Trpc7 Antibodies

Short transient receptor potential channel 7 (Trpc7)

Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors.

Activated by diacylglycerol (DAG). May also be activated by intracellular calcium store depletion.

Gene Information

Mouse
Gene Name:	Trpc7
Uniprot:	Q9WVC5
Entrez:	26946

Family

Belongs to:
transient receptor (TC 1.A.4) family

Alternative Names

hTRP7; KNP3; likley ortholog of mouse transient receptor potential cation channel, subfamilyC, member 7; putative capacitative calcium channel; short transient receptor potential channel 7; transient receptor potential cation channel, subfamily C, member 7; transient receptor potential-related channel 7, a novel putative Ca2+ channelprotein10TRPM2; Transient receptor protein 7; TRP7; TRP-7; TrpC7

Molecular Weight

Mass (kDA):
99.475 kDA

Genomic Context

Mouse
Location:	13|13 B1
Sequence:	13;

Diseases

• Cardiac Hypertrophy
• Hypertrophy
• Hypertensive Disease
• Columnar Cell Hyperplasia Of The Breast
• Heart Failure
• Pathologic Vasoconstriction
• Melanoma
• Hypoxia
• Lung Diseases
• Infarction
• Chronic Obstructive Airway Disease
• Myocardial Infarction
• Pulmonary Hypertension

• Bipolar Disorder
• Neuroblastoma
• Beckwith-wiedemann Syndrome
• Polycystic Kidney Diseases
• Kidney Diseases
• Lung Diseases, Obstructive
• Segmental Glomerulosclerosis

Pathways

• Secretion
• Store-operated Calcium Entry
• Localization
• Reflex
• Vasoconstriction
• Phototransduction
• Cell Growth
• Transport
• Gene Silencing
• Platelet Activation
• Neurogenesis
• Oxidative Phosphorylation
• Keratinocyte Differentiation

• Membrane Depolarization
• Cell Differentiation
• Cell Proliferation
• Lactation
• Parturition
• Insulin Secretion
• Blood Circulation

PTMs

• Phosphorylation

• Dephosphorylation

• Acylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/Trpc7

Best Uses Of The TRPC7 Marker

The TRPC7 mark is a gene that is expressed within the brain, liver, kidney. The TRPC7 genes is found in more 100 different human tissues. There are two forms of the gene: TRPC7+ and TRPC7-. It is expressed in cells by the positive form and is found in the nuclei in all mammalian tissues.

TRPC7+/+

A human TRPC7 gene has been identified and characterized. This gene regulates the protein's levels in the blood. The following are the best uses of TRPC7:

The cytosolic domain of the TRPC7 gene contains a cation current channel. This channel plays an important part in calcium influx for immunocytes. The blood cells and peripheral blood contain high levels of the human protein TRPC7. It is believed that the protein regulates the automaticity of mESC–CMs. This gene has many possible uses in biology and medicine. This marker will help researchers determine the most useful applications for the gene.

An agonist activates TRPC7 in a greater degree than thapsigargin. The agonist activates the channel by increasing the Ca2+ entry while thapsigargin ejects intracellular Ca2+ stores. Thapsigargin or agonist treatments can cause activation. Activation can be facilitated by an increase of Ca2+ entry. Anger stimulation increases the signaling to TRPC7.

As a possible treatment for bradycardia biological pacemakers, derived from pluripotent and stem cells, are currently being investigated. However, one of the major barriers is the development of tachyarrhythmia by derived cardiomyocytes. Understanding the mechanisms that govern the spontaneous actions potential of ESCCMs might help to solve this problem. It is important to remember that the TRPC7 marker has been widely used in many studies including those on ESC–CMs.

One of the most common ways to activate TRPC7 is via the release of a molecule called Peptidecyclin. This protein regulates activity of NCX molecules. TRPC7 can positively regulate NCX's activity if it is expressed in cells. TRPC7's positive effect on NCX is very beneficial. These results also support TRPC7's importance in neurodegeneration. It has many other potential uses in biology and medicine.

The TRPC7 gene can be used to study tumor growth. Transfection of the TRPC7 genes in mice causes a decrease in tumor volume but does not completely eradicate tumor formation. SASP, which is a cellular senescence proteins, is elevated in mice that are deficient. Transfected cells also are susceptible to UVB. Further, studies have shown TRPC7 is essential for activating certain cellular processes.

TRPC7 can also monitor UVB radiation. These channels are important in regulating UVB irradiation. These channels are important in regulating UVB radiation. Cells that lack them may become susceptible to heart failure. Therefore, understanding how TRPC7 plays a role in heart failure is critical. This marker is beneficial in many areas of cardiovascular health. For more information, contact your doctor today.

