Recombinant Human Serine/Threonine-Protein Phosphatase 5 (PPP5C) Protein (His&Myc)

Name: Recombinant Human Serine/Threonine-Protein Phosphatase 5 (PPP5C) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00810P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Serine/Threonine-Protein Phosphatase 5 (PPP5C) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P53041
Target Symbol	PPP5C
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AMAEGERTECAEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM
Expression Range	2-499aa
Protein Length	Full Length of Mature Protein
Mol. Weight	64.2 kDa
Research Area	Epigenetics And Nuclear Signaling
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	Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2. Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90.
Subcellular Location	Nucleus. Cytoplasm. Cell membrane.
Protein Families	PPP phosphatase family, PP-5 (PP-T) subfamily
Database References	HGNC: 9322 OMIM: 600658 KEGG: hsa:5536 STRING: 9606.ENSP00000012443 UniGene: Hs.654604
Tissue Specificity	Ubiquitous.

Gene Functions References

This work offers insights of how cantharidin-like inhibitors interact with human PP5, potentially allowing the design of more specific and even less cytotoxic drugs for cancer treatments. PMID: 30280322
PP5 binds and dephosphorylates the elastic N2B-unique sequence (N2Bus) of titin in cardiomyocytes. PP5 is pathologically elevated and likely contributes to hypo-phosphorylation of N2Bus in failing human hearts. Furthermore, Hsp90-activated PP5 interacts with components of a sarcomeric, N2Bus-associated, mechanosensor complex, and blocks mitogen-activated protein-kinase signaling in this complex. PMID: 29343782
High PPP5C expression is associated with urinary bladder cancer. PMID: 28534961
PP5-dependent impairment of GRalpha function represents a novel mechanism driving GC insensitivity in ASM in severe asthma. PMID: 27501780
Our results showed 1) a critical role for PP5 in cytokine-induced resistance to GC-mediated eosinophil death, 2) supported the dependence of GCR phosphorylation on PP5 activity, and 3) revealed that PP5 is a target of the lipoxin A4-induced pathway countering cytokine-induced resistance to GCs in eosinophils. PMID: 27742828
the importance of PP5 in CRC cell growth PMID: 25322973
PPP5C could be essential for glioma cell growth. PMID: 25796168
Measles Virus Infection Inactivates Cellular Protein Phosphatase 5 with Consequent Suppression of Sp1 and c-Myc Activities. PMID: 26157124
We demonstrate for the first time that PPP5C is essential for growth of HCC cells, which suggests that inhibition of PPP5C by RNAi may be a potential therapeutic strategy for the treatment of hepatocellular carcinoma. PMID: 25326185
Data indicate that Cu-oxidized S100 calcium binding protein A4 (S100A4) interacted with S100 calcium binding protein A1 (S100A1) and prevented protein phosphatase 5 (PP5) activation. PMID: 25269953
These results demonstrate that Hsp70 recruits PP5 and activates its phosphatase activity which suggests dual roles for PP5 that might link chaperone systems with signaling pathways in cancer and development. PMID: 24327656
these results suggest that caveolin-1 is a novel physiological activator of PP5. PMID: 23352616
Chp-1 and melusin can interact with cochaperones PP5 and Sgt1 and with each other in an ATP-dependent manner PMID: 23184943
Suggest that Slim/KLHDC10 is an activator of ASK1, contributing to oxidative stress-induced cell death through the suppression of PP5. PMID: 23102700
proasthmatic cytokine-induced corticosteroid insensitivity in airway smooth muscle cells is due, in part, to PP5-mediated impairment of glucocorticoid receptor-Ser211 phosphorylation. PMID: 22592921
Findings are indicative of a regulatory role of PP5 in cardiac function. PMID: 20875921
S100A1 and permanently active S100P inhibited the apoptosis signal-regulating kinase 1 (ASK1) and PP5 interaction, resulting the inhibition of dephosphorylation of phospho-ASK1 by PP5 PMID: 22399290
genetic disruption of PP5 is associated with enhanced and prolonged phosphorylation of a single serine (Ser-345) on Chk1 PMID: 21921034
PP5 plays a crucial role in ATR-mediated repair of UV-induced DNA damage. PMID: 21144835
Specific binding of PP5 to activated Rac1 provides a direct mechanism by which PP5 can be stimulated and recruited to participate in Rac1-mediated signaling pathways. PMID: 19948726
PP5 suppresses a pathway regulating the expression of p21(waf1) PMID: 12519780
protein phosphatase 5 interacts with DNA-PKcs and dephosphorylates with surprising specificity at least two functional sites. PMID: 14734805
structure of Serine/threonine protein phosphatase-5(PP5c) provides a structural basis for explaining the exceptional catalytic proficiency of protein phosphatases. PMID: 15155720
PP5 is regulated by mTOR and activates apoptosis signal-regulating kinase 1 signaling PMID: 15218033
PP5 plays an important role in the survival of cells in a low oxygen environment by suppressing a hypoxia-induced ASK-1/MKK4/JNK signaling cascade that promotes an apoptotic response PMID: 15328343
Results describe the structure of the autoinhibited state of protein phosphatase 5, revealing mechanisms of tetratricopeptide repeat-mediated phosphatase inhibition and Hsp90- and arachidonic acid-induced stimulation of phosphatase activity. PMID: 15577939
PP5 plays a critical role in ATR-mediated checkpoint activation PMID: 16260606
We report the solution structure of a complex of the TPR domain of Ppp5 with the C-terminal pentapeptide of Hsp90.This may be important for the relief of autoinhibition in Ppp5 and for the mechanisms of TPR-mediated recognition of Hsp90 by other proteins. PMID: 16531226
PP5, casein kinase Iepsilon, and cryptochrome dynamically regulate the mammalian circadian clock PMID: 16790549
PP5 is a physiological regulator of Raf-1 signalling pathways. PMID: 16892053
Protein phosphatase 5 as a key dephosphorylation regulator of Raf-1 activation. PMID: 17084641
these studies indicate that elevated levels of PP5 protein occur in human breast cancer and suggest that PP5 over-expression may aid tumor progression. PMID: 18280813
domain amphiphilicity is of higher importance than amino acid sequence specificity in the determination of protein adsorption and interfacial activity. PMID: 18547097
PP5 plays an important role in the regulation of 53BP1 phosphorylation and activity in vivo PMID: 19176521
Estrogen inhibits glucocorticoid action via protein phosphatase 5 (PP5)-mediated glucocorticoid receptor dephosphorylation. PMID: 19586900

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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.

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