Recombinant Human Prokineticin-1 Protein (PROK1), Active

Name: Recombinant Human Prokineticin-1 Protein (PROK1), Active
Brand: Beta LifeScience
SKU: BLC-05971P
Availability: InStock

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Product Overview

Description	Recombinant Human Prokineticin-1 Protein (PROK1), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 98% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using bovine EJG cells is less than 2.0 μg/ml, corresponding to a specific activity of >500 IU/mg.
Uniprotkb	P58294
Target Symbol	PROK1
Synonyms	Black mamba toxin related protein; EG VEGF; EG-VEGF; EGVEGF; Endocrine-gland-derived vascular endothelial growth factor; Mambakine; PK1; PRK1; PROK1; PROK1_HUMAN; Prokineticin 1; Prokineticin-1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	AVITGACERD VQCGAGTCCA ISLWLRGLRM CTPLGREGEE CHPGSHKVPF FRKRKHHTCP CLPNLLCSRF PDGRYRCSMD LKNINF
Expression Range	20-105aa
Protein Length	Full Length of Mature Protein
Mol. Weight	9.7 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered PBS, pH 7.4, 0.02 Tween-20
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	Potently contracts gastrointestinal (GI) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types. Induces proliferation and differentiation, but not migration, of enteric neural crest cells. Directly influences neuroblastoma progression by promoting the proliferation and migration of neuroblastoma cells. Positively regulates PTGS2 expression and prostaglandin synthesis. May play a role in placentation. May play a role in normal and pathological testis angiogenesis.
Subcellular Location	Secreted.
Protein Families	AVIT (prokineticin) family
Database References	HGNC: 18454 OMIM: 606233 KEGG: hsa:84432 STRING: 9606.ENSP00000271331 UniGene: PMID: 29405963 Elevated PROK1 in the first pregnancy trimester is a more effective marker than PAPP-A in the prediction of pre-eclampsia and fetal growth restriction. PMID: 28675948 The VEGF/sVEGF-R1 ratio in follicular fluid on the day of oocyte retrieval in women undergoing IVF procedure, regardless of the type of stimulation protocol, might predict the risk of developing ovarian hyperstimulation syndrome (OHSS). To the best of our knowledge this is the first paper in the literature to show interplay among VEGF, EG-VEGF and sVEGF-R1 and the correlation between their concentration and OHSS risk. PMID: 28820403 These findings demonstrate a novel function of primary cilia in controlling EG-VEGF-regulated trophoblast invasion and reveal the underlying molecular mechanism. PMID: 27736039 miR-346 and miR-582-3p regulate EG-VEGF-induced trophoblast invasion through repressing MMP 2 and MMP 9, and may become novel diagnostic biomarkers or therapeutic targets for EG-VEGF-related obstetric disorders. (c) 2016 BioFactors, 43(2):210-219, 2017. PMID: 27619846 Each follicular fluid (FF) was individually aspirated and FF/serum EG-VEGF, inhibin-a, and FF IGF-1 levels were evaluated. The pregnant group was characterized by increased numbers of WVFs (p = 0.044), a WVE (p = 0.022), and increased levels of FF IGF-1 (p = 0.001) and serum EG-VEGF (p = 0.03). PMID: 27484063 Results show the biological effects of PROK1-V67I on cell functions are similar to those of wild type, and the common variant of V67I may act as a modifier in the PROK1-PROKR system through down-regulation of PROK1 expression. PMID: 26828479 EG-VEGF and its receptor PKR1 might play a role in the pathogenesis of adrenocortical tumors and could serve as prognostic markers for this rare malignant disease. PMID: 26475302 The prognosis was poorer in colorectal cancers that expressed both PROK1 and VEGF relative to the cases that expressed only 1 protein, and the expression of both proteins was found to be an independent prognostic factor. PMID: 26318037 PROK1 levels in follicular fluid and fertilization culture media could constitute new predictive noninvasive markers of successful embryo implantation in conventional in vitro fertilization-embryo transfer PMID: 26401590 Simultaneous targeting of both angiogenic growth factors (VEGF/PROK1) may prove more useful in colorectal cancer PMID: 25788276 High Prokineticin 1 protein expression is associated with sporadic colorectal cancer. PMID: 25331005 Expression of PROK1 and PROKR1 was significantly higher in mid-gestation ovaries (17-20 wk) than at earlier gestations (8-11 and 14-16 wk). PMID: 26192875 More importantly this paper argues for EG-VEGF clinical relevance as a potential biomarker of the onset of pregnancy pathologies and discusses its potential usefulness for future therapeutic directions. PMID: 24955357 EG-VEGF and VEGFA systems shared several canonical signaling pathways that may contribute to gene-gene interactions, including the Akt, IL-8, EGFR, MAPK, SRC, VHL, HIF-1A and STAT3. PMID: 24671265 Study corroborates the clinical relevance of the EG-VEGF system in human early pregnancy, and provides evidence for the gene-gene interactions of EG-VEGF and PROKR variants. PMID: 25064403 An increased mRNA expression of PROK1 and LIF could be one of the several abnormalities characterizing the endometrium in women recurrent pregnancy loss. PMID: 25128195 Defective placental maturation is associated with an imbalance of expression of basic fibroblast growth factor (FGF) and PK1. PMID: 23891065 preliminary data suggest a high potential of prokineticin 1 in the success of