In the previous study of skin samples, we used skin from TRPC7-transfected mice with siRNATK. We then incubated the cells with 10 mM Gd3+. To detect TRPC presence in skin samples, we used antibodies against Ki-67 and P16INK4A. We found that TRPC7 expression is higher in transfected skin cells than in controls.

TRPC7+/-

The TRPC7 protein is an essential component of the calcium-binding channel ATPase. The protein is activated in two ways, either by a store-operated or receptor-operated mechanism. The discovery of TRPC7 rearranged the conflicting findings of previous studies. The findings showed that TRPC7 can be operated in a shop-operated mode. This mechanism may account for the small store-operated Ca2+ entry in TRPC3-expressing HEK-293 cells.

TRPC7 can be found in peripheral blood, as well as in various blood cells. It is predicted to play a role in nucleotide metabolism activity. The MutT motif located at its C-terminus is essential for the protein's role in nucleotide metabolism activity. Although other nucleotides do not induce a response from TRPC7, beta-NAD induced an immediate response.

TRPC7 is found in tumors and can increase skin sensitivity to UVB, which accelerates the skin's aging process. TRPC7 may be activated by UVB, contrary to evidence. TRPC7 deficient mice showed reduced UVB-induced tumors. TRPC7 knockout mice had less epidermal thickening, and no UVB-induced cancers.

The TRPC7 protein is produced by transient transfection of HEK-293 cells. This transfection was carried out using wild-type TRPC7 from humans or a mutant with a proline in position 111. Qiagen sells specific oligonucleotides to generate this mutation. After the mutation has been introduced to the cell line the DNA is sequenced in order to confirm its existence.

The TRPC7 marker is a protein that plays a crucial role in UVB irradiation. The gene encodes an enzyme that helps absorb UVB radiation. TRPC7 inhibitions are useful for UVB research. It is also useful when researching cancer, particularly in the context tumor irradiation. These are its best uses.

We observed similar constitutive Ba2+ influx in TRPC3 compared to TRPC7 in HeK-293 cells. In contrast, the TRPC3 or TRPC7-expressing cells displayed significant constitutive Ba2+ entry in the absence of Ca2+. TRPC3 & TRPC7 were also free from passive leakage. This makes them useful in many other studies.

TRPC7-/-

The TRPC7 marker has been identified as a molecular target for neurodegenerative diseases. Its C terminal MutT motif is believed to participate in nucleotidehydralase activity. TRPC7 was not responsive to other nucleotides, but ADP ribose elicited an immediate response. Beta-NAD however elicited a delayed response. In addition, TRPC7 immunostaining was detected in a variety of cell types, including human ES cells and pancreatic cancer cells.

The TRPC7 signal was induced in non-small-cell lung cancer cells using an adenovirus in a study of the role of TRPC7 in the progression of tumors. This study involved the examination of 100 nonsmall-cell lung-cancer cells from Liouying in Taiwan. Before being allowed to participate, all participants were informed. Each participant was subjected immunohistochemistry to confirm the presence and amount of TRPC7 proteins.

TRPC7 regulates LCR frequency, amplitude, and kinetics. It also regulates DDR & INCX. TRPC7 therefore has a positive impact on both. DD is a relay race. The HCN channel starts the race. Next, the T-type Ca2+ channels comes next. NCX comes last. If TRPC7 is mutated, it will negatively affect the function of a cell.

Two mechanisms activate TRPC7 protein channel: store-operated mod and receptor-operated mod. This study provides new information regarding TRPC7 function, and it also reconciles contradictory findings from other laboratories. TRPC7 plays a role in the regulation of gene expression, as well as its ability to influence cell processes. Researchers will be able to identify the mechanisms that activate a store-operated channel using this information.

Professor Yasuo Miori, Kyoto University, obtained a mouse TRPC7-cDNA sequence. The sequence was ligated into the pcDNA3.1(+) vector. To confirm the presence of the mutated DNA, it was sequenced. This was how the cloned it. Then the cDNA fragments were subjected to site-directed mutagenesis.

This gene has many potential uses. One of these potential uses is in aging. The TRPC gene is involved in tumor progression. TRPC7 activation stimulates activity of many genes involved with skin aging. Activated TRPC7 causes a shift in the ratio of proliferation and apoptosis. It also plays a role in cellular senescence. To identify the role of TRPC7 in aging, the TRPC gene expression in skin cells is detected by a TaqMan Gene Expression Assay kit from Thermo Fisher Scientific.

Another study found that skin samples from mice that lack TRPC7 showed lower levels of COX-2 protein. These results are consistent in previous studies showing that COX-2 protein expression is lower in TRPC7 mice. This demonstrates that TRPC7 is involved in the aging process of damaged tissues. It has been implicated in cancer research but the exact mechanisms are still unknown. The TRPC7 gene is essential in aging, and detecting it early can help prevent cancer and other skin diseases.