Aspartyl/asparaginyl beta-hydroxylase Recombinant Protein | ASPH recombinant protein

Recombinant Human Aspartyl/asparaginyl beta-hydroxylase

Cat. Num. AAA969472

• Gene Names: ASPH; AAH; BAH; HAAH; JCTN; FDLAB; junctin; CASQ2BP1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Aspartyl/asparaginyl beta-hydroxylase; Recombinant Human Aspartyl/asparaginyl beta-hydroxylase; Aspartate beta-hydroxylase; ASP beta-hydroxylase; Peptide-aspartate beta-dioxygenase; ASPH 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: 75-270aa; Partial of Isoform 6
• Sequence: FDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPDT
• Sequence Length: 729

• 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 ASPH recombinant protein

Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.

Product Categories/Family for ASPH recombinant protein

Signal Transduction

References

Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase.Korioth F., Gieffers C., Frey J.Gene 150:395-399(1994) Overexpression of human aspartyl(asparaginyl) beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma.Lavaissiere L., Jia S., Nishiyama M., de la Monte S., Stern A.M., Wands J.R., Friedman P.A.J. Clin. Invest. 98:1313-1323(1996) cDNA cloning and characterization of human cardiac junctin.Lim K.Y., Hong C.-S., Kim D.H.Gene 255:35-42(2000) Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin.Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J., O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F., Friedman P.A.J. Biol. Chem. 275:39543-39554(2000) Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo) plasmic reticulum membrane.Treves S., Feriotto G., Moccagatta L., Gambari R., Zorzato F.J. Biol. Chem. 275:39555-39568(2000) Molecular cloning of junctin from human and developing rabbit heart.Wetzel G.T., Ding S., Chen F.Mol. Genet. Metab. 69:252-258(2000) 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) DNA sequence and analysis of human chromosome 8.Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.Nature 439:331-335(2006)

NCBI and Uniprot Product Information

• NCBI GI #: 258613943
• NCBI GeneID: 444
• NCBI Accession #: NP_001158222.1
• NCBI GenBank Nucleotide #: NM_001164750.1
• UniProt Accession #: Q12797; Q6NXR7; Q8TB28; Q9H291; Q9H2C4; A6NDF4; A6NHI2; B4DIC9; B4E2K4; B7ZM95; E5RGP5; F5H667
• Molecular Weight: 38.2 kDa
• NCBI Official Full Name: aspartyl/asparaginyl beta-hydroxylase isoform f
• NCBI Official Synonym Full Names: aspartate beta-hydroxylase
• NCBI Official Symbol: ASPH
• NCBI Official Synonym Symbols: AAH; BAH; HAAH; JCTN; FDLAB; junctin; CASQ2BP1
• NCBI Protein Information: aspartyl/asparaginyl beta-hydroxylase
• UniProt Protein Name: Aspartyl/asparaginyl beta-hydroxylase
• Protein Family: Aspartyl/asparaginyl beta-hydroxylase
• UniProt Gene Name: ASPH
• UniProt Synonym Gene Names: BAH; ASP beta-hydroxylase
• UniProt Entry Name: ASPH_HUMAN

NCBI Description

This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis. [provided by RefSeq, Sep 2009]

Uniprot Description

ASPH: Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. Belongs to the aspartyl/asparaginyl beta-hydroxylase family. 9 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; EC 1.14.11.16; Oxidoreductase

Chromosomal Location of Human Ortholog: 8q12.1

Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; integral to endoplasmic reticulum membrane; integral to membrane; plasma membrane; sarcoplasmic reticulum lumen; sarcoplasmic reticulum membrane

Molecular Function: calcium ion binding; electron carrier activity; peptide-aspartate beta-dioxygenase activity; protein binding; structural constituent of muscle; structural molecule activity

Biological Process: activation of store-operated calcium channel activity; detection of calcium ion; limb morphogenesis; muscle contraction; negative regulation of cell proliferation; palate development; pattern specification process; peptidyl-aspartic acid hydroxylation; positive regulation of proteolysis; positive regulation of transcription, DNA-dependent; regulation of inositol-1,4,5-triphosphate receptor activity; regulation of protein stability; response to ATP; transmembrane transport