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TNFSF10 recombinant protein :: Tumor necrosis factor ligand superfamily member 10 Recombinant Protein

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Catalog # MBS717233
Unit / Price
  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

Tumor necrosis factor ligand superfamily member 10 (TNFSF10), Recombinant Protein

Full Product Name

Recombinant Human Tumor necrosis factor ligand superfamily member 10

Product Synonym Names
Apo-2 ligand; Apo-2; LTNF-related apoptosis-inducing ligand; Protein TRAIL; CD253
Product Synonym Gene Name
APO2L; TRAIL[Similar Products]
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
39-281aa; Extracellular Domain
Sequence
TNELKQMQDK YSKSGIACFL KEDDSYWDPN DEESMNSPCW QVKWQLRQLV RKMILRTSEE TISTVQEKQQ NISPLVRERG PQRVAAHITG TRGRSNTLSS PNSKNEKALG RKINSWESSR SGHSFLSNLH LRNGELVIHE KGFYYIYSQT YFRFQEEIKE NTKNDKQMVQ YIYKYTSYPD PILLMKSARN SCWSKDAEYG LYSIYQGGIF ELKENDRIFV SVTNEHLIDM DHEASFFGAF LVG
OMIM
603598
3D Structure
ModBase 3D Structure for P50591
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 TNFSF10 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.
Related Product Information for
TNFSF10 recombinant protein
Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.
Product Categories/Family for TNFSF10 recombinant protein

TNFSF10 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 TNFSF10. 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
55.8kD
NCBI Official Full Name
tumor necrosis factor ligand superfamily member 10 isoform 2
NCBI Official Synonym Full Names
tumor necrosis factor superfamily member 10
NCBI Official Symbol
TNFSF10  [Similar Products]
NCBI Official Synonym Symbols
TL2; APO2L; CD253; TRAIL; Apo-2L; TNLG6A
  [Similar Products]
NCBI Protein Information
tumor necrosis factor ligand superfamily member 10
UniProt Protein Name
Tumor necrosis factor ligand superfamily member 10
UniProt Synonym Protein Names
Apo-2 ligand; Apo-2L; TNF-related apoptosis-inducing ligand; Protein TRAIL; CD_antigen: CD253
UniProt Gene Name
TNFSF10  [Similar Products]
UniProt Synonym Gene Names
APO2L; TRAIL; Apo-2L; Protein TRAIL  [Similar Products]
UniProt Entry Name
TNF10_HUMAN
NCBI Summary for TNFSF10
The protein encoded by this gene is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. This protein binds to several members of TNF receptor superfamily including TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4, and possibly also to TNFRSF11B/OPG. The activity of this protein may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4, and TNFRSF11B/OPG that cannot induce apoptosis. The binding of this protein to its receptors has been shown to trigger the activation of MAPK8/JNK, caspase 8, and caspase 3. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2010]
UniProt Comments for TNFSF10
TRAIL: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis. Homotrimer. Widespread; most predominant in spleen, lung and prostate. Belongs to the tumor necrosis factor family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Cytokine; Membrane protein, integral

Chromosomal Location of Human Ortholog: 3q26

Cellular Component: extracellular region; extracellular space; integral to plasma membrane

Molecular Function: cytokine activity; metal ion binding; protein binding; receptor binding; tumor necrosis factor receptor binding

Biological Process: apoptosis; caspase activation; cell surface receptor linked signal transduction; cell-cell signaling; immune response; negative regulation of caspase activity; positive regulation of apoptosis; positive regulation of caspase activity; positive regulation of I-kappaB kinase/NF-kappaB cascade; programmed cell death; signal transduction
Product References and Citations for TNFSF10 recombinant protein
Identification and characterization of a new member of the TNF family that induces apoptosis.Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K., Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G.Immunity 3:673-682(1995) Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family.Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A.J. Biol. Chem. 271:12687-12690(1996) Isolation of a TRAIL antagonist from the serum of HIV-infected patients.Schnepple D.J., Shepard B., Bren G.D., Cummins N.W., Natesampillai S., Trushin S., Algeciras-Schimnich A., Meng X.W., Sainski A.M., Rizza S.A., Kaufmann S.H., Badley A.D.J. Biol. Chem. 286:35742-35754(2011) Novel TRAIL splice variant TRAIL-delta.Woods D.C., Haugen M.J., Johnson A.L.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 DNA sequence, annotation and analysis of human chromosome 3.Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.Nature 440:1194-1198(2006) A secreted tyrosine kinase acts in the extracellular environment.Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr., Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.Cell 158:1033-1044(2014) Triggering cell death the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., Kelley R.F., Ashkenazi A., de Vos A.M.Mol. Cell 4:563-571(1999) Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation.Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y., Screaton G.R.Nat. Struct. Biol. 6:1048-1053(1999) 2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity.Cha S.-S., Kim M.S., Choi Y.H., Sung B.J., Shin N.K., Shin H.C., Sung Y.C., Oh B.-H.Immunity 11:253-261(1999)

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Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

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