Protein TFG Antibodies

Protein TFG (TFG)

Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules (PubMed:23479643, PubMed:27813252). Required for secretory freight traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:21478858).

.

Gene Information

Human
Gene Name:	TFG
Uniprot:	Q92734
Entrez:	10342

Family

Belongs to:
No superfamily

Alternative Names

FLJ36137; protein TFG; TF6; TRK-fused gene protein; TRK-fused gene; TRKT3 oncogene; TRKT3

Molecular Weight

Mass (kDA):
43.448 kDA

Genomic Context

Human
Location:	3q12.2
Sequence:	3; NC_000003.12 (100709290..100748967)

Tissue Specificity

Ubiquitous.

Subcellular Localizations

Endoplasmic reticulum. Localizes to endoplasmic reticulum exit site (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:27813252, PubMed:21478858).

Diseases

• Neoplasms
• Malignant Neoplasms
• Myocardial Infarction
• Carcinoma
• Infarction
• Cell Transformation, Neoplastic
• Lymphoma
• Stemi
• Malignant Neoplasm Of Larynx
• Malignant Squamous Cell Neoplasm
• Laryngeal Neoplasm
• Chromosomal Translocation
• Cell Invasion

• Acute Myocardial Infarction
• Neoplasm Metastasis
• Anaplastic Lymphoma
• Thyroid Neoplasm
• Lymphatic Metastasis
• Laryngeal Squamous Cell Carcinoma
• Diffuse Large B-cell Lymphoma

Interacting Proteins

• ANXA11
• ARHGEF16
• BOLL
• CEP55
• CSTF2

• EWSR1
• HNRNPF
• MAGED1
• MAPK1IP1L
• PEF1

• PLSCR1
• PRR20D
• RBPMS
• SEC24A
• SPG21

• VPS37C

Pathways

• Secretion
• Cell Growth
• Oncogenesis
• Cell Proliferation
• Fibrinolysis
• Cell Death
• Pathogenesis
• Programmed Cell Death
• Cytokine Secretion
• Immune Response
• Localization
• Chromatin Remodeling
• Proteolysis

• Protein Secretion
• Platelet Aggregation
• Embryo Development
• Interphase
• Response To Stress
• Anaphylaxis
• Glycosylation

PTMs

• Phosphorylation
• Nitration

• Cleavage
• Glycosylation

Research Areas

• Signal Transduction

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/TFG

Best Uses of the TFG Marker

TFG is an important marker for molecular biological research. It is found at ER exit sites in human cell. The Human homolog is also found here. We will be discussing the best uses of this marker in this article. We will also discuss TFG ER exit points, the human homolog, GFP fusion to full length TFG and Sec16B. TFG is an integral part of molecular biological research.

Exit sites from the ER

TFG-1 binds to ER exits and forms a matrices. It is colocalized to SEC-13, both of which are located at the exit sites. TFG-1 as well as SEC-13 both localize to ER exits sites when used with the COPII equipment. These results suggest that TFG-1 is required to locate the exit site.

TFG was initially identified as part gene fusions with TrkA, NTRK1, but it is now also a fusion partner of ALK. After transfection of cells using TFG alone or with fusions with GFP, the cells were separated with SDS-PAGE. Next, a panERK1-ERK2 antibody was used to probe the cells.

Boster Bio is an antibody production company that was founded back in 1993. Boster Bio specializes exclusively in antibody manufacturing and recently began offering PCR related molecular biology products. The company offers a wide range of services, including technical assistance and support that is available 24 hours a days. It offers dedicated customer support to answer questions and help scientists maximize the results of their experiments. Boster Bio optimization guides are available for you to help optimize your experiments.

v!mAB@lSxsN9 corresponds to RY!iuuuuf-emoiu. Both of these proteins are related to ER exit sites, but the corresponding mRNA is RY!iuuuuuu$IUJ0f)emoiu. It has been shown, that v!mAB@lSxsN9 shares similar properties as the RY!iuu–muj0ff)emoiu.

