TRPC3 Antibodies

Short transient receptor potential channel 3 (TRPC3)

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

Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5- triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion.

Gene Information

Human
Gene Name:	TRPC3
Uniprot:	Q13507
Entrez:	7222

Family

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

Alternative Names

hTrp3; hTrp-3; short transient receptor potential channel 3; transient receptor potential cation channel, subfamily C, member 3; transient receptor potential channel 3; Transient receptor protein 3; TRP3; TRP-3; TrpC3

Molecular Weight

Mass (kDA):
96.009 kDA

Genomic Context

Human
Location:	4q27
Sequence:	4; NC_000004.12 (121874481..121952060, complement)

Tissue Specificity

Expressed predominantly in brain and at much lower levels in ovary, colon, small intestine, lung, prostate, placenta and testis.

Subcellular Localizations

Membrane; Multi-pass membrane protein.

Diseases

• Hypertensive Disease
• Hypertrophy
• Cardiac Hypertrophy
• Pathologic Vasoconstriction
• Malignant Neoplasms
• Nervousness
• Hypoxia
• Cardiovascular Diseases
• Heart Failure
• Pain
• Stenosis
• Neoplasms

• Atherosclerosis
• Columnar Cell Hyperplasia Of The Breast
• Diabetes Mellitus
• Pulmonary Hypertension
• Vascular Diseases
• Essential Hypertension
• Ataxia

Interacting Proteins

• ITPR3
• MX1
• ORAI1
• Plcg1
• Src

• Wnk4

Pathways

• Localization
• Vasoconstriction
• Cell Proliferation
• Pathogenesis
• Membrane Depolarization
• Rna Interference
• Secretion
• Store-operated Calcium Entry
• Cell Death
• Transport
• Synaptic Transmission
• Gene Silencing
• Angiogenesis

• Exocytosis
• Lymphocyte Activation
• Vasodilation
• Cell Growth
• Cell Adhesion
• Cell Migration
• Cell Differentiation

PTMs

• Phosphorylation
• Biotinylation
• Glycosylation
• Cleavage
• Reduction

• Dephosphorylation
• Myristoylation
• Nitration
• Methylation
• Oxidation

• Acylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/TRPC3

Best Uses Of The TRPC3 Marker

This article will focus on the TRPC3Marker. It is an analogue to DAG that activates TRPC6. You'll also learn how it inhibits apoptosis and activates HDPCs. Let's take a closer look! We'll also explain the best uses for this unique peptide. This article was created for those who are looking for a better way to use TRPC3 marker.

TRPC3Marker is an analogue to DAG that activates TRPC6

DAG is a phosphoinositide. It is the major regulator and controller of the TRPC3 Channel. It plays an important function in controlling cellular Ca2+. DAG is produced by phosphoinositide-specific phospholipase C and interacts with specific receptors within the ER membrane. DAG also activates TRPCs at the plasma membrane, which allow Ca2+ into cells from the extracellular media.

After transfection of macrophages using the DAG-em1 biosensor was completed, cells were stimulated by LPS and then labeled using the ER-Tracker TR. The colocalization of TRPC3 (and DAG) was significantly higher in stimulated cells when compared to controls. This was consistent with TRPC3's DAG-binding capability to activate TRPC6.

DAG can also stimulate TRPC3 activity in macrophages. It activates a Pyr10-sensitive Current that is inducible in macrophages. TRPC3 has also been shown to have DAG binding ability. The currents induced by OAG can be measured using Fluo-4 fluorescence.

DAG-sensitive channels are DAGresponsive channels found in the cortex. Some of them are heteromeric, and constitute DAG sensitive Ca2+ channels. These channels are also voltage-independent and insensitive to tyrosinekinase inhibitors. It is still unknown why DAG activates them in neurons.

Lipin-1 provides DAG to TRPC3 activation. Lipin-1 inhibition inhibits TLR4-mediated Ca2+ fluxes, fld mice. This suggests that lipin-1 may be an upstream target for the TRPC3 signaling pathway. In addition, it prevents LPS-induced systemic inflammation in mice. The study has important implications for the development of drugs that target this pathway.

Complex rectification of I-V curves is sometimes a criterion to assess TRPC6 activity. However, it is not entirely clear how the complex rectification process is mediated by TRPC6. The cell type, as well as the degree of membrane contact, will affect the rectification type. Further, it is unknown what is responsible for the rectification.

TRPC3 is essential for LPS-induced signaling and upregulation of proinflammatory genes. A pharmacological approach to reduce inflammation is needed. However, it is important to understand the exact mechanism of LPS-mediated LPS-induced activation. These findings suggest that TRPC3 may be an important effector for LPS, if they are confirmed.

Several studies have reported that DAG-dependent activation of TRPC channels is independent of PKC activity. However, in the case of the DAG-dependent activation of TRPC6 channels, DAG-dependent activation is independent of PKC. In fact, DAG-dependent activation of TRPC channels may require a PKC-independent response.

