Arylsulfatase B Recombinant Protein | ARSB recombinant protein

Recombinant Human Arylsulfatase B

Cat. Num. AAA113379

• Gene Names: ARSB; ASB; G4S; MPS6
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Arylsulfatase B; N/A; Recombinant Human Arylsulfatase B; N-acetylgalactosamine-4-sulfatase; G4S; ARSB recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 37-533aa; Full Length of Mature Protein
• Sequence: SGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for ARSB recombinant protein

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.

Product Categories/Family for ARSB recombinant protein

Cancer

References

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.

NCBI and Uniprot Product Information

• NCBI GI #: 38569405
• NCBI GeneID: 411
• NCBI Accession #: NP_000037.2
• NCBI GenBank Nucleotide #: NM_000046.3
• UniProt Accession #: P15848; Q8N322; Q9UDI9; B2RC20
• Molecular Weight: 58 kDa
• NCBI Official Full Name: arylsulfatase B isoform 1
• NCBI Official Synonym Full Names: arylsulfatase B
• NCBI Official Symbol: ARSB
• NCBI Official Synonym Symbols: ASB; G4S; MPS6
• NCBI Protein Information: arylsulfatase B
• UniProt Protein Name: Arylsulfatase B
• UniProt Gene Name: ARSB
• UniProt Synonym Gene Names: ASB; G4S
• UniProt Entry Name: ARSB_HUMAN