Human homolog

The TFG mark is a protein containing an octameric rings structure. It can be found on human genome. The TFG is believed involved in cell growth, and development. This hypothesis comes with several caveats. First, the human homolog uses another marker to identify cell type. The mouse homolog, on the other hand, uses a TFG marker which is more sensitive to changes of protein concentration. Although the human homolog is of a different species than the mouse, it contains the same protein.

TFG serves two roles in cells. It forms a meshwork at ER/ERGIC and keeps cargo-containing vesicles for a temporary period. The vesicles become uncoated and fuse to other target compartments. The TFG marker is unique among PB1-domain proteins. To identify COPII transporters, the human homolog uses TFG markers.

TFG is involved in ER functions and is also a target of many acquired, oncogenic translocations. This includes cancer cells. These results suggest that TFG could be involved in fusion gene creation. TFG is also associated to apoptosis. Furthermore, TFG-deficient cells exhibit a reduced rate of autophagie flux compared to controls. These observations suggest that TFG function is essential for apoptosis, metabolic restrictions, and other functions.

TFG polymerization also was investigated in vitro using purified TFG isoforms that were supplemented and modified with a variety truncation mutants and salts. TFG octamers were analysed using dynamic light scattering. At least 10 measurements were taken for each salt concentration. The experiments were then repeated three times. The TFG marker is co-expressed with GFP in a 1:1,000 molar ratio.

GFP Fusion to Full-Length TFG

Boster Bio's laboratory uses genome editing to tag genes at levels similar to their native expression levels. For best results, fusion proteins should be expressed from a plasmid-based system. The length of the fluorescent tag, which fluorescent protein variant to use, as well as the location to add the tag to the fusion proteins are all options. The fusion protein is detected at its target site using immunofluorescence. Its properties can then be compared to its expected functions.

Functional fluorescent fusion proteins have been developed by Sheridan, Douglas L., and their collaborators. These fluorescent proteins are tagged with organelle-specific dyes in live cells. Aequorea victoria GFP has a C-terminus that sticks out and is considered a linker. Many FRET biosensors can be based on truncated fluorescent proteins.

One way to express FFP within cells is using a cytomegalovirus vector-containing vector (EGFP–C1). The investigator can also use the EGFP1 gene expression vector. Alternatively, investigators can create multiple color variants of GFP gene by using PCR primers that allow them to amplify multiple variants simultaneously.

FFPs with full-length TFG marker are useful tools to study protein function. The fusions have a wide range of applications, making them an excellent choice for biochemical studies. FFPs can be used by researchers to examine the behaviour of proteins in cells. FFPs should be considered when selecting the FFP-fusion to TFG markers. They are best for cell-based experiments that first assess the untagged protein.

One concern with GFP fusion to full-length TFM marker is the degree of labeling. GFP-Booster reduces the distance between the epitope (primary and secondary antibody) and the label (in a conventional combination). It is also important not to forget that it is completely free of TurboGFP, RFP and mCherry.

Before use, validation should be done on any sample type that is used to fuse GFP to full-length TFM markers. Boster Bio does not routinely validate tissue heterogenates as a sampling type. For linearity to be determined, you will need two aliquots each for spiked and unspilled samples. Linearity and expected recovery are between 80-120 percent. If you are using tissue homogenates, the GFP to full-length TFG markers should be detected in one aliquot.

mCherry fusion to Sec16B

ChromoTek developed mCherry-fusion to Sec17B, a novel expression system for mCherry. Sec16B, unlike TFG, has high photobleaching recovery and a poor recovery rate. Half-times range between 8.22 and 0.64 second. We will now describe the initial experiments performed to validate Sec16B by mCherry Fusion.

The fluorescent protein known as mCherry, which was first isolated in coral, was published in 2004. The protein was initially isolated from cnidarians, and has enhanced brightness, superior photostability, and rapid maturation. It is a well-known fluorescent protein, which can be used to monitor physiological processes and transgenic expression. Antibodies against mCherry-tagged protein can be used to detect it in its native and fusion forms.