TRPC3 activation promotes Ca2+ flux through ER. It is necessary for the production and release of inflammatory mediators by human macrophages. It regulates the secretion ER calcium+. To activate TRPC3, activated TLR4 produces DAG in the ER. TLR4-mediated activation can be inhibited by inactivating TRPC6.

It activates HDPCs

PTHrP, which is a natural product, acts as a potent activator for HDPCs. The compound has a high affinity in the cytoplasm. It has the ability to stimulate the growth and development of several cell types. The enzyme is naturally found in the body, including HDPCs. In vivo studies of HDPCs in a dish allow for the determination of their functional ability. This enzyme is naturally found throughout the gastrointestinal tract. It can cause many problems, including anemia as well as digestive disorders and diabetes.

One of the key characteristics of HDPCs is their ability differentiation into different cell types. 1a.25(OH),2D3 showed a positive effect on HDPCs through enhancing ALP activation in an animal model. The compound stimulated p38 and JNK in HDPCs, but it did not increase ALP activity. After incubation, the number of ALP positive cells increased after 1a,25(OH),2D3.

We used hDPCs grown in a culture dish to determine if PTHrP can activate HDPCs. We seeded hDPCs with 2 x105 cells in each well. After incubating the cells in 1a,25 (OH)2D3, they were dried in 70% ethanol for one hour. The cells were then stained with 40mmol/L Alizarin orange S at room temperatures for 15 min. The cells were then washed extensively with deionized water and photographed using an HP Officejet Pro L7580 scanner.

The inhibitors PTHrP inhibited ERK signaling and induced odontogenic differentiation in HDPCs. Western blotting confirmed the presence of PTHrP. Both inhibitors inhibit p38 and ERK activity. Further research is needed to determine which signaling pathway is involved in PTHrP-induced Odontogenic Differentiation of HDPCs. So what does PTHrP contribute to the odontogenic division of HDPCs.

Inflammation is a primary symptom of pulpitis, and excessive secretion of pro-inflammatory factors is a primary cause. Our study used LPS-treated, hDPCs to model pulpitis. LPS-treated LPS hDPCs produced elevated levels of proinflammatory factors. S14G humanin significantly decreased this condition. S14G-humanin and its inhibitors also inhibited NF-kB signaling. LPS and inflammation are both inflammatory processes.

It has also been reported 1a,25(OH),2D3 induces osteogenic differentiation of human dental pulp cells. Although the exact mechanisms of the effect are not yet known, this discovery is a significant step towards developing new therapeutic strategies for protecting the dental pulp from injury. MAPKs are thought responsible for the HDPC-mediated effects of 1a.25 (OH)2D3. It is therefore vital to understand the mechanisms through which this hormone promotes differentiation of odontoblasts.

It prevents apoptosis

Tanshinone IIA can inhibit cell proliferation and induce death. It is an anti-cancer drug from traditional Chinese medicine. Tanshinone IIA inhibits cell growth in EC-1 cells and ECa109 cells. It activates the mitochondrial caspase pathway and induces apoptosis. It also stops cell cycle progression by preventing the S and G2/M phases.

NO, also called nitric oxygen, is an organic molecule that inhibits the apoptosis of cells when present in sufficient levels. It also inhibits the apoptosis inducible by TNF/alpha/ActD and LPS. The antipoptotic mechanism involves gene transposition of protective proteins, including the hemeoxygenase cyclooxygenase.

ESE also blocks DNA fragmentation which is essential for apoptosis. ESE inhibits DNA fragmentation, which in turn inhibits cell proliferation and promotes expression p53. ESE can also reduce the percentage of cells that are in the S phase and induce cell cycle arrest in cancer-cells. ESE also detects superoxide and is essential for apoptosis.

Tanshinone IIA suppresses the Akt signaling pathway and p53-dependent apoptosis. The Western blot analysis was used to analyze the results. A b -actin probe was used for loading control. These findings are consistent and consistent with previous reports. If you are looking to find a powerful anti-cancer medication, look no further. We have the answer.

Survivin is part of the inhibitors of apoptosis group. Survivin, which is expressed in excess, protects cells from dying. Inhibition of survivin expression leads to increased apoptosis and higher chemosensitivity. Recent research on Caenorhabditiselegans as well as yeast has raised doubts regarding survivin's ability to act alone as an antiapoptotic. It is also believed that it is involved in cell division. Some early studies even showed defects in cell division.

Various diseases cause osteoclasts to undergo apoptosis. This causes the death or bone cells to form in osteoporosis. Other diseases include hyperparathyroidism and Paget's disease of bone. Osteoporotic bones have a lower rate of apoptotic than osteoarthritic bones. Moreover, p53 inhibits osteoporosis through blocking the ERK signaling pathway.

Different tissues express Survivin, with fetal tissues being more likely to have the protein. Its expression in human cancer cells is evidence that the survivin gene may be reactivated in carcinogenesis and malignant progress. Survivin may be a target for cancer therapy if it is increased in expression. The next step in the process is to identify survivin inhibitors that target this gene, and prevent its overexpression.