Recombinant Mouse Prokineticin-2 (PROK2) Protein (His-B2M)

Beta LifeScience SKU/CAT #: BLC-06722P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Prokineticin-2 (PROK2) Protein (His-B2M)

Beta LifeScience SKU/CAT #: BLC-06722P
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Product Overview

Description Recombinant Mouse Prokineticin-2 (PROK2) Protein (His-B2M) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9QXU7
Target Symbol PROK2
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His-B2M
Target Protein Sequence AVITGACDKDSQCGGGMCCAVSIWVKSIRICTPMGQVGDSCHPLTRKSHVANGRQERRRAKRRKRKKEVPFWGRRMHHTCPCLPGLACLRTSFNRFICLARK
Expression Range 27-128aa
Protein Length Full Length of Mature Protein
Mol. Weight 25.5 kDa
Research Area Cancer
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 May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle.
Subcellular Location Secreted.
Protein Families AVIT (prokineticin) family
Database References
Tissue Specificity Expressed in the SCN and among a few other discrete brain areas, including the islands of Calleja, media l preoptic area of the hypothalamus and the shell of the nucleus accumbens. Highly expressed in testis. In the SCN, expression subjected to high ampli

Gene Functions References

  1. The study shows that PK2beta ligand, a splice variant of prokineticin 2, is able to modulate and drive signaling through prokineticin receptor 1. PMID: 30253862
  2. Prokineticin-2 is upregulated during neuronal injury, and it mediates a compensatory protective response against dopaminergic neuronal degeneration PMID: 27703142
  3. mammalian diurnality or nocturnality is likely determined by the differential signaling of prokineticin 2 from the intrinsically photosensitive retinal ganglion cells onto their retinorecipient brain targets. PMID: 27535380
  4. In mouse models, PK2 over-expression aggravated psoriasis while its knock-down inhibited pathological development. The results indicate that PK2 over-production perpetuates psoriatic symptoms by creating PK-2-IL-1 vicious loop. PK2 is a central player in psoriasis and a promising psoriasis-specific target. PMID: 27887936
  5. PROK2 plays a role in cerebral amyloidosis and that PROK2 antagonists may represent a new approach for ameliorating the defining pathology of AD. PMID: 26477583
  6. Data show that the prokineticins and their receptors PROK2, PKR1 and PKR2 contributes to altered sensitivity in diabetic neuropathy and its inhibition blocked both allodynia and inflammatory events underlying disease. PMID: 26730729
  7. These findings suggest that PROK2 plays a crucial role in neuropathic pain and might represent a novel target of treatment for this disease. PMID: 25685780
  8. Controlling the activation of the Bv8/prokineticin system reduces neuroinflammation and abolishes thermal and tactile hyperalgesia in neuropathic animals PMID: 24902717
  9. PK2 plays an important role in energy intake and expenditure. PMID: 22960406
  10. Data suggest that elevated prokineticin 2 levels, as a consequence of gastrointestinal tract inflammation, induce visceral pain via prokineticin receptors. PMID: 22050240
  11. Intracerebroventricular administration of PK2 affects regulation of food intake. PMID: 19933997
  12. Bv8 and EG-VEGF, along with other factors such as VEGF-A, may maintain the integrity and also regulate proliferation of the blood vessels in the testis PMID: 12604792
  13. Light inducibility of PK2 suggests that in addition to its role in clock-driven rhythms of locomotor behaviour, PK2 may also participate in the photic entrainment of circadian locomotor rhythms. PMID: 15762991
  14. findings define an essential role for G protein-coupled PK2 signaling in postnatal and adult olfactory bulb neurogenesis PMID: 15976302
  15. The depolarizing effect of Prok2 on neurons that express Prok2 receptor may represent a possible mechanism for the regulatory role of Prok2 in circadian rhythms. PMID: 16279936
  16. Attenuated circadian rhythms in mice lacking the prokineticin 2 gene. PMID: 17093083
  17. Prokineticin 2 as a common functional target gene for different bHLH transcriptional factors in mediating their respective functions. PMID: 17259180
  18. Homozygous loss-of-function PROK2 mutations cause both Kallmann syndrome and normosmic idiopathic hypogonadotropic hypogonadism PMID: 17959774
  19. identification of granulocyte colony-stimulating factor as a major positive regulator of Bv8 expression; anti-Bv8 antibodies reduced CD11b+Gr1+ cell mobilization elicited by granulocyte colony-stimulating factor PMID: 18064003
  20. verify a role for Bv8 in the mobilization and recruitment of myeloid cells and in the induction of tumor angiogenesis in the early stages of neoplastic progression PMID: 18268320
  21. Cardiomyocyte-PKR1 signaling upregulates its own ligand prokineticin-2 that acts as a paracrine factor, triggering epicardial-derived progenitor cell proliferation/differentiation. PMID: 18421008
  22. study indicates that PK2 signaling plays a critical role in the stress-related traits in mice, and establish a possible molecular link between circadian rhythms and mood regulation PMID: 18432189
  23. Bv8 was elevated in the synovium and bone marrow of CIA mice, suggesting that Bv8 plays an important role in the pathogenesis of arthritis. PMID: 19405944
  24. Data show that the inflammation-induced up-regulation of PK2 was significantly less in pkr1 null mice than in WT and pkr2 null mice, demonstrating a role of PKR1 in setting PK2 levels during inflammation. PMID: 19667192

FAQs

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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.

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

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