Catenin beta-1 (CTNNB1), human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 2-781aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: ATQADLMELD MAMEPDRKAA VSHWQQQSYL DSGIHSGATT TAPSLSGKGN PEEEDVDTSQ VLYEWEQGFS QSFTQEQVAD IDGQYAMTRA QRVRAAMFPE TLDEGMQIPS TQFDAAHPTN VQRLAEPSQM LKHAVVNLIN YQDDAELATR AIPELTKLLN DEDQVVVNKA AVMVHQLSKK EASRHAIMRS PQMVSAIVRT MQNTNDVETA RCTAGTLHNL SHHREGLLAI FKSGGIPALV KMLGSPVDSV LFYAITTLHN LLLHQEGAKM AVRLAGGLQK MVALLNKTNV KFLAITTDCL QILAYGNQES KLIILASGGP QALVNIMRTY TYEKLLWTTS RVLKVLSVCS SNKPAIVEAG GMQALGLHLT DPSQRLVQNC LWTLRNLSDA ATKQEGMEGL LGTLVQLLGS DDINVVTCAA GILSNLTCNN YKNKMMVCQV GGIEALVRTV LRAGDREDIT EPAICALRHL TSRHQEAEMA QNAVRLHYGL PVVVKLLHPP SHWPLIKATV GLIRNLALCP ANHAPLREQG AIPRLVQLLV RAHQDTQRRT SMGGTQQQFV EGVRMEEIVE GCTGALHILA RDVHNRIVIR GLNTIPLFVQ LLYSPIENIQ RVAAGVLCEL AQDKEAAEAI EAEGATAPLT ELLHSRNEGV ATYAAAVLFR MSEDKPQDYK KRLSVELTSS LFRTEPMAWN ETADLGLDIG AQGEPLGYRQ DDPSYRSFHS GGYGQDALGM DPMMEHEMGG HHPGADYPVD GLPDLGHAQD LMDGLPPGDS NQLAWFDTDL. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML . Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle . Reference: Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver.Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F. NIEHS SNPs programComplete 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). Function: nan