Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit Recombinant Protein | DDOST recombinant protein

Recombinant Human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit

Cat. Num. AAA717401

• Gene Names: RPN1; OST1; RBPH1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit; Recombinant Human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit; Dolichyl-diphosphooligosaccharide-protein glycosyltransferase 67 kDa subunit; Ribophorin I; RPN-I; Ribophorin-1; DDOST recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 44-427aa; Partial
• Sequence: SHLAKVTAEVVLAHLGGGSTSRATSFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKISVIVETVYTHVLHPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIEIDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVH
• Sequence Length: 607

• 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 DDOST recombinant protein

Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.

References

Human ribophorins I and II the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins.Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.EMBO J. 6:75-82(1987) 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 full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007)

NCBI and Uniprot Product Information

• NCBI GI #: 4506675
• NCBI GeneID: 6184
• NCBI Accession #: NP_002941.1
• NCBI GenBank Nucleotide #: NM_002950.3
• UniProt Accession #: P04843; Q68DT1; B2R5Z0; D3DNB6
• Molecular Weight: 70.6 kDa
• NCBI Official Full Name: dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
• NCBI Official Synonym Full Names: ribophorin I
• NCBI Official Symbol: RPN1
• NCBI Official Synonym Symbols: OST1; RBPH1
• NCBI Protein Information: dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
• UniProt Protein Name: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
• Protein Family: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase
• UniProt Gene Name: RPN1
• UniProt Synonym Gene Names: RPN-I
• UniProt Entry Name: RPN1_HUMAN

NCBI Description

This gene encodes a type I integral membrane protein found only in the rough endoplasmic reticulum. The encoded protein is part of an N-oligosaccharyl transferase complex that links high mannose oligosaccharides to asparagine residues found in the Asn-X-Ser/Thr consensus motif of nascent polypeptide chains. This protein forms part of the regulatory subunit of the 26S proteasome and may mediate binding of ubiquitin-like domains to this proteasome. [provided by RefSeq, Jul 2008]

Uniprot Description

RPN1: Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Belongs to the OST1 family.

Protein type: Membrane protein, integral; EC 2.4.99.18; Transferase; Glycan Metabolism - N-glycan biosynthesis

Chromosomal Location of Human Ortholog: 3q21.3

Cellular Component: endoplasmic reticulum membrane; integral to membrane; melanosome; membrane; oligosaccharyl transferase complex; rough endoplasmic reticulum

Molecular Function: dolichyl-diphosphooligosaccharide-protein glycotransferase activity; protein binding

Biological Process: cellular protein metabolic process; gene expression; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine; protein modification process; SRP-dependent cotranslational protein targeting to membrane; translation