J-Perk v6.08 serial key or number
J-Perk v6.08 serial key or number
THE CAR HACKER’S HANDBOOK
2
BUS PROTOCOLS
In this chapter, we’ll discuss the different bus protocols common in vehicle communications. Your vehicle may have only one of these, or if it was built earlier than , it may have none.
Bus protocols govern the transfer of packets through the network of your vehicle. Several networks and hundreds of sensors communicate on these bus systems, sending messages that control how the vehicle behaves and what information the network knows at any given time.
Each manufacturer decides which bus and which protocols make the most sense for its vehicle. One protocol, the CAN bus, exists in a standard location on all vehicles: on the OBD-II connector. That said, the packets themselves that travel over a vehicle’s CAN bus aren’t standardized.
Vehicle-critical communication, such as RPM management and braking, happens on high-speed bus lines, while noncritical communication, such as door lock and A/C control, happens on mid- to low-speed bus lines.
We’ll detail the different buses and protocols you may run across on your vehicle. To determine the bus lines for your specific vehicle, check its OBD-II pinout online.
The CAN Bus
CAN is a simple protocol used in manufacturing and in the automobile industry. Modern vehicles are full of little embedded systems and electronic control units (ECUs) that can communicate using the CAN protocol. CAN has been a standard on US cars and light trucks since , but it wasn’t made mandatory until ( for European vehicles). If your car is older than , it still may have CAN, but you’ll need to check.
CAN runs on two wires: CAN high (CANH) and CAN low (CANL). CAN uses differential signaling (with the exception of low-speed CAN, discussed in “The GMLAN Bus” on page 20), which means that when a signal comes in, CAN raises the voltage on one line and drops the other line an equal amount (see Figure ). Differential signaling is used in environments that must be fault tolerant to noise, such as in automotive systems and manufacturing.
Figure CAN differential signaling
Figure shows a signal captured using a PicoScope, which listens to both CANH (darker lines at the top of the graph) and CANL (lighter lines at the bottom of the graph). Notice that when a bit is transmitted on the CAN bus, the signal will simultaneously broadcast both 1V higher and lower. The sensors and ECUs have a transceiver that checks to ensure both signals are triggered; if they are not, the transceiver rejects the packet as noise.
The two twisted-pair wires make up the bus and require the bus to be terminated on each end. There’s a ohm resistor across both wires on the termination ends. If the module isn’t on the end of the bus, it doesn’t have to worry about termination. As someone who may tap into the lines, the only time you’ll need to worry about termination is if you remove a terminating device in order to sniff the wires.
The OBD-II Connector
Many vehicles come equipped with an OBD-II connector, also known as the diagnostic link connector (DLC), which communicates with the vehicle’s internal network. You’ll usually find this connector under the steering column or hidden elsewhere on the dash in a relatively accessible place. You may have to hunt around for it, but its outline looks similar to that in Figure
Figure Possible locations of the OBD-II connector
In some vehicles, you’ll find these connectors behind small access panels. They’ll typically be either black or white. Some are easy to access, and others are tucked up under the plastic. Search and you shall find!
Finding CAN Connections
CAN is easy to find when hunting through cables because its resting voltage is V. When a signal comes in, it’ll add or subtract 1V (V or V). CAN wires run through the vehicle and connect between the ECUs and other sensors, and they’re always in dual-wire pairs. If you hook up a multimeter and check the voltage of wires in your vehicle, you’ll find that they’ll be at rest at V or fluctuating by 1V. If you find a wire transmitting at V, it’s almost certainly CAN.
You should find the CANH and CANL connections on pins 6 and 14 of your OBD-II connector, as shown in Figure
Figure CAN pins cable view on the OBD-II connector
In the figure, pins 6 and 14 are for standard high-speed CAN lines (HS-CAN). Mid-speed and low-speed communications happen on other pins. Some cars use CAN for the mid-speed (MS-CAN) and low-speed (LS-CAN), but many vehicles use different protocols for these communications.
You’ll find that not all buses are exposed via the OBD-II connector. You can use wiring diagrams to help locate additional “internal” bus lines.
CAN Bus Packet Layout
There are two types of CAN packets: standard and extended. Extended packets are like standard ones but with a larger space to hold IDs.
