Recombinant Human Cone-Rod Homeobox Protein (CRX) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-11241P
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CRX.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CRX.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CRX.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CRX.

Recombinant Human Cone-Rod Homeobox Protein (CRX) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-11241P
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Product Overview

Description Recombinant Human Cone-Rod Homeobox Protein (CRX) 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 O43186
Target Symbol CRX
Synonyms Cone rod homeobox; Cone rod homeobox protein; Cone rod homeobox-containing gene; cone-rod homeobox; Cone-rod homeobox protein; CORD 2; CRD; CRX; CRX_HUMAN; LCA 7; LCA7; Orthodenticle homeobox 3; OTX 3; OTX3
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence MMAYMNPGPHYSVNALALSGPSVDLMHQAVPYPSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGGQAKARPAKRKAGTSPRPSTDVCPDPLGISDSYSPPLPGPSGSPTTAVATVSIWSPASESPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYGSPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYGAYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
Expression Range 1-299aa
Protein Length Full Length
Mol. Weight 39.3 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 Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors.
Subcellular Location Nucleus.
Protein Families Paired homeobox family
Database References
Associated Diseases Leber congenital amaurosis 7 (LCA7); Cone-rod dystrophy 2 (CORD2); Retinitis pigmentosa (RP)
Tissue Specificity Retina.

Gene Functions References

  1. that two photoreceptor-specific transcription factors, NRL and CRX, are master regulators of this program and are required for tumor maintenance in this subgroup PMID: 29533784
  2. A novel CRX pathogenic variant has been identified in our patients. The novel pathogenic variant seems to have a different effect on the phenotype of cone-rod dystrophy. PMID: 30078014
  3. A sensitive and simple method of tumour cell assessment has been developed that can be used in the clinics to assess for potential extraocular dissemination after intravitreal injections to assure its performance. PMID: 29089355
  4. we revealed a novel frameshift mutation (NM_000554.4:c.538dupG:p.Val180fs) in exon 4 of the CRX gene in a Chinese family with Cone-rod dystrophy. This study broadens the known pathogenic mutation spectrum of the CRX gene and contributes to improved genetic counseling for Cone-rod dystrophy patients. PMID: 30095615
  5. analysis of a homozygous nonsense mutation in SAMD11 in five individuals diagnosed with adult-onset retinitis pigmentosa; SAMD11 interacts with CRX and is expressed in retina PMID: 27734943
  6. CRX mutations are associated with a variety of clinical phenotypes, including an adult-onset macular dystrophy that simulates benign concentric annular macular dystrophy with a bull's eye macular lesion and fairly well preserved visual acuity. PMID: 28945142
  7. data demonstrate the successful application of ZFN technology to generate CRX-GFP labeled hESC lines, which can be used to study and isolate photoreceptor precursors during hESC differentiation. PMID: 26608863
  8. Loss of OTX2 expression resulted in decreased expression of C-MYC and CRX, genes previously implicated in retinoblastoma tumorigenesis. Loss of OTX2 expression increased the phosphorylation of RB, a potential mechanism of modulating cell proliferation PMID: 26397460
  9. Mutations involving the CRX gene may demonstrate an autosomal dominant inheritance pattern for leber congenital amaurosis. PMID: 24093488
  10. Con rod homeobox protein mRNA is a novel marker for retinoblastoma at extraocular sites. PMID: 25928893
  11. Two de novo mutations in CRX were found in Chinese patients with Leber congenital amaurosis. The CRX mutation might create a dominantly inherited trait. PMID: 24001014
  12. Mutations in CRX demonstrate significant phenotypic heterogeneity both between and within pedigrees. A novel, adult-onset, macular dystrophy phenotype is characterized, further extending our knowledge of the etiology of dominant macular dystrophies. PMID: 25270190
  13. CRX could be useful in surgical neuropathology for the differential diagnosis of pineal region tumors, in particular to discriminate pineal tumors from glial tumors PMID: 24555912
  14. Data have identified a novel retinal SAM domain protein, Samd7, which could act as a transcriptional repressor involved in fine-tuning of Crx-regulated gene expression. PMID: 23565263
  15. the potential utility of CRX as a marker of pineal lineage in routine diagnostic neuropathology. PMID: 23235340
  16. In this study, three variations were detected in 3 of 130 families with CORD, including two novel mutations, c.239A>G (p.Glu80Gly) and c.362C>T (p.Ala121Val) PMID: 22960069
  17. These findings suggest that CRX is a useful marker to discriminate metastatic retinoblastoma from other, more common, malignant small round cell tumors of childhood PMID: 22790857
  18. Photosensitive photoreceptor cells can be generated by combinations of transcription factors. The combination of CRX and RX generate immature photoreceptors: and additional NEUROD promotes maturation. PMID: 22558175
  19. Data show no interaction of barrier-to-autointegration factor (BAF) with HIV-1 MA, cone-rod homeobox (Crx) or MAN1-C in absence of DNA. PMID: 21966431
  20. CRX has a role in retinal and pineal lineage tumors PMID: 19936203
  21. DNA-binding domain mutations in NR2E3 affect in vivo dimerization and interaction with CRX PMID: 19823680
  22. Two patients with Leber congenital amaurosis who carried heterozygously one of two novel frameshift mutations. PMID: 11748859
  23. The frameshift mutation in CRX gene in the patient with Leber congenital amaurosis did not cause impairment in vision PMID: 11910559
  24. results support the hypothesis that CRX mutations involved in human photoreceptor degeneration act by impairing CRX-mediated transcriptional regulation of the photoreceptor genes PMID: 11971869
  25. A novel frameshift mutation was detected in exon III of the CRX retinal homeobox gene. PMID: 12359607
  26. both Nrl and Crx are required for full transcriptional activity of the PDE6A gene PMID: 15001570
  27. A 615delC mutation in the CRX gene was identified and found to cosegregate with cone-rod dystrophy PMID: 15531334
  28. Nr2e3 is a dual-function transcriptional regulator that acts in concert with Crx to promote and maintain the function of rod photoreceptors. PMID: 15689355
  29. description of a 2-generation family with a novel mutation in CRX; the resulting phenotype is that of cone-rod dystrophy with variable age at onset and progression PMID: 17320181
  30. Transmission of the disease through three generations provides evidence that Lebers congenital amaurosis is transmitted as an autosomal dominant trait. PMID: 17347810
  31. authors identified a novel disease causing mutation, c.636delC, in the CRX gene, associated with autosomal dominant cone-rod dystrophy PMID: 18653602
  32. CRX expression in the inner nuclear layer of the retina. PMID: 19686387

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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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