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RPL17 recombinant protein :: 60S ribosomal protein L17 Recombinant Protein

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Catalog # MBS717067
Unit / Price
Scan QR to view Datasheet
  0.01 mg  /  $160 +1 FREE 8GB USB
  0.05 mg  /  $200 +1 FREE 8GB USB
  0.1 mg  /  $295 +1 FREE 8GB USB
  0.2 mg  /  $480 +1 FREE 8GB USB
  0.5 mg  /  $790 +1 FREE 8GB USB
  1 mg  /  $1,215 +1 FREE 8GB USB
SDS-PAGE
Product Name

60S ribosomal protein L17 (RPL17), Recombinant Protein

Full Product Name

Recombinant Human 60S ribosomal protein L17

Product Synonym Names
60S ribosomal protein L23; PD-1
Matching Pairs
Antibody: RPL17 (MBS7041793)
Standard: 60S ribosomal protein L17 (MBS717067)
Comments: Standards are recommendations only. Compatibility of the standards in the user developed application needs to be established and confirmed by the researcher.
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
2-184aa; Full Length
Sequence
VRYSLDPENP TKSCKSRGSN LRVHFKNTRE TAQAIKGMHI RKATKYLKDV TLQKQCVPFR RYNGGVGRCA QAKQWGWTQG RWPKKSAEFL LHMLKNAESN AELKGLDVDS LVIEHIQVNK APKMRRRTYR AHGRINPYMS SPCHIEMILT EKEQIVPKPE EEVAQKKKIS QKKLKKQKLM ARE
OMIM
603661
3D Structure
ModBase 3D Structure for P18621
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of RPL17 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

RPL17 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for RPL17. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
48.7kD
NCBI Official Full Name
60S ribosomal protein L17 isoform a
NCBI Official Synonym Full Names
ribosomal protein L17
NCBI Official Symbol
RPL17  [Similar Products]
NCBI Official Synonym Symbols
L17; PD-1; RPL23
  [Similar Products]
NCBI Protein Information
60S ribosomal protein L17
UniProt Protein Name
60S ribosomal protein L17
UniProt Synonym Protein Names
60S ribosomal protein L23; PD-1
Protein Family
UniProt Gene Name
RPL17  [Similar Products]
UniProt Entry Name
RL17_HUMAN
NCBI Summary for RPL17
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22P family of ribosomal proteins. It is located in the cytoplasm. This gene has been referred to as rpL23 because the encoded protein shares amino acid identity with ribosomal protein L23 from Halobacterium marismortui; however, its official symbol is RPL17. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream C18orf32 (chromosome 18 open reading frame 32) gene. [provided by RefSeq, Dec 2010]
UniProt Comments for RPL17
RPL17: a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22P family of ribosomal proteins. It is located in the cytoplasm. This gene has been referred to as rpL23 because the encoded protein shares amino acid identity with ribosomal protein L23 from Halobacterium marismortui; however, its official symbol is RPL17. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the neighboring downstream C18orf32 (chromosome 18 open reading frame 32) gene. [provided by RefSeq, Dec 2010]

Protein type: Ribosomal; Translation

Chromosomal Location of Human Ortholog: 18q21

Cellular Component: cytosol; nucleus

Molecular Function: structural constituent of ribosome

Biological Process: cellular protein metabolic process; gene expression; mRNA catabolic process, nonsense-mediated decay; selenium metabolic process; selenocysteine metabolic process; SRP-dependent cotranslational protein targeting to membrane; translation; translational elongation; translational initiation; translational termination; viral infectious cycle; viral reproduction; viral transcription
Product References and Citations for RPL17 recombinant protein
A human gene related to the ribosomal protein L23 gene of Halobacterium marismortui.Mager D.L., Freeman J.D.Nucleic Acids Res. 18:5301-5301(1990) Isolation and characterization of a complementary DNA (PD-1) differentially expressed by human pancreatic ductal cell tumors.Batra S.K., Metzgar R.S., Hollingsworth M.A.Cell Growth Differ. 2:385-390(1991) The human ribosomal protein genes sequencing and comparative analysis of 73 genes.Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.Genome Res. 12:379-390(2002) 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) Li W.B., Gruber C., Jessee J., Polayes D. DNA sequence and analysis of human chromosome 18.Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.Nature 437:551-555(2005)

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