Standard Packets
Each CAN bus packet contains four key elements:
Arbitration ID The arbitration ID is a broadcast message that identifies the ID of the device trying to communicate, though any one device can send multiple arbitration IDs. If two CAN packets are sent along the bus at the same time, the one with the lower arbitration ID wins.
Identifier extension (IDE) This bit is always 0 for standard CAN.
Data length code (DLC) This is the size of the data, which ranges from 0 to 8 bytes.
Data This is the data itself. The maximum size of the data carried by a standard CAN bus packet can be up to 8 bytes, but some systems force 8 bytes by padding out the packet.
Figure shows the format of standard CAN packets.
Figure Format of standard CAN packets
Because CAN bus packets are broadcast, all controllers on the same network see every
PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia
Abstract
The PERK-eIF2α branch of the Unfolded Protein Response (UPR) mediates the transient shutdown of translation in response to rising levels of misfolded proteins in the endoplasmic reticulum. PERK and eIF2α activation are increasingly recognised in postmortem analyses of patients with neurodegenerative disorders, including Alzheimer’s disease, the tauopathies and prion disorders. These are all characterised by the accumulation of misfolded disease-specific proteins in the brain in association with specific patterns of neuronal loss, but the role of UPR activation in their pathogenesis is unclear. In prion-diseased mice, overactivation of PERK-P/eIF2α-P signalling results in the sustained reduction in global protein synthesis, leading to synaptic failure, neuronal loss and clinical disease. Critically, restoring vital neuronal protein synthesis rates by inhibiting the PERK-eIF2α pathway, both genetically and pharmacologically, prevents prion neurodegeneration downstream of misfolded prion protein accumulation. Here we show that PERK-eIF2α-mediated translational failure is a key process leading to neuronal loss in a mouse model of frontotemporal dementia, where the misfolded protein is a form of mutant tau. rTg mice, which overexpress the PL tau mutation, show dysregulated PERK signalling and sustained repression of protein synthesis by 6 months of age, associated with onset of neurodegeneration. Treatment with the PERK inhibitor, GSK, from this time point in mutant tau-expressing mice restores protein synthesis rates, protecting against further neuronal loss, reducing brain atrophy and abrogating the appearance of clinical signs. Further, we show that PERK-eIF2α activation also contributes to the pathological phosphorylation of tau in rTg mice, and that levels of phospho-tau are lowered by PERK inhibitor treatment, providing a second mechanism of protection. The data support UPR-mediated translational failure as a generic pathogenic mechanism in protein-misfolding disorders, including tauopathies, that can be successfully targeted for prevention of neurodegeneration.
Introduction
Endoplasmic reticulum (ER) stress and its associated Unfolded Protein Response (UPR) are emerging as major common themes in neurodegenerative disorders [13, 33]. The modulation of proteostasis is increasingly a potential therapeutic target in a wide range of human diseases associated with protein misfolding [12]. The UPR involves three major signalling cascades that enable the cell to deal with the build up of misfolded (or unfolded) proteins, which are detected by sensors within the ER [30]. One branch of the UPR, mediated by protein kinase RNA (PKR)-like/Pancreatic ER kinase (PERK), leads to the transient shutdown of protein synthesis. Activated (phosphorylated) PERK (PERK-P) phosphorylates the alpha subunit of eukaryotic initiation factor 2 (eIF2α); this inhibits the initiation of translation and induces expression of the transcription factor ATF4, and associated downstream signalling events, including induction of GADD34, the stress-induced eIF2α-P-specific phosphatase. (eIF2α can also be phosphorylated by other kinases as part of the integrated stress response (ISR), in response to cellular stresses such as viral infection and amino acid starvation). Increased PERK-P and eIF2α-P have been reported in postmortem analyses of brains from patients with Alzheimer’s disease (AD), Parkinson’s disease (PD) and the tauopathies Progressive Supranuclear Palsy (PSP) and Frontotemporal Dementia (FTD), as well as in prion disease [3, 15, 16, 37, 38]. In AD patients, UPR activation is thought to occur early in disease pathology in association with the accumulation of abnormal phosphorylated tau in neurons, but before neurofibrillary tangle formation [16, 26]. PERK-P staining has also been shown to be associated with phospho-tau-positive neurons in CA1 and dentate gyrus and subiculum regions of the hippocampus in FTD-tau cases [26].