implantation and pregnancy PMID: 23972922 number of blood vessels in PROK1-positive primary gastrointestinal lesions was higher than that in PROK1-negative primary lesions. CONCLUSION: PROK1 expression might be related to the extent of malignancy in gastrointestinal cancer PMID: 24324064 EG-VEGF as a new placental growth factor acting during the first trimester of pregnancy, established its mechanism of action, and provide evidence for its deregulation in FGR. PMID: 22941044 During the first trimester of pregnancy, hCG and EG-VEGF exhibit the same pattern of expression, suggesting that EG-VEGF is potentially regulated by hCG. PMID: 22138749 Findings, together with the detection of sequence variants in PROKR1, PROK1 and PROKR2 genes associated to HSCR and, in some cases in combination with RET or GDNF mutations, provide evidence to consider them as susceptibility genes for HSCR. PMID: 21858136 Data show that decidualization was associated with increased expression of 428 genes including SCARA5 (181-fold), DKK1 (71-fold) and PROK1 (32-fold), and decreased expression of 230 genes including MMP-7 (35-fold) and SFRP4 (21-fold). PMID: 21858178 identified a novel signalling pathway whereby PROK1 can induce the expression of DKK1 in the human endometrium and first trimester decidua. PMID: 21546446 The data shows that much more PK1 in healthy pregnant women is produced than those suffering from preeclampsia. PMID: 21876489 Prok1 is significantly increased in ppapillary thyroid cancer, and its expression in PTC is related to BRAF mutation. PMID: 21385081 CTGF expression in early pregnancy decidua is regulated by PROK1, via activation of the Gq, PLC, cSrc, EGFR, MAPK/ERK kinase pathway and has a role in cell adhesion. PMID: 21098624 Data show that expression of PK1 and PKR1 was detected in primary MM cells and myeloma cell lines. PMID: 20795791 When endometrial stromal cells from both groups of women were differentiated to decidual phenotype, PROK1 mRNA was up-regulated and PR and HOXA10 mRNA were down-regulated to the same extent. PMID: 20400074 findings identify EG-VEGF as a novel paracrine regulator of trophoblast invasion. We speculate that a failure to correctly down-regulate placental expression of EG-VEGF at the end of the first trimester of pregnancy might lead to PE PMID: 19602057 Altered expression of PROK1 could be one of the several biochemical abnormalities characterizing eutopic endometrium in endometriosis. PMID: 19285664 Treatment of human decidua with a lentiviral miRNA to abolish endogenous PROK1 expression results in a significant reduction in IL-11 expression and secretion PMID: 19801577 EG-VEGF expression was significantly higher in ectopic endometriotic tissue when compared to eutopic samples in infertile women. PMID: 19135668 The role of EG-VEGF in the regulation of angiogenesis in endocrine glands. Review. PMID: 12858543 acting via either PK-R2 or PK-R1, prokineticin 1 may have angiogenic as well as nonangiogenic functions in the ovary PMID: 12915658 Expression of VEGFR-1 mRNA, but not EG-VEGF and the other three VEGF receptors studied, was elevated in preeclamptic vs. normal placentas. PMID: 15126581 Human EG-VEGF may play a role in angiogenesis both during the early endocrine development of testis and in the adult testis as well as in Leydig cell tumor growth. PMID: 15292351 EG-VEGF may only play a role in vascular function of peri-implantation endometrium, but is unlikely to be associated with the etiology of endometrial cancer development. PMID: 16210375 PK1 could be one of the causative factors of age-related macular degeneration (AMD); transgenic mice expressing human PK1 exhibit choroidal neovascularization in a model that may be useful for establishing treatments for the exudative form of AMD. PMID: 16263331 Inverse resgulation of mRNA expression by ovarian cells may suggest that in addition to its angiogenic effects, EG-VEGF/PK-1 may also play other roles in ovary. (review) PMID: 16320832 High EG-VEGF is associated with carcinogenesis and portal vein tumor thrombus formation in human hepatocellular carcinoma PMID: 17167981 Overexpressed Prk1 conferred Adriamycin resistance in a human embryo kidney cell line. PMID: 17178891 EG-VEGF/Prok-1 signaling has a role in neuroblastoma progression PMID: 17289879 Either EG-VEGF is not exclusive of endocrine organs, or the pancreas should be considered as a functional steroidogenic tissue. PMID: 17683928 PROK1 and PROKR1 expression is elevated in human decidua during early pregnancy PROK1-PROKR1 interaction regulates expression of a host of implantation-related genes. PMID: 18339712 EG-VEGF may enhance cell proliferation through the activation of MAPK pathway, although not through the Akt pathway. PMID: 18571163 High PK1 mRNA levels were observed only in cultured pancreatic stellate cells and microdissected islet cells, but not in cancer cells, and PK1 protein was localized mainly in islets and cancer-associated stromal cells. PMID: 19077468 hCG-mediated LIF expression in the endometrium is dependent on prior induction of PROK1. PMID: 19255255 EG-VEGF protects pancreatic cancer cells from apoptosis through upregulation of myeloid cell leukemia-1, an anti-apoptotic protein of the bcl-2 family. PMID: 19523441

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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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