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SDS-PAGE

THAP domain-containing protein 11 Recombinant Protein | THAP11 recombinant protein

Recombinant Human THAP domain-containing protein 11

Gene Names
THAP11; RONIN; CTG-B43a; CTG-B45d; HRIHFB2206
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
THAP domain-containing protein 11; Recombinant Human THAP domain-containing protein 11; THAP11 recombinant protein
Ordering
For Research Use Only!
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
1-313aa; Partial
Sequence
MPGFTCCVPGCYNNSHRDKALHFYTFPKDAELRRLWLKNVSRAGVSGCFSTFQPTTGHRLCSVHFQGGRKTYTVRVPTIFPLRGVNERKVARRPAGAAAARRRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQSSPSASTAQTAQLQPNLVSASAAVLLTLQATVDSSQAPGSVQPAPITPTGEDVKPIDLTVQVEFAAAEGAAAAAAASELQAATAGLEAAECPMGPQLVVVGEEGFPDTGSDHSYSLSSGTTEEELLRKLNEQRDILALMEVKMKEMKGSIRHLRLTEAKLREELREKDRLLAMAVIRKKHG
Sequence Length
314
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

SDS-PAGE
Related Product Information for THAP11 recombinant protein
Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic st (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers.
Product Categories/Family for THAP11 recombinant protein
References
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) Searching for interaction partners of the transcription factor REST/NRSF by two-hybrid screening.Santana-Roman H., Curiel-Quesada E., Tapia-Ramirez J.Selection system for genes encoding nuclear-targeted proteins.Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.Nat. Biotechnol. 16:1338-1342(1998) SMARCA2 and THAP11 potential candidates for polyglutamine disorders as evidenced from polymorphism and protein-folding simulation studies.Pandey N., Mittal U., Srivastava A.K., Mukerji M.J. Hum. Genet. 49:596-602(2004) NMR studies of a new family of DNA binding proteins the THAP proteins.Gervais V., Campagne S., Durand J., Muller I., Milon A.J. Biomol. NMR 56:3-15(2013)

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
50.3 kDa
NCBI Official Full Name
THAP domain-containing protein 11
NCBI Official Synonym Full Names
THAP domain containing 11
NCBI Official Symbol
THAP11
NCBI Official Synonym Symbols
RONIN; CTG-B43a; CTG-B45d; HRIHFB2206
NCBI Protein Information
THAP domain-containing protein 11
UniProt Protein Name
THAP domain-containing protein 11
UniProt Gene Name
THAP11
UniProt Entry Name
THA11_HUMAN

NCBI Description

The protein encoded by this gene contains a THAP domain, which is a conserved DNA-binding domain that has striking similarity to the site-specific DNA-binding domain (DBD) of Drosophila P element transposases. [provided by RefSeq, Jul 2008]

Uniprot Description

THAP11: Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers. Belongs to the THAP11 family. Interacts (via coiled coil domain) with HCFC1.

Protein type: DNA-binding

Chromosomal Location of Human Ortholog: 16q22.1

Cellular Component: cytoplasm; intercellular bridge; nucleoplasm

Molecular Function: DNA binding; protein binding; zinc ion binding

Biological Process: regulation of transcription, DNA-dependent; transcription, DNA-dependent

Research Articles on THAP11

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Product Notes

The THAP11 thap11 (Catalog #AAA1399793) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 1-313aa; Partial. The amino acid sequence is listed below: MPGFTCCVPG CYNNSHRDKA LHFYTFPKDA ELRRLWLKNV SRAGVSGCFS TFQPTTGHRL CSVHFQGGRK TYTVRVPTIF PLRGVNERKV ARRPAGAAAA RRRQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQSSPSASTA QTAQLQPNLV SASAAVLLTL QATVDSSQAP GSVQPAPITP TGEDVKPIDL TVQVEFAAAE GAAAAAAASE LQAATAGLEA AECPMGPQLV VVGEEGFPDT GSDHSYSLSS GTTEEELLRK LNEQRDILAL MEVKMKEMKG SIRHLRLTEA KLREELREKD RLLAMAVIRK KHG. It is sometimes possible for the material contained within the vial of "THAP domain-containing protein 11, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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