How can I join a domain on Surface 3: Troubleshooting Common Issues and Errors

You can domain join the Surface Hub to your AD domain to allow users from a specified security group to configure settings. During first run, choose to use Active Directory Domain Services. You'll need to provide credentials that are capable of joining the domain of your choice, and the name of an existing security group. Anyone who is a member of that security group can enter their credentials and unlock Settings.

How can I join a domain on Surface 3 

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If your Surface Hub loses trust with the domain (for example, if you remove the Surface Hub from the domain after it is domain joined), you won't be able to authenticate into the device and open up Settings. If you decide to remove the trust relationship of the Surface Hub with your domain, reset the device first.

You can Azure Active Directory (Azure AD) to join the Surface Hub to allow IT pros from your Azure AD tenant to configure settings. During first run, choose to use Microsoft Azure Active Directory. You will need to provide credentials that are capable of joining the Azure AD tenant of your choice. After you successfully Azure AD join, the appropriate people will be granted admin rights on the device.

By default, all global administrators will be given admin rights on an Azure AD joined Surface Hub. With Azure AD Premium or Enterprise Mobility Suite (EMS), you can add additional administrators:

If your organization is using AD or Azure AD, we recommend you either domain join or Azure AD join, primarily for security reasons. People will be able to authenticate and unlock Settings with their own credentials, and can be moved in or out of the security groups associated with your domain.

For Surface Hub v1 and Surface Hub 2S devices joined to Azure AD, Windows 10 Team 2020 Update lets you limit admin permissions to management of the Settings app on Surface Hub. This enables you to scope admin permissions for Surface Hub only and prevent potentially unwanted admin access an entire Azure AD domain. To learn more, see Configure non-Global Admin accounts on Surface Hub.

Windows registers your device to your work or school network, letting you access your resources using your personal account. After your device is registered, Windows then joins your device to the network, so you can use your work or school username and password to sign in and access restricted resources.

First off, I am entering in correct password. Ive tried it with fqdn and without. Wireless is connected prior to login. No other notebooks connecting to domain wireless have exhibited this problem. I have even tried just using the surfaces software keyboard. I even wiped it a did a clean windows 10 (1607) Pro 64 bit install.

Did searching on google for about an hour but nothing exactly like what im seeing could be located. I never tried to join this tablet to domain before because it had Windows 10 Home edition up until yesterday.

I did try logging on with FQDN domain.local\user. didnt work. Event logs on domain controller only show event ids 4634 - "logon type 3 - This event is generated when a session is destroyed" I could find no useful logs on the surface itself to indicate what is happening

Not that it makes a difference, but unless you're using group policy or need to log into a domain account to access a mail profile to a local Exchange server, do you really need to join the domain? I tend to never join Surfaces or even regular notebooks to the domain unless absolutely necessary. If the user needs to access resources, I create a login on a terminal server which they can access via VPN and RDP when out of the building.

I had a Surface 3 that I was able to join to the domain without incident and login with domain accounts. Make sure your wireless VLAN has internal network rights. We have 3 wireless networks (1 is internal, 1 is internet only, and 1 is for facilities devices which have to have a static IP).

Another thing to look into: check your DNS on the server. At another office, I had a bad DNS entry that was preventing my new Server 2012 from staying connected to the domain. In that case, I could join the server to the domain, but I couldn't login to the server with any domain account.

When you login locally on the surface, check to see if the domain network is the type of network or if it is thinking it is on public. If it thinks it is on public, most likely the DNS server has a bad entry. Windows 10 devices cannot connect unless they are using the automatically detect connection type. If you try to force the connection to be one thing, the automatic detection will overrule.

Lymphocyte activation gene-3 (LAG-3; CD223), a structural homolog of CD4, binds to MHC class II molecules. Recent research indicated that signaling mediated by LAG-3 inhibits T cell proliferation, and LAG-3 serves as a key surface molecule for the function of regulatory T cells. Previous reports demonstrated that the majority of LAG-3 is retained in the intracellular compartments and is rapidly translocated to the cell surface upon stimulation. However, the mechanism by which LAG-3 translocates to the cell surface was unclear. In this study, we examined the trafficking of human LAG-3 under unstimulated as well as stimulated conditions of T cells. Under the unstimulated condition, the majority of LAG-3 did not reach the cell surface, but rather degraded within the lysosomal compartments. After stimulation, the majority of LAG-3 translocated to the cell surface without degradation in the lysosomal compartments. Results indicated that the cytoplasmic domain without Glu-Pro repetitive sequence is critical for the translocation of LAG-3 from lysosomal compartments to the cell surface. Moreover, protein kinase C signaling leads to the translocation of LAG-3 to the cell surface. However, two potential serine phosphorylation sites from the LAG-3 cytoplasmic domain are not involved in the translocation of LAG-3. These results clearly indicate that LAG-3 trafficking from lysosomal compartments to the cell surface is dependent on the cytoplasmic domain through protein kinase C signaling in activated T cells.

If the same TS works for all the other images, then i can' think there should be any issue on Surface devices. Is the surface getting correct IP address. Try to browse to a different OU and see if it joins. Check the domain account, password may needs to be updated.

Using AD Domain Controller, you can centrally manage domain-joined Windows 11 PCs. You can create, configure and apply group policies to push various user and computer settings to a domain-joined Windows 11 computers.

The domain join process of Windows 11 is simple. To join a Windows 11 computer to AD domain, you need to log in to the machine as local administrator. You must use domain administrator credentials while joining the machine to the domain.

In this step, ensure your computer name is correct. You may change your computer name if required. Select Domain and enter the domain name to which your Windows 11 computer should join. Click OK.

To join your Windows 11 computer to domain, you must enter the credentials to add the machine to domain. Enter the username in the format domain\username and specify the password. Click OK.

If the supplied credentials are correct, the Windows 11 computer will be added to AD domain. Welcome to the domainname domain confirms that Windows 11 computer has been successfully joined to the domain. Click OK.

Hii have a situation and i think its a strange one.some WIN10 clients joined to a domain controller win2016.the problem is that even if the controller is SHUTDOWN(Unreachble), clients still Authenticate normally!!Is it Normal !!!

Bacterial surface display is widely used to screen peptide libraries for e.g. epitope mapping and selection of high affinity binders [1]. As differences in display efficiency among different clones could cause unwanted biases during the selection process, knowledge of the capabilities, as well as the limitations of the particular display scaffold used, is considered to be of importance [2].

One such scaffold is the OmpA protein in Escherichia coli. OmpA is an integral outer membrane protein (OMP) embedded in the bacterial outer membrane (OM) as a β-barrel. It contains four surface exposed loops in which peptides can be inserted that subsequently are displayed on the cell surface [3]. Several reports exist in which the OmpA protein has been used as a bacterial surface display system, for applications such as peptide library screening [4], [5] use in a novel selection strategy [6], use as live vaccines [7] or to sequestrate cadmium for bioremediation [8].

Our goal was to display an epitope on the bacterial cell surface that could be recognized by commercially available antibodies and used as a handle in biophysical force experiments (to be published elsewhere). OmpA was chosen because it is very abundant (typically about 105 copies/cell (Koebnik et al. 2000)) and widely studied [12], [13]. For our biophysical application, adverse effects of peptide-insertion on protein levels or OM insertion were unwanted. Because epitope-sized insertions in loop 2 or 4 of OmpA have been shown to be tolerated without negative effects [3], this served as an additional reason to choose OmpA. Thus, we have inserted the epitope tags 3xFLAG and 2xmyc into loop 2 and 3 of the transmembrane domain of OmpA (here also referred to as OmpA-177), and studied their stability and outer membrane incorporation in vivo. As the cell wall anchoring by the periplasmic domain was unwanted in these experiments, the TM domain of OmpA was initially used instead of the full-length protein. 2ff7e9595c