However, it is unclear what the pathological significance of these findings is for the human diseases; specifically, whether they reflect activation of a protective mechanism or the signature of a pathogenic process (see Scheper and Hoozemans, for review [33]). This is of key significance for both mechanistic understanding and for development of potential treatments. Important insights come from animal models. PERK branch UPR overactivation occurs in several mouse models of neurodegenerative disease, including AD [1, 9, 13], prion [24], tauopathy [1, 18] and ALS [3, 32]. In prion-diseased mice, accumulation of misfolded prion protein (PrP) causes persistently high levels of PERK-P and eIF2α-P, and hence sustained translational failure. This results in a catastrophic decline in levels of key synaptic proteins, leading to synaptic failure and ultimately to neuronal loss [24]. This is true for both PrP overexpressing mice and for wild-type mice, supporting that PERK-eIF2α overactivation is not an artefact of high levels of protein expression, but occurs at endogenous levels (consistent with observations in humans). Critically, both genetic manipulations that reduce eIF2α-P levels [24] and pharmacological inhibition of PERK using the inhibitor GSK [4], or with the small molecule inhibitor, ISRIB, which acts downstream of eIF2α-P, restored vital protein synthesis rates and prevented neurodegeneration and clinical disease in prion-infected mice [11, 23, 24]. In contrast, pharmacological treatment preventing the reduction of eIF2α-P levels accelerated disease and exacerbated toxicity in prion-diseased mice [24]. Given the range of neurodegenerative diseases in which PERK branch UPR dysregulation is seen, it is crucial to understand its role in mediating neuronal loss in protein-misfolding disorders more broadly, particularly in AD and other dementias. This will also help determine its potential as a therapeutic target in these disorders. Wider relevance of the pathway in AD is supported by the fact that both PERK haploinsufficiency [9] and genetic suppression of other eIF2α kinases [21] rescue memory deficits and neurodegeneration in mouse models of AD. Indeed, neuronal eIF2α-P levels—and hence rates of protein synthesis—in wild-type mice are key to learning and memory [6], and pharmacological inhibition of eIF2α-P signalling boosts cognition [35]. Further, with relevance for AD and other tauopathies, PERK branch UPR activation is also known to contribute to the phosphorylation of tau—which is central to pathology in these diseases—both in vitro and in vivo [14, 20, 39]. In vitro, this has been shown to be due to PERK-mediated induction of glycogen synthase kinase-3 (GSK3β), a serine/threonine kinase that phosphorylates tau at disease-relevant epitopes [25], an effect that can be reversed by PERK inhibition [39]. Thus, UPR activation may have a dual pathological role in tauopathies, impacting on two processes fundamental to neurodegeneration in these disorders.
We have now examined the role of PERK pathway activation in the rTg mouse model of FTD caused by the human tau PL mutation [29, 31]. Mice positive for the mutant tau transgene (tau+PL) show high levels of PL tau expression throughout their lives, with age-related tau pathology, progressive memory deficits and, importantly, extensive forebrain neurodegeneration from months of age [29, 31]. Tau+PL rTg mice show abnormal conformations of tau from months, with pre-tangle hyperphosphorylated tau detected by 4 months of age, with the appearance of mature neurofibrillary tangles and neurodegeneration in the hippocampus from months. Neuronal loss becomes widespread throughout the forebrain after 7 months of age, leading to marked forebrain atrophy associated with clinical signs of poor grooming and motor impairment. Transgene-negative (tau−PL) rTg mice have normal brain morphology, behaviour and appearance and do not show phosphorylated tau [29, 31]. Increased levels of PERK-P in the brain of these mice have been reported during later disease stages (from 9 months), although the role of PERK-P signalling in mediating neurodegeneration in these animals has not previously been examined [1].
We first confirmed activation of PERK-eIF2α signalling in rTg mice due to mutant tau expression. We then examined the effects of therapeutic inhibition of PERK signalling on both rates of neuronal protein synthesis and on tau phosphorylation and their role in neurodegeneration in these animals.
