Human Chromodomain Y-Linked 1 (CDY1) Protein
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Description
Human CDY1 Protein is a recombinant Human protein produced in a Prokaryotic expression system (E. coli).
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | CDY1 |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 61.9 kDa Observed MW (SDS-PAGE): 61.9 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Met1-Val250 Tag: N-terminal His tag and GST tag |
| Expression | Recombinant |
| Purity | > 90% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Liquid |
| Tested Applications | WB, SDS-PAGE |
| Buffer | PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q9Y6F8 |
| Background | Protein CDY1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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This gene encodes a protein containing a chromodomain and a histone acetyltransferase catalytic domain. Chromodomain proteins are components of heterochromatin-like complexes and can act as gene repressors. This protein is localized to the nucleus of late spermatids where histone hyperacetylation takes place. Histone hyperacetylation is thought to facilitate the transition in which protamines replace histones as the major DNA-packaging protein. The human chromosome Y has two identical copies of this gene within a palindromic region; this record represents the more centromeric copy. Chromosome Y also contains a pair of closely related genes in another more telomeric palindrome as well as several related pseudogenes. Two protein isoforms are encoded by transcript variants of this gene. Additional transcript variants have been described, but their full-length nature has not been determined.
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