Recombinant Human Polycystin-2 (PKD2), partial

Code CSB-YP618787HU
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Source Yeast
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Code CSB-EP618787HU
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Source E.coli
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Code CSB-EP618787HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP618787HU
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Source Baculovirus
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Code CSB-MP618787HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PKD2
Uniprot No.
Alternative Names
APKD2; Autosomal dominant polycystic kidney disease type II; Autosomal dominant polycystic kidney disease type II protein; MGC138466; MGC138468; PC 2; PC2; PKD 2; PKD2; PKD2_HUMAN; PKD4; Polycystic kidney disease 2 (autosomal dominant); Polycystic kidney disease 2; Polycystic kidney disease 2 protein; Polycystin 2; Polycystin 2 transient receptor potential cation channel; Polycystin-2; Polycystin2; Polycystwin; R48321; Transient receptor potential cation channel subfamily P member 2; TRPP2
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel. Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum. Together with TRPV4, forms mechano- and thermosensitive channels in cilium. PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality.
Gene References into Functions
  1. PKD2 and PKD1 genes are mutated in autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2. PMID: 29899465
  2. this is the first report of autosomal dominant polycystic kidney disease complicated with aortic dissection caused by PKD2 mutation PMID: 29378535
  3. This noticeable hot spot regions hold higher frequency (50%) of pathogenic / likely pathogenic genetic variants constituting single nucleotide variants than large deletion and insertion that actually represents only 41.08% of coding sequence of PKD2. Statistically significant association for IVS3-22AA genotype was observed with PKD, while association of IVS4+62C>T was found insignificant. PMID: 29321346
  4. The novel pathogenic variant in c.637C> T in PKD2 is very interesting since they may represent Italian clusters. PMID: 27499327
  5. Upregulation of miR-106b-5p or downregulation of PKD2 expression can cause A549/DDP cells to become considerably more sensitive to cisplatin. The results showed that miR-106b-5p enhanced the sensitivity of A549/DDP cells to cisplatin by targeting the expression of PKD2. PMID: 28723865
  6. investigated the interaction network of human PKD2 in the cytosol and in Golgi-enriched subcellular protein fractions PMID: 27559607
  7. We aimed to revisit PKD2 prevalence, clinical presentation, mutation spectrum, and prognosis through the Genkyst cohort. Patients with PKD2-related dominant polycystic kidney disease typically present with mild disease PMID: 28356211
  8. Here, we review previous studies that connect the molecular properties of the domains of PC2 Cterm to distinct aspects of PC2 functions and regulation. PMID: 26857659
  9. TRPP2 mutations are associated with autosomal dominant polycystic kidney disease. PMID: 28154010
  10. Two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations. PMID: 28092368
  11. The structure of human PC2 in a closed conformation, solved by electron cryomicroscopy at 4.2-A resolution. PMID: 27991905
  12. SNPs in and near PKD2 showed significant evidence of association in individual samples of black adults (rs17013735, P-value=0.0009) and white adults (rs11938025; P-value=0.0005; rs2725270, P-value=0.003). PMID: 28100911
  13. Pancreatic cysts were more prevalent in patients with ADPKD with PKD2 mutation than in control subjects or patients with PKD1 mutation. PMID: 27046073
  14. This suggests that a precise dosage of PC2 is necessary for an adequate mechanosensitive alpha-actinin recruitment at junctions. PMID: 27575580
  15. TRPP2 may be used as a biomarker for evaluating patient prognosis and as a novel therapeutic target in human laryngeal squamous cell carcinoma. PMID: 27832627
  16. Novel PKD2 mutations in Chinese autosomal dominant polycystic kidney disease patients PMID: 26632257
  17. Two neutral missense PKD2 variants indentified in exon1 c.83G>C (p.R28P) and c.568G>A (p.A190T), which the former segregate with the mutation in affected relatives, and two new intronic and 3'UTR variants, c.1548+63C>T and c.*363delA. PMID: 26950445
  18. this study presents the cryo-EM structure of PKD2 in lipid bilayers at 3.0 A resolution, which establishes PKD2 as a homotetrameric ion channel and provides insight into potential mechanisms for its activation. PMID: 27768895
  19. PKD2 and RSK1 regulate integrin beta4 phosphorylation at threonine 1736 to stabilize keratinocyte cell adhesion and its hemidesmosomes. PMID: 26580203
  20. The coiled-coil domain in the PC2 C-terminal forms a stable helix bundle regardless of the presence of Ca(2+). PMID: 26574436
  21. Results show that some of the previously reported missense or synonymous mutations in PKD2 gene caused altered pre-mRNA splicing. PMID: 26692149