Methods
Mice
All animal work conformed to the UK Home Office regulations and institutional guidelines. rTg tau+PL and tau−PL mice were obtained from Eli Lilly and Company. Treatment with doxycycline was performed from 4 months of age, by oral dosing as described [31]. rTg mice were given two oral (bolus) doses of 10 mg/kg, then followed by Harlan Teklad T, diet with doxycycline mg/kg in chow (n = 6 female mice). Treatment with GSK was by oral gavage twice daily with 50 mg/kg GSK suspended in vehicle ( % HPMC + % Tween in H2O at pH ) (n = 10 male), or with vehicle alone (n = 8 male) as described [23] from ~6 months of age.
Western blotting
Protein extraction from hippocampi and immunoblots of UPR and synaptic proteins were performed as described [23, 24]. Proteins were detected with the following antibodies: eIF2α-P (S51) (; , Cell Signaling) and eIF2α (L57A5) (; , Cell Signaling), ATF4 (CREB-2, ; sc, Santa Cruz), GADD34 (, AP, Proteintech), PERK-P (, , Santa Cruz), PERK (, , Cell Signaling), SNAP25 (,, ab, Abcam), PSD (, EPY, Millipore) total tau (Tau 5, , AHB, Invitrogen), GSK3β (, , Cell Signaling), pSer9-GSK3β (, , Cell Signaling) and pTyr/-GSK3α/β (, , Millipore). Horseradish peroxidase (HRP)-conjugated secondary antibodies (,; DAKO) were applied, and protein was visualised using enhanced chemiluminescence (GE Healthcare) and quantitated using ImageJ. Antibodies against GAPDH (; sc, Santa Cruz) and Beta-III-tubulin (, MAB, Millipore) were used to determine loading.
Protein synthesis rates
Global translational levels (protein synthesis rates) were calculated by measuring 35S-methionine incorporation into proteins in acute hippocampal slices, as described [23, 24]. Briefly, slices were incubated with mBq of 35S-methionine label in oxygenated artificial cerebrospinal fluid at 37 °C for 1 h. Incorporation of radiolabel was measured by scintillation counting (WinSpectral, Wallac Inc.). All biochemical analyses were performed in hippocampi from three to four mice.
Histology
Paraffin-embedded brains were sectioned at 5 μm and stained with haematoxylin and eosin or NeuN antibody (; MAB, Millipore) for neuronal counts as described [23, 24]. CA1 pyramidal neuron counts were determined using three serial sections from three to four separate mice [24]. All neuronal counting was performed with the investigator being blind to the sample group being analysed. Immunohistochemistry for pSer/Thr tau was performed using AT8 (; MN, Thermo Scientific). Non-specific binding was blocked prior to primary antibodies using Histostain-Plus Bulk kit (Invitrogen). A biotinylated secondary antibody (Invitrogen) was used and stain visualised by diaminobenzidine reagent. All images were taken on using Axiovision software (Zeiss) and counted using Volocity imaging system (Version ) [24]. Immunofluorescence for pSer/Thr tau was performed using AT8 (; MN, Thermo Scientific) and PERK-P (, , Santa Cruz). Sections were blocked and permeabilized in blocking buffer (2 % donkey serum, % Triton X in TBS) for 1 h and then incubated overnight at 4 °C with primary antibody in TBS+2 % serum. Alexa Fluor nm and nm (, Invitrogen) were then applied for 1 h. Slides were then mounted with VECTASHIELD Mounting media with DAPI (Vector laboratories). All images were taken using Zeiss LSM confocal microscope and counted using Volocity imaging system.
Phospho-tau biochemical analysis
To detect levels of phosphorylated tau in total lysates AlphaScreen assays (Amplified Luminescent Proximity Homogeneous Assay Screen) were performed as described in [2] and as per manufacturer’s instructions. Phospho-tau-specific AT8 (pSer/Thr tau) and PHF1 (pSer/ tau) antibodies were used. Briefly, optimised antibody/acceptor bead mix was incubated overnight at 4 °C with sample lysate or standard diluted in AlphaScreen assay buffer. Next, streptavidin-coated donor beads were added and incubated in the dark at room temperature for 4 h. Plates were read at excitation nm and emission – nm using an Envision plate reader.
XBP1-splicing assay
Total RNA was extracted from hippocampi with the mirVana isolation kit (Ambion). RNA samples were reversed-transcribed with oligo(dT) primers using ImProm-II Reverse Transcriptase (Promega). XBP1 mRNA was amplified with primers flanking the 26b intron (5′-GGAGTGGAGTAAGGCTGGTG and 5′-CCAGAATGCCCAAAAGGATA) using Phusin High-Fidelity taq polymerase (New England Biolabs) [23]. PCR products were resolved on 3 % agarose gels. MEF cells were treated with 5 μg/ml tunicamycin for 6 h and used as a positive control for XBP1 splicing.
