

ARSB: Defects in ARSB are the cause of mucopolysaccharidosis type 6 (MPS6); also known as Maroteaux-Lamy syndrome. MPS6 is an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of dermatan sulfate. Clinical features can include abnormal growth, short stature, stiff joints, skeletal malformations, corneal clouding, hepatosplenomegaly, and cardiac abnormalities. A wide variation in clinical severity is observed. Arylsulfatase B activity is defective in multiple sulfatase deficiency (MSD). A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Arylsulfatase B activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSB at residue Cys- 91 that is not converted to 3-oxoalanine. Belongs to the sulfatase family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: EC 3.1.6.12; Hydrolase; Glycan Metabolism - glycosaminoglycan degradation. Chromosomal Location of Human Ortholog: 5q14.1. Cellular Component: cell surface; endoplasmic reticulum lumen; Golgi apparatus; lysosomal lumen; lysosome; mitochondrion; rough endoplasmic reticulum. Molecular Function: arylsulfatase activity; metal ion binding; N-acetylgalactosamine-4-sulfatase activity. Biological Process: autophagy; carbohydrate metabolic process; cellular protein metabolic process; central nervous system development; chondroitin sulfate catabolic process; chondroitin sulfate metabolic process; glycosaminoglycan metabolic process; glycosphingolipid metabolic process; lysosomal transport; lysosome organization and biogenesis; post-translational protein modification; response to estrogen stimulus; response to methylmercury; response to nutrient; response to pH; sphingolipid metabolic process. Disease: Mucopolysaccharidosis Type Vi

0.05 mg (E-Coli)

180 USD

0.05 mg (Yeast)

260

0.2 mg (E-Coli)

490

0.2 mg (Yeast)

600

0.5 mg (E-Coli)

715