Signal transducer and activator of transcription 3 (STAT3), partial, human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 127-688aa. Protein Length: Partial. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: GQANHPTAAV VTEKQQMLEQ HLQDVRKRVQ DLEQKMKVVE NLQDDFDFNY KTLKSQGDMQ DLNGNNQSVT RQKMQQLEQM LTALDQMRRS IVSELAGLLS AMEYVQKTLT DEELADWKRR QQIACIGGPP NICLDRLENW ITSLAESQLQ TRQQIKKLEE LQQKVSYKGD PIVQHRPMLE ERIVELFRNL MKSAFVVERQ PCMPMHPDRP LVIKTGVQFT TKVRLLVKFP ELNYQLKIKV CIDKDSGDVA ALRGSRKFNI LGTNTKVMNM EESNNGSLSA EFKHLTLREQ RCGNGGRANC DASLIVTEEL HLITFETEVY HQGLKIDLET HSLPVVVISN ICQMPNAWAS ILWYNMLTNN PKNVNFFTKP PIGTWDQVAE VLSWQFSSTT KRGLSIEQLT TLAEKLLGPG VNYSGCQITW AKFCKENMAG KGFSFWVWLD NIIDLVKKYI LALWNEGYIM GFISKERERA ILSTKPPGTF LLRFSESSKE GGVTFTWVEK DISGKTQIQS VEPYTKQQLN NMSFAEIIMG YKIMDATNIL VSPLVYLYPD IPKEEAFGKY CR. Purity: Greater than 90% 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: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1. Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. May play an apoptotic role by transctivating BIRC5 expression under LEP activation. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion. Reference: SeattleSNPs variation discovery resourceDNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.Nature 440:1045-1049(2006). Function: nan