Recombinant Human Piezo-Type Mechanosensitive Ion Channel Component 1 (PIEZO1) Protein (His&Myc)

Name: Recombinant Human Piezo-Type Mechanosensitive Ion Channel Component 1 (PIEZO1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00551P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Piezo-Type Mechanosensitive Ion Channel Component 1 (PIEZO1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q92508
Target Symbol	PIEZO1
Synonyms	(Membrane protein induced by beta-amyloid treatment)(Mib)(Protein FAM38A)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	RSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIIPFTAQAYEELSRQFDPQPLAMQFISQYSPEDIVTAQIEGSSGALWRISPPSRAQMKRELYNGTADITLRFTWNFQRDLAKGGTVEYANEKHMLALAPNSTARRQLASLLEGTSDQSVVIPNLFPKYIRAPNGPEANPVKQLQPNEEADYLGVRIQLRREQGAGATGFLEWWVIELQECRTDCNLLPMVIFSDKVSPPS
Expression Range	2198-2431aa
Protein Length	Partial
Mol. Weight	33.6 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology. Acts as sensor of phosphatidylserine (PS) flipping at the plasma membrane and governs morphogenesis of muscle cells. In myoblasts, flippase-mediated PS enrichment at the inner leaflet of plasma membrane triggers channel activation and Ca2+ influx followed by Rho GTPases signal transduction, leading to assembly of cortical actomyosin fibers and myotube formation.
Subcellular Location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane. Cell membrane; Multi-pass membrane protein. Cell projection, lamellipodium membrane. Cell membrane; Multi-pass membrane protein.
Protein Families	PIEZO (TC 1.A.75) family
Database References	HGNC: 28993 OMIM: 194380 KEGG: hsa:9780 STRING: 9606.ENSP00000301015 UniGene: Hs.377001
Associated Diseases	Dehydrated hereditary stomatocytosis 1 with or without pseudohyperkalemia and/or perinatal edema (DHS1); Lymphedema, hereditary, 3 (LMPH3)
Tissue Specificity	Expressed in numerous tissues. In normal brain, expressed exclusively in neurons, not in astrocytes. In Alzheimer disease brains, expressed in about half of the activated astrocytes located around classical senile plaques. In Parkinson disease substantia

Gene Functions References

Both vertebrate and invertebrate mechanosensitive PIEZO ion channels are polymodal, being voltage modulated, and can even be directly voltage gated following a preceding mechanical stimulus. PMID: 29545531
In the absence of extracellular matrix (ECM) proteins Piezo1 receptors are relatively insensitive to mechanical forces pushing the cellular membrane, whereas they can hardly be activated by mechanically pulling the membrane. Yet, if conjugated with Matrigel, a mix of ECM proteins, the receptors become sensitized. PMID: 28164706
present study was designed to evaluate in hereditary xerocytosis the functional link between mutated Piezo1 and KCNN4 PMID: 28619848
the knockdown of PIEZO1 significantly reduced the cell-viability of SW982 cells. PMID: 29757938
analysis of Piezo1 domains by using localized force on magnetic nanoparticles PMID: 27694883
Piezo1-shRNA could inhibit the invasion of the osteosarcoma cells. PMID: 29065102
Piezo1 plays an important role in the apoptosis of human osteoarthritis-derived chondrocytes through a caspase-12-dependent pathway. PMID: 28731145
MiR-103a might be a potential biomarker of myocardium infarction and could be used as an index for the diagnosis of AMI. It may be involved in the development of HBP and onset of AMI through regulating the Piezo1 expression. PMID: 27515482
The structural dynamics of the PIEZO1 channel activation and inactivation by coarse-grained modeling has been reported. PMID: 28905417
Additional alterations in mutant PIEZO1 channel kinetics, differences in response to osmotic stress, and altered membrane protein trafficking, predicting variant alleles that worsen or ameliorate erythrocyte hydration. PMID: 28716860
differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II. PMID: 27160899
data demonstrate that PIEZO1 is required for the regulation of NO formation, vascular tone, and blood pressure. PMID: 27797339
The Piezo1 convert a variety of mechanical stimuli into channel activation and subsequent inactivation, and what molecules and mechanisms modulate Piezo function. PMID: 27743844
Because Piezo1 senses both mechanical crowding and stretch, it may act as a homeostatic sensor to control epithelial cell numbers, triggering extrusion and apoptosis in crowded regions and cell division in sparse regions. PMID: 28199303
platelets and Meg-01 cells express the MS cation channel Piezo1, which may contribute to Ca(2+) entry and thrombus formation under arterial shear. PMID: 28416610
correlation between HPCHA and PIEZO1-gene mutated findings raise an important question as to whether any of the high phosphatidylcholine hemolytic anemia cases previously diagnosed in Japan may have in fact been the form of hemolytic anemia known as hereditary xerocytosis or dehydrated hereditary stomatocytosis with PIEZO1 gene mutation PMID: 26971963
Piezo1 responds to lateral membrane tension with exquisite sensitivity as compared to other mechanically activated channels and that resting tension can drive channel inactivation, thereby tuning overall mechanical sensitivity of Piezo1. PMID: 26646186
When the "split protein" is coexpressed, the parts associate to form a normal channel. PMID: 26963637
Mutations in PIEZO1 is associated with persistent lymphoedema caused by congenital lymphatic dysplasia. PMID: 26387913
Homozygous and compound heterozygous mutations in PIEZO1, result in an autosomal recessive form of generalized lymphatic dysplasia with a high incidence of non-immune hydrops fetalis and childhood onset of facial and four limb lymphoedema. PMID: 26333996
Mechanically activated Piezo1 plays an essential role in red blood cell volume homeostasis. PMID: 26001274
Piezo1 is amenable to chemical activation and thus there is a possibility that endogenous Piezo1 agonists might exist. PMID: 26001275
PIEZO1 is permeable to monovalent ions (K+, Na+, Cs+, Li+) and most divalent ions (Ba2+, Ca2+ and Mg2+), but not to Mn2+. PMID: 25955826
a possible role of Piezo1 in invasion and metastatic propagation. PMID: 25666479
Piezo1 channels are likely to function in normal RBCs and suggest a previously unidentified mechanotransductive pathway in ATP release. PMID: 26351678
study reports two unrelated families with hereditary xerocytosis where probands presented fetal hydrops for which the same heterozygous mutation in PIEZO1 was identified PMID: 23581886
PIEZO1 stretch sensitivity is modulated by polycystin-2. PMID: 24157948
family of mechanically activated channels that counts only two members in human, piezo1 and 2, has emerged recently. [review] PMID: 25037583
Protonation of the human PIEZO1 ion channel stabilizes inactivation. PMID: 25561736
the mechanically gated ion channel Piezo1 is an important determinant of mechanosensitive lineage choice in neural stem cells and may play similar roles in other multipotent stem cells. PMID: 25349416
Hereditary xerocytosis and familial haemolysis due to mutation in the PIEZO1 gene have been found in a Danish pedigree. PMID: 24314002
The R2488Q PIEZO1 mutation is an apparent major cause of familial hereditary xerocytosis. PMID: 25044010
Piezo1 is a novel TFF1 binding protein that is important for TFF1-mediated cell migration in gastric cancer cells. PMID: 24798994
gating and inactivation as a function of pressure PMID: 23972840
The gain-of-function PIEZO1 phenotype provides insight that helps to explain the increased permeability of cations in red blood cells of dehydrated hereditary stomatocytosis patients. PMID: 23695678
R2456H and R2488Q mutations in PIEZO1 alter mechanosensitive channel regulation, leading to increased cation transport in erythroid cells. PMID: 23479567
Xerocytosis is caused by mutations that alter the kinetics of the mechanosensitive channel PIEZO1. PMID: 23487776
Piezo1 responses in a patch emulate many of the responses seen in whole-cell mode, there are significant differences, presumably in the force transfer structures. PMID: 22790451
Loss of Fam38A expression may cause increased cell migration and metastasis in lung tumours. PMID: 22792288
Data show that the transmission of PIEZO1 mutations and cosegregation with the disease phenotype in all affected persons in both kindreds. PMID: 22529292
siRNA knockdown in epithelial cells inactivates endogenous beta1 integrin, reducing cell adhesion PMID: 20016066
The MIB index was strongly correlated with disease progression in papillary urothelial neoplasms in the urinary bladder. PMID: 18311491

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.