Recombinant Human CRYGD
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Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Host | E.Coli |
| Reactivity | Human |
| Assay Data | Centrifuge the vial before opening, reconstitute in sterile distilled water to a concentration of 0.1-1 mg/ml by gently pipetting 2-3 times, don't vortex. |
| Observed MW | 19 kDa |
| Expression | 1-174 |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Size 1 | 50μg |
| Size 2 | 200μg |
| Size 3 | 1mg |
| Form | Lyophilized powder |
| Tested Applications | Western Blot, ELISA |
| Buffer | Lyophilized from a 0.2 μm filtered solution in 10 mM Hepes, 500 mM NaCl with 5% trehalose, pH 7.4. |
| Availability | 3-4 weeks |
| Storage | The lyophilized protein is stable at -20 °C for up to 1 year. After reconstitution, the protein solution is stable at -20 to -80 °C for 3 months or 1 week at 2 to 8 °C under sterile conditions. For extended storage, it is recommended to further dilute in working aliquots, avoid repeated freeze/thaw cycle. |
| UniProt ID | P07320 |
| Alias | CACA, CCA3, CCP, CRGD_HUMAN, CRYG4, Crygd, Crystallin, gamma D, Crystallin, gamma-4, CTRCT4, Gamma crystallin D, Gamma D crystallin, Gamma-crystallin 4, Gamma-crystallin D, Gamma-D-crystallin, PCC |
| Background | Protein CRYGD |
| Status | RUO |
| Note | Tag : N-terminal His Tag or N-terminal His-IF2DI Tag, determined during production process |
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CRYGD Antibody is a Rabbit Polyclonal antibody against CRYGD. Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains 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 considered 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. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
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Gamma-Crystallin D (CRYGD) Antibody
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains 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 considered 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. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
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