Recombinant Human Zinc Finger Protein Zic 2 (ZIC2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07752P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Zinc Finger Protein Zic 2 (ZIC2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-07752P
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.

Product Overview

Description Recombinant Human Zinc Finger Protein Zic 2 (ZIC2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb O95409
Target Symbol ZIC2
Synonyms Zinc finger protein of the cerebellum 2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His
Target Protein Sequence PHAAHVGSYSGPPFNSTRDFLFRSRGFGDSAPGGGQHGLFGPGAGGLHHAHSDAQGHLLFPGLPEQHGPHGSQNVLNGQMRLGLPGEVFGRSEQYRQVASPRTDPYSAAQLHNQYGPMNMNMGMNMAAAAAHHHHHHHHHPGAFFRYMRQQCIKQELICKWIDPEQLSNPKKSCNKTFSTMHELVTHVSVEHVGGPEQSNHVCFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFQCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVH
Expression Range 100-415aa
Protein Length Partial
Mol. Weight 41.6 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 Acts as a transcriptional activator or repressor. Plays important roles in the early stage of organogenesis of the CNS. Activates the transcription of the serotonin transporter SERT in uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-specific projections in primary visual targets. Its transcriptional activity is repressed by MDFIC. Involved in the formation of the ipsilateral retinal projection at the optic chiasm midline. Drives the expression of EPHB1 on ipsilaterally projecting growth cones. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter region from ventrotemporal retinal segments of retinal embryos.
Subcellular Location Nucleus. Cytoplasm.
Protein Families GLI C2H2-type zinc-finger protein family
Database References
Associated Diseases Holoprosencephaly 5 (HPE5)

Gene Functions References

  1. Results show that ZIC2 is highly expressed in osteosarcoma cells and tissues, and its overexpression promotes viability, invasion of osteosarcoma cells via SHIP2 suppression, and PI3K/AKT activation. PMID: 28857346
  2. the studies confirm the extent of ZIC2 allelic heterogeneity and that pathogenic variants of ZIC2 are associated with both classic and middle interhemispheric variant (MIHV) HPE which arise from defective ventral and dorsal forebrain patterning, respectively. PMID: 29442327
  3. miR-1271/Zic2/PAK4 axis plays an important role in hepatocellular carcinoma progression. PMID: 28577975
  4. Together SMAD3 and ZIC2 regulate FOXA2 transcription in cultured cells and Zic2 also controls the foxA2 expression during Xenopus development. These findings reveal a new mechanism of NODAL signal transduction in the mammalian node and provide the first molecular explanation of how ZIC2 loss-of-function precipitates Holoprosencephaly (HPE PMID: 27466203
  5. Data show that Zinc finger protein ZIC 2 (ZIC2) is indispensable in the regulation of pancreatic ductal adenocarcinoma (PDAC) cell apoptosis. PMID: 26318045
  6. ZIC2 acts upstream of OCT4 and recruits the nuclear remodeling factor complex to the OCT4 promoter, initiating OCT4 activation. ZIC2 levels positively correlated to the clinicopathological stages of HCC patients. PMID: 26426078
  7. Mutational screening for HPE genes revealed the occurrence of a frameshift mutation in the ZIC2 gene. PMID: 24677696
  8. ZIC2 and RASGRF1 are susceptibility genes, not only for common myopia, but also for high myopia. PMID: 24150758
  9. The c.1401_1406dup (p.Ala469_470dup) or alanine tract expansion to 17 residues) in the ZIC2 gene are likely to be medically significant for holoprosencephaly in a Brazilian cohort. PMID: 22847929
  10. A high level of sequence variation in the 3'UTR of ZIC2 may be associated with holoprosencephaly. PMID: 22859937
  11. ZIC2, a transcription factor related to the sonic hedgehog pathway, is a strong discriminant between MAL and LMP tumors: it may be a major determinant of outcome of EOTs. PMID: 22733541
  12. Mutations in ZIC2 is associated with holoprosencephaly. PMID: 22310223
  13. Brain malformations, including neuronal migration defects, predominated in individuals with ZIC2 mutations. PMID: 21940735
  14. role for ZIC2 as a transcriptional regulator of the beta-catenin.TCF4 complex. PMID: 21908606
  15. Our findings suggest that Zic2 is a positive modulator increasing Gli1 transcriptional and oncogenic activity by retaining Gli1 in the nucleus of cervical cancer cells. PMID: 21661123
  16. mutation of ZIC2 is a rare cause of, or contributor to, RES associated with HPE. PMID: 21638761
  17. the smallest 13q deletion associated to DWM allows further narrowing of the previously established critical region for this brain malformation to 13q32.2-32.3. Among the few genes of the deleted region, ZIC2 and ZIC5 seem the most plausible candidates. PMID: 20683983
  18. screened four known HPE genes in a Dutch cohort of 86 non-syndromic HPE index cases, including 53 family members. We detected 21 mutations (24.4%), 3 in SHH, 9 in ZIC2 and 9 in SIX3 PMID: 20531442
  19. Holoprosencephaly due to ZIC2 mutations is distinct from that due to mutations in other genes. PMID: 19955556
  20. ZIC2 expression was associated with the histopathologic types of oral squamous cell carcinoma PMID: 19784848
  21. Sample was too small to reach definitive conclusions, but the evidence is sufficiently intriguing to encourage further research. PMID: 11857562
  22. Holoprosencephaly in monosomy 13q may be related to ZIC2 gene loss of function. PMID: 11910512
  23. Zic2 is an evolutionarily conserved determinant of retinal ganglion cells that project ipsilaterally PMID: 13678579
  24. Four novel ZIC2 mutations found in a cohort of Holoprosencephaly patinets. PMID: 15221788
  25. The C-terminal alanine-tract of ZIC2 influences the strength of DNA binding and alters transcriptional activity in a promoter-specific manner PMID: 15590697
  26. Forms two different complexes with DNA-dependent protein kinase, poly(ADP-ribose) polymerase, and RNA helicase A; all the components interacted directly with Zic2 protein PMID: 17251188
  27. This transcription factor regulates the expression of EphB1 in RGCs and also suggest the existence of an additional EphB1-independent pathway controlled by Zic2 that contributes to retinal axon divergence at the midline. PMID: 18417618
  28. ZIC2, SPRY2, and GPC5 genes are candidate genes suspected to explain the malformations associated with cerebral anomalies in the hypothesis of a contiguous gene syndrome in 13q deletion syndrome PMID: 19022413
  29. Loss-of-function as the likely pathogenetic mechanism common to most, if not all, of ZIC2 mutations in holoprosencephaly. PMID: 19177455

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.

Recently viewed