Statistics
All statistical analyses were performed using Prism V6 software using Student’s t test for data sets with normal distribution and a single intervention. ANOVA testing was performed using one-way analysis with Tukey’s post hoc test for multiple comparisons.
Results and discussion
High levels of total mutant tau expression lead to activation of the PERK branch of the UPR and sustained translational repression in rTg FTD mice
We assessed PERK branch UPR activation in the brains of rTg mice by measuring levels of eIF2α-P, ATF4, GADD34 and global protein synthesis rates over the course of disease. PL transgene-expressing mice (tau+PL) express high levels of mutant tau from birth (repressible by doxycycline administration [31]). Characteristically, they show memory impairment and hippocampal neuronal loss by 6 months, with widespread forebrain atrophy and overt clinical signs by 8 months [29, 31] (Fig. 1a). We tested mice from 4 months of age. All tau+PL mice expressed high levels of total tau compared to low levels in non-transgenic controls, which express only wild-type (murine) tau (Fig. 1b).
Levels of eIF2α-P and ATF4 were low in all animals until 6 months of age, by which time there was marked elevation of eIF2α-P and ATF4 levels in tau+PL mice compared to non-transgenic littermates (Fig. 1b), consistent with activation of PERK signalling. Interestingly, GADD34 levels did not increase over time (Fig. 1b), which is unexpected given induction of ATF4, but consistent with the effects of PERK branch overactivation seen in prion-infected mice [24]. The failure to induce GADD34 would explain the persistent high levels of eIF2α-P seen in tau+PL older mice (Fig. 1b), again similar to the sustained elevation of eIF2α-P levels seen in prion-diseased mice, both wild type and overexpressing [24]. We found no change in the other two signalling cascades of the UPR involving IREmediated XBP1 splicing (Fig. 1c) and cleavage of ATF6 (data not shown) throughout the time course of disease in rTg transgene-positive mice, consistent with findings in prion-infected mice [23].
Consistent with PERK branch eIF2α-P activation, rates of global protein synthesis measured in brain slices of tau+PL mice had declined to ~40 % of those seen in non-transgenic littermates by 6 months of age, remaining repressed until 11 months (Fig. 1d), after which time the animals were killed. Protein synthesis rates were normal up to 5 months of age, suggesting the onset of sustained translational repression is between 5 and 6 months (Fig. 1d). Levels of the pre- and post-synaptic proteins SNAP25 and PSD were equivalent in transgene-positive and -negative mice at 4 months, but reduced in tau+PL mice at 6 months (Fig. 1e), reflecting the drop in protein synthesis due to high levels of eIF2α-P at this time. As in prion-diseased mice [24], the onset of eIF2α-P-mediated translational repression was closely associated with onset of neurodegeneration at 6 months in rTg mice, which is absent at 4 months (Fig. 1f).
To confirm that activation of PERK-eIF2α-P signalling is indeed the result of mutant tau expression in rTg tau+PL mice, we tested the effect of repressing tau levels on eIF2α-P and ATF4 levels using doxycycline administration. Treatment of transgene-positive mice with doxycycline from 4 months resulted in marked reduction in total tau levels by 8 months (although not as low as levels in transgene-negative controls that express only murine tau) (Fig. 1g). This produced a corresponding marked reduction in eIF2α-P and ATF4 levels compared to levels seen in untreated tau+PL mice, and equivalent to those seen in non-transgenic mice (Fig. 1g). Our data are, therefore, consistent with UPR activation being a direct result of elevated levels of mutant total tau in these mice. Consistent with this, reduced PERK-P immunostaining after doxycycline treatment in rTg mice has also been reported by others [1].
Thus, the onset of PERK/eIF2α-mediated translational repression is closely associated with synaptic protein loss and onset of neurodegeneration in mutant tau-expressing rTg mice, similar to the temporal relationship between these events in prion-diseased animals [24]. Importantly, although it is true that levels of mutant tau overexpression are very high in this model, the pR5 mouse model of tauopathy in which levels of mutant tau expression are much lower, at ~70 % endogenous tau, also shows UPR activation [17, 18]. This is similar to the detection of PERK/eIF2α activation in prion-diseased mice, which is seen in both PrP overexpressing and wild-type mice [24], and is, therefore, unlikely to reflect an artefact of protein overexpression.
