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Recombinant Human herpesvirus 2 Ribonucleoside-diphosphate reductase large subunit (UL39), partial

Recombinant Human herpesvirus 2 Ribonucleoside-diphosphate reductase large subunit (UL39), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

RIR1

Uniprot NO.

P89462

Species

Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)

Source

Yeast

Expression Region

1-1142

Target Protein Sequence

MANRPAASAL AGARSPSERQ EPREPEVAPP GGDHVFCRKV SGVMVLSSDP PGPAAYRISD SSFVQCGSNC SMIIDGDVAR GHLRDLEGAT STGAFVAISN VAAGGDGRTA VVALGGTSGP SATTSVGTQT SGEFLHGNPR TPEPQGPQAV PPPPPPPFPW GHECCARRDA RGGAEKDVGA AESWSDGPSS DSETEDSDSS DEDTGSETLS RSSSIWAAGA TDDDDSDSDS RSDDSVQPDV VVRRRWSDGP APVAFPKPRR PGDSPGNPGL GAGTGPGSAT DPRASADSDS AAHAAAPQAD VAPVLDSQPT VGTDPGYPVP LELTPENAEA VARFLGDAVD REPALMLEYF CRCAREESKR VPPRTFGSAP RLTEDDFGLL NYALAEMRRL CLDLPPVPPN AYTPYHLREY ATRLVNGFKP LVRRSARLYR ILGVLVHLRI RTREASFEEW MRSKEVDLDF GLTERLREHE AQLMILAQAL NPYDCLIHST PNTLVERGLQ SALKYEEFYL KRFGGHYMES VFQMYTRIAG FLACRATRGM RHIALGRQGS WWEMFKFFFH RLYDHQIVPS TPAMLNLGTR NYYTSSCYLV NPQATTNQAT LRAITGNVSA ILARNGGIGL CMQAFNDASP GTASIMPALK VLDSLVAAHN KQSTRPTGAC VYLEPWHSDV RAVLRMKGVL AGEEAQRCDN IFSALWMPDL FFKRLIRHLD GEKNVTWSLF DRDTSMSLAD FHGEEFEKLY EHLEAMGFGE TIPIQDLAYA IVRSAATTGS PFIMFKDAVN RHYIYDTQGA AIAGSNLCTE IVHPASKRSS GVCNLGSVNL ARCVSRQTFD FGRLRDAVQA CVLMVNIMID STLQPTPQCT RGNDNLRSMG IGMQGLHTAC LKMGLDLESA EFRDLNTHIA EVMLLAAMKT SNALCVRGAR PFSHFKRSMY RAGRFHWERF SNASPRYEGE WEMLRQSMMK HGLRNSQFIA LMPTAASAQI SDVSEGFAPL FTNLFSKVTR DGETLRPNTL LLKELERTFG GKRLLDAMDG LEAKQWSVAQ ALPCLDPAHP LRRFKTAFDY DQELLIDLCA DRAPYVDHSQ SMTLYVTEKA DGTLPASTLV RLLVHAYKRG LKTGMYYCKV RKATNSGVFA GDDNIVCTSC AL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

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.

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Target Background

Function(From Uniprot)

Ribonucleoside-diphosphate reductase holoenzyme that provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells, as well as reactivation from latency in infected hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. The N-terminal region confers antiapoptotic activity in differentiated cells such as neurons and is important for viral reactivation to increase neural survivability. Prevents host necroptosis by targeting host RIPK1 and RIPK3, thereby hampering the formation of necroptotic RIPK1-RIPK3 complexes. May form hetero-amyloid structures with host proteins RIPK3 or ZBP1, thereby preventing RIPK3- and ZBP1-mediated necroptosis. In addition, inhibits extrinsic apoptosis by targeting host CASP8.

Gene References into Functions

The ribonucleotide reductase large subunit R1 was sufficient to suppress TNF-induced necrosis, and its RIP homotypic interaction motif (RHIM) domain was required to disrupt the RIP1/RIP3 complex in human cells. PMID:26559832
Thus, by interacting with caspase 8 and RIP1, HSV R1s impair the apoptotic host defense mechanism prompted by dsRNA. PMID:21697465
may contribute to HSV-2 reactivation by increasing neuronal survival PMID:16162476
by constructing N- and C-terminal deletions in HSV-2 R1, we mapped the domain of HSV-2 R1 involved in its antiapoptotic potential PMID:17251554