  22. PKD2 is a core factor in the formation of this multiprotein complex at the TGN that controls constitutive secretion of matrix metalloproteinase cargo. PMID: 26507660
  23. Human polycystin-2 transgene dose-dependently rescues autosomal-dominant polycystic kidney disease phenotypes in Pkd2 mutant mice PMID: 26435415
  24. FLNA anchors PC2 to the actin cytoskeleton through complex PC2-FLNA-actin to reduce degradation and increase stability, and possibly regulate PC2 function in a Ca-dependent manner. PMID: 25861040
  25. The data indicate that the cAMP pathway regulates PC2-mediated cation transport in the hST PMID: 26269590
  26. POlycystin-2 and its patogenic mutants inhibit PIEZO1 activity in renal tubular epithelial cells. PMID: 24157948
  27. There is only one Ca2+ binding site in the human PC2 C-terminus, located within its EF-hand domain; the Ca2+ binding affinity of the C-terminal trimer is greatly enhanced. PMID: 25716316
  28. TRPV4, TRPC1, and TRPP2 contribute to the ion permeation pore of the channels PMID: 25114176
  29. Data indicate that N-Glycosylation of transient receptor potential channel TRPP2 is required for adequate TRPP2 protein levels. PMID: 24719335
  30. The molecular analysis of an Iranian family showed that the PKD was due to a PKD2 mutation. PMID: 24011172
  31. Probable pathogenic mutations in the PKD2 gene were detected in patients with autosomal dominant polycystic kidney disease. PMID: 24694054
  32. analysis of EF hand motifs and how they affect the calcium dependence of polycystin-2 function PMID: 24558196
  33. CIB1a is a novel mediator of PKD2-driven carcinogenesis. PMID: 23503467
  34. The median age at onset of dialysis was significantly earlier in patients with PKD1 mutations (52 years) than in patients with PKD2 mutations (65.5 years) and those with an undetermined genotype (67 years) by survival analysis. PMID: 23985799
  35. Overexpression of polycystin (PC)1, but not a carboxy-terminal truncation mutant, increases ciliary PC2 expression levels in mouse kidney cells. PMID: 24009235
  36. In human subjects we found an association between ADPKD and IDCM and suggest that PKD mutations contribute to the development of heart failure PMID: 23376035
  37. C-terminal polycystin-2 phosphorylation influences the interaction with PIGEA14 PMID: 23838289
  38. early growth response 1, a transcription factor that binds to the NDRG1 promoter, was mediated in the NDRG1 expression regulation by PKD2. PMID: 23212942
  39. these data suggest that PKD2 and PKD3 coordinate to promote prostate cancer cell invasion through p65 NF-kappaB- and HDAC1-mediated expression and activation of uPA. PMID: 22797919
  40. PKD2 testing has a clinically significant detection rate in the pre-ESRF population. PMID: 22863349
  41. rs2728121 in PKD2 may contribute to the development of gout in Europeans. PMID: 22609445
  42. study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein PMID: 22802962
  43. PC2 and the Ca(2+)-dependent transient receptor potential channels in general are regulated by similar conformational changes in their cytoplasmic domains that are propagated to the channel pore. PMID: 22474326
  44. role in interferon-gamma-induced PD-L1 surface expression on human oral squamous carcinoma PMID: 22204817
  45. This study reports for the first time a patient with neonatal onset of polycystic kidney disease homozygous for an incomplete penetrant PKD2 missense variant due to uniparental disomy PMID: 22114106
  46. PKD2:c.2020 1_2020delAG is a mutation found in a Chinese family with autosomal dominant polycystic kidney disease. PMID: 21983717
  47. study reports the association of autosomal dominant polycystic kidney disease resulting from a mutation in PKD2 and left-right asymmetry defect PMID: 21719175
  48. High Protein kinase D2 is associated with glioblastoma growth and tumor formation. PMID: 21727210
  49. Findings clarify the structural properties of PC2t domain and strongly support a homotetramer assembly of PC2. PMID: 21622852
  50. In the molecular pathway to secretion, PKD2 is a key component of the PKC-mediated pathway to platelet activation and thrombus formation through its selective regulation of dense granule secretion. PMID: 21527521

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Involvement in disease
Polycystic kidney disease 2 (PKD2)
Subcellular Location
Cell projection, cilium membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Basolateral cell membrane. Cytoplasmic vesicle membrane. Golgi apparatus.
Protein Families
Polycystin family
Tissue Specificity
Detected in fetal and adult kidney. Detected at the thick ascending limb of the loop of Henle, at distal tubules, including the distal convoluted tubule and cortical collecting tubules, with weak staining of the collecting duct. Detected on placenta syncy
Database Links

HGNC: 9009

OMIM: 173910

KEGG: hsa:5311

STRING: 9606.ENSP00000237596

UniGene: Hs.181272

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