PERK inhibitor treatment reduces eIF2α-P levels and restores global translation rates
Given the known neuroprotective effects of restoring protein synthesis rates in prion-diseased mice downstream of misfolded PrP accumulation [11, 23], we first asked if restoring translation through PERK inhibition in tau transgene-expressing mice was similarly neuroprotective. We treated tau+PL mice with the specific PERK inhibitor GSK [4] or vehicle alone from ~6 months of age, when eIF2α-P levels are known to be elevated (Fig. 1b) and neuronal loss is beginning (Fig. 1f; [31]). (These were proof-of-principle studies, as GSK is known to produce pancreatic toxicity despite profound neuroprotection after prolonged treatment in prion-diseased mice [23]. The question was whether similar neuroprotective effects of reversing translational repression—achieved through PERK inhibition—are seen in this model; not whether GSK is a viable treatment).
rTg tau+PL mice received 50 mg/kg GSK (n = 10) or vehicle (n = 8) by oral gavage twice daily, a dose optimised for good levels of brain penetration, as described in [23], for 2 months (Fig. 2a). At this time point, at 8 months of age, animals were killed for analysis. As predicted, and consistent with previous observations in prion-diseased mice [23], GSK treatment significantly reduced levels of PERK-P, eIF2α-P and ATF4 levels in tau+PL mice, compared to vehicle-treated animals, which showed persistently elevated of levels of these proteins (Fig. 2b, c). Critically, PERK inhibitor treatment restored global protein synthesis rates to normal in 8-month-old tau+PL mice, in contrast to vehicle-treated animals, which showed markedly reduced translation rates at this time point (Fig. 2d). (GSK does not affect eIF2α-P levels and global protein synthesis where the UPR is not activated [23]).
PERK inhibitor treatment is neuroprotective in FTD mice: reducing tau phosphorylation, and brain atrophy and abrogating clinical signs
Importantly, PERK inhibitor treatment was neuroprotective in rTg mice, as in prion-diseased mice [23], partially restoring neuronal numbers, maintaining total brain weight and preventing clinical signs in 8-month-old animals, and preventing any progression of neuronal loss from 6 months of age, when treatment was begun (Fig. 3a–c). Thus, all vehicle-treated tau+PL mice (8/8) showed poor grooming, hunched posture, hind-leg clasping and/or poor mobility by 8 months of age (Fig. 3a, panel ii). In contrast, all PERK inhibitor-treated tau+PL mice (10/10) showed normal grooming, posture and movement at this stage (Fig. 3a, panel iii). Indeed, PERK inhibitor-treated tau+PL mice were indistinguishable clinically from their transgene-negative tau−PL littermates (Fig. 3a, panel i). Histological examination confirmed marked neuroprotection in tau+PL mice treated with GSK, compared to vehicle-treated mice, which showed profound hippocampal neuronal loss (Fig. 3a, compare panels v and vi), characteristic of the extensive forebrain neurodegeneration described in these mice at this stage [31]. GSK treatment resulted in preservation of ~60 % of CA1 neurons at 8 months, compared to ~25 % in vehicle-treated mice at this time (Fig. 3b). The protective effect is notable especially given that treatment begun at 6 months, when neuronal loss is already beginning in the hippocampus (Fig. 1f; [29, 31]). On a macroscopic scale, PERK inhibitor treatment significantly reduced brain atrophy, with greater total brain weights compared to untreated transgene-expressing animals at this stage (Fig. 3c). Both the number of CA1 neurons and brain weights of PERK inhibitor-treated animals at 8 months were very similar to neuronal numbers reported in untreated tau+PL rTg mice at months by other workers [29, 31
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What’s New in the J-Perk v6.08 serial key or number?
Screen Shot
System Requirements for J-Perk v6.08 serial key or number
- First, download the J-Perk v6.08 serial key or number
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You can download its setup from given links:
J-Perk v6.08 serial key or number & Free Download
J-Perk v6.08 serial key or number& Free Download
J-Perk v6.08 serial key or number
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