Nucleotide Analogs - Jena Bioscience

Recombinant Proteins
206
HIV-1 Nef protein
(full length, 1-210) His
Recombinant, E. coli
Cat. No. Amount Price (€)
PR-381 50 µg 200,--
Liquid. Supplied as ca. 1 mg/ml solution in PBS.
Recombinant N-terminal His-tagged full-length HIV-1
Nef protein (SF2 strain).
Human immunodefi ciency virus type 1 (HIV-1) Nef
is a membrane-associated protein that is produced
at the earliest stage of viral gene expression and
is a component of viral particles. Nef has been
demonstrated to bind and downregulate cell-surface
receptors CD4 and MHC I. In addition, Nef has been
reported to have diverse effects on cellular signal
transduction pathways. It interacts with various cellular
protein kinases and acts both as a kinase substrate
and as a modulator of kinase activity.
Purity: 90% by SDS-PAGE.
Store: 4 °C
Selected references:
Cullen, B. R. (1994) The role of Nef in the replication cycle
of the human and simian immunodefi ciency viruses. Virology
205:1.
Grzesiek et al. (1996) The solution structure of HIV-1 Nef
reveals an unexpected fold and permits delineation of the
binding surface for the SH3 domain of Hck tyrosine protein
kinase. Nat. Struct. Biol. 3:340.
Preusser et al. (2001) Direct in vitro binding of full-length HIV-1
Nef protein to CD4 cytoplasmic domain. J. Virol. 75:3960.
HIV-1 Nef protein (full length,
myr2-210) His , myristoylated
Recombinant, E. coli
Cat. No. Amount Price (€)
PR-382 50 µg 200,--
Liquid. Supplied in 10 mM Tris-HCl, pH 7.8, 50 mM
NaCl and 2 mM DTE.
Recombinant myristoylated full-length HIV-1 Nef
protein (myr2-210, C210S, SF2 strain) with a
C-terminal His-tag. Runs on SDS-PAGE at 33 kD.
Human immunodefi ciency virus type 1 (HIV-1) Nef is
a membrane-associated protein that is produced at an
early stage of viral gene expression and is a component
of viral particles. Nef has been demonstrated to bind
and downregulate cell-surface receptors CD4, MHC
class I and II molecules and DC-SIGN. A Nef mutant
with simple alanine substitutions at the myristoylation
and dileucine sites was impaired in its ability to elicit
Nef-specifi c CD4(+) and CD8(+) T cell responses.
In addition, Nef has been reported to have diverse
effects on cellular signal transduction pathways. It
interacts with various cellular protein kinases and
acts both as a kinase substrate and as a modulator
of kinase activity.
Purity: > 95% by SDS-PAGE.
Store: -80°C
Selected references:
Geyer M. et al. (2001) Structure-function relationships in HIV-1
Nef. EMBO reports 2:580.
Geyer M. and Peterlin B. M. (2001) Domain assembly, surface
accessibility and sequence conservation in full length HIV-1
Nef. FEBS Lett. 496:91.
Fackler O.T. and Baur A.S. (2002) Live and let die: Nef functions
beyond HIV replication. Immunity 16:493.
Peterlin B.M. and Trono D. (2003) Hide, shield and strike
back: how HIV-infected cells avoid immune eradication. Nature
Immun. 3:97.
Doms R.W. and Trono D. (2000) The plasma membrane as a
combat zone in the HIV battlefi eld. Genes Dev. 14:2677.
Liang et al. (2002) Development of HIV-1 Nef vaccine
components: immunogenicity study of Nef mutants lacking
myristoylation and dileucine motif in mice. Vaccine 20:3413.
HIV-2 RT
Recombinant, E. coli
Cat. No. Amount Price (€)
PR-352 10 µg 220,--
Liquid. Supplied as 1 mg/ml solution in 20 mM Tris-
HCl, pH 7.8, 1 mM DTT, 1 mM EDTA, 15% glycerol,
and 0.2% BSA.
HIV-2 Reverse Transcriptase (RT) is used by the
Human Immunodefi ciency Virus-1 to transcribe its
RNA genome into single-stranded DNA. HIV-2 RT
can be used for incorporation of nucleotide analogs
into DNA by RT-PCR or as a standard for assaying
HIV-2 RT activity in human serum. In contrast to
HIV-1 RT, HIV-2 RT is not inhibited by non-nucleoside
RT inhibitors (NNRTI´s).
Purity: > 95% by SDS-PAGE.
Activity: 10.000 U/mg (1 unit is defi ned as the amount
of enzyme that incorporates 1 nmol of dTTP into acidinsoluble
products in 10 min at 37°C)
Store: -80 °C
Selected references:
Pata et al. (2002) Assembly, purifi cation and crystallization of
an active HIV-1 reverse transcriptase initiation complex. Nucl.
Acids Res. 30:4855.
Divita et al. (1995) Dimerization Kinetics of HIV-1 and HIV-2
Reverse Transcriptase – A two step process. J. Mol. Biol. 245:
508.
Mansky et al. (2002) Infl uence of reverse transcriptase variants,
drugs, and Vpr on human immunodefi ciency virus type 1 mutant
frequencies. J. Virol. 77:2071.
Larder et al. (1999) Closing in on HIV drug resistance. Nature
Structural Biology 6:103.
Ren et al. (2002) Structure of HIV-2 reverse transcriptase at
2.35 Å resolution and the mechanism of resistance to nonnucleoside
inhibitors. PNAS 99:14410.
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