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- Table of Contents
Facts about Ras-related protein Rab-1B.
RAB1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development that occur at specialized regions of the endoplasmic reticulum.
Mouse | |
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Gene Name: | Rab1b |
Uniprot: | Q9D1G1 |
Entrez: | 76308 |
Belongs to: |
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small GTPase superfamily |
RAB1B, member RAS oncogene family; ras-related protein Rab-1B; small GTP-binding protein
Mass (kDA):
22.187 kDA
Mouse | |
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Location: | 19|19 A |
Sequence: | 19; |
If you're interested in finding the most effective antibodies against the RAB1B Marker you've come the right place. Boster offers high-affinity primary antibodies that have been extensively cited in the research community for the last 25 years. Boster antibodies have been validated by Western Blotting, Immunohistochemistry, and ELISA. Find out more about the RAB1B Marker and how it can help in your experiments.
The PCR to determine Rap1b mRNA was done in two steps. First we employed the lambdaZAP II mouse cDNA library to isolate Rap1b mRNA. The mRNA was expressed in pET15b cells. Western blot analysis was used to confirm Rap1b's presence. The resultant cDNA was characterized by an open reading frame (552 bp) and a predicted protein size (21 kD). The results were also confirmed by in vitro translation.
Next, we employed miR-708 to increase Rap1B expression in the SKOV -I6iv cell lines. The Rap1B level of expression in the SKOV–I6iv cells ranged from two to three times that of the SKOV-3 parental cells. Additionally, Rap1B expression was negatively correlated with miR-708 expression. It was therefore essential to isolate Rap1B's cDNA using miR-708 as an appropriate target.
The PCR to detect Rap1b mRNA was also successful in detecting mRNA from various tissues. Rap1B is part of the Ras-proximity-1 familia and shares 95% sequence similarity with Rap1A. Both Rap1A and Rap1B were tested for their roles in ovarian cancer cells. Rap1B knockdown slowed cell migration and invasion in SKOV-I6iv as well as SKOV-3 cells. Rap1B knockdown also reduced FAs and signalling pathways that are mediated by FAs.
We also examined whether Rap1B is directly targeted by miR-708 via reporter plasmids. MiR-708 inhibited Rap1B expression in SKOV-3 cells by the reduction of luciferase's activities. The inhibition was reversed by anti-miR-708. We also confirmed Rap1B's significance in miR-708-mediated ovarian carcinoma cell migration and invasion.
The discovery of new effectsor proteins from Legionella pneumophila is crucial to finding out the nature of the virulence of these bacteria. These effector proteins are vital for Legionella species to develop intracellular life and pathogenicity. Each Legionella strain is capable of translocating up to 300 proteins into the host cell. They are referred to as effectors. A review of the genome of the pan-genus species revealed that there are 608 orthologous groups that comprise possible effectors. Due to significant functional redundancy it is challenging to discern the function of each effector. Methods for phenotypic screening which use single gene deletion mutants for phenotyping are not very effective.
Engineered mice have created a variety of varieties that provide a more thorough understanding of the host-effector relationship. In vivo, A/J mice infected with wild-type Legionella are currently the most prevalent. Additionally, studies of flagellin-deficient mice have revealed significant information about the effector and immune biology.
F-Box proteins that have two ankyrin repeats are the protein that acts as an effector from Legionella. These repeat domains are typically involved in protein-protein interactions. However this domain is not found in other eukaryotic F-box proteins. It is likely to play an important role in substrate recruiting. It is interesting to note that some deletion mutants of AnkB display significant intracellular bacterial growth impairments. Other experiments have revealed that deletions of this protein do not affect the growth of L. pneumophila. This suggests that this gene could be controlled by both strain and host cell types.
The potential for immunotherapies using the bacterial effector protein is very promising. They can stop serious diseases that are caused by immune dysfunction. Some of these effector proteins could even be used as vaccines. They are able to control the immune response of the host in an unrelated inflammation-related issue. These proteins are becoming increasingly popular and could alter your life. This is only the beginning of the exciting research!
Since these proteins are secreted by different protein secretion systems They play a significant role in the host-pathogen relationship. Therefore, it is essential to develop computational tools that predict the effects of proteins. The present tools are based on different machine learning techniques as well as heterogeneous features that are taken from structural information and protein sequences. The curated data sets and features used by each predictor are highly variable. These analyses provide a complete overview of T3SS effector proteins.
These proteins could be candidates for vaccine development because of their widespread conservation in host species. In the future, the protein Ags may be used to develop cross-serotype-reactive vaccines. The discovery of these proteins is expected to help researchers discover new ways to fight Legionnaires' disease. They could also be more effective in developing vaccines as a result of the discovery of novel Ags within the bacteria.
Boster Bio has the ideal product if you are seeking a primary antibody that can serve multiple uses. With more than 16000 antibodies to choose from, Boster has a diverse product portfolio, including antibodies validated for IHC, WB, FC, and ELISA. Boster also has a rabbit polyclonal antibody. This is available for free when you buy an initial antibody. Boster's antibody is available for mice and humans. They have been tested for biological activity.
Primary antibodies are immunoglobulins which only connect to a specific antigen. Their quality is typically determined by their affinity and specificity, with the first indicating the strength of the non-covalent bond. High specificity means that the antibodies aren't likely attach to unintended antigens, which makes them perfect to detect, measure, or cleaning an antigen. What are the advantages of using Boster Bio's high-affinity antibodies?
High-affinity antibody are designed to be used in a variety of applications. They are specific to a particular epitope of the antigen and are characterized by a minimal amount of lot-to lot variation. Boster Bio high-affinity primaries are made by mixing an antibody of your choice with an antibody that is monoclonal. This results in a highly specific antibody that can be used in the laboratory as well as on the target.
A site-directed mutagenesis method (SDM) was used to generate human IgG antibodies using the mouse IgG1–AVITag Vector. The mAb was then isolated by size-exclusion chromatography and biotinylated according to the directions. The scFab construct was also created by constructing paired light- and heavy chains that were separated by a linker of 72 residues. The final antibody is supplied in the form of a Liquid.
MBP-Linker-scFv was tested to determine its specificity for IFN-g. It it was found not to react to other antigens. A quantitative ELISA was performed to determine its affinity for IFN-g, and the resulting results were used to determine the affinity constant. These antibodies have a high affinity for IFN-g and are extremely specific.
MBP-Lk–scFv was also examined for its capability to bind standard IFN–g. A 20-kDa signal was detected after photographic and imaging fixation. This indicates that MBP–Lk–scFv has a high degree of specificity to the standard IFN–g antigen. A high-affinity antibody is an excellent tool for immunotherapy and cell research.
PMID: 23188820 by Mochizuki Y., et al. Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) is regulated by small GTPase Rab1B in the early secretory and autophagic pathways.