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CRYBA2 (NM_005209) Human Tagged ORF Clone Lentiviral Particle
CAT＃: RC216085L3V
- LentiORF®
-
Lenti ORF particles, CRYBA2 (Myc-DDK tagged) - Human crystallin, beta A2 (CRYBA2), transcript variant 1, 200ul, >10^7 TU/mL
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CNY 7,410.00
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Specifications
| Product Data | |
| Product Name | CRYBA2 (NM_005209) Human Tagged ORF Clone Lentiviral Particle |
| Synonyms | crystallin, beta A2; eye lens structural protein |
| Vector | pLenti-C-Myc-DDK-P2A-Puro |
| ACCN | NM_005209 |
| ORF Size | 591 bp |
| Sequence Data |
The ORF insert of this clone is exactly the same as(RC216085).
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| OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
| OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
| Reference Data | |
| RefSeq | NM_005209.1, NP_005200.1 |
| RefSeq Size | 709 bp |
| RefSeq ORF | 593 bp |
| Locus ID | 1412 |
| MW | 22.1 kDa |
| Gene Summary | Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also defined as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq, Jul 2008] |
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