Thermo Fisher Scientific a-B-Crystallin Polyclonal Antibody
Human a-B-Crystallin을 인식하는 Rabbit Polyclonal Antibody로, WB 및 IHC(P) 실험에 적합. Antigen affinity chromatography로 정제되어 높은 특이성과 재현성 제공. PBS buffer에 안정화되어 장기 보관 가능.
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Applications
| Application | Tested Dilution |
|---|---|
| Western Blot (WB) | 0.1–1 µg/mL |
| Immunohistochemistry (Paraffin) (IHC (P)) | 2–10 µg/mL |
Product Specifications
| 항목 | 내용 |
|---|---|
| Species Reactivity | Human |
| Host / Isotype | Rabbit / IgG |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | A synthetic peptide corresponding to the C-terminus of human Crystallin-a-B protein |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 0.5 mg/mL |
| Purification | Antigen affinity chromatography |
| Storage buffer | PBS with proprietary stabilizer |
| Contains | 0.01% sodium azide |
| Storage conditions | Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles. |
| Shipping conditions | Ambient (domestic); Wet ice (international) |
Product Specific Information
- Positive control: Mouse liver lysate
- Cellular location: Cytoplasm, Nuclear
Target Information
Lens proteins consist almost entirely of crystallins (about 95%), which are also found in vertebrate skeletal muscle tissue. In the lens, their structural function is to maintain the proper refractive index. The mammalian lens contains three major classes of crystallins: alpha, beta, and gamma.
Alpha-crystallin is the largest and composed of two primary gene products, alpha-A and alpha-B. Alpha-B crystallin comprises about 40% of total lens protein and functions as a molecular chaperone, preventing protein aggregation that may lead to cataract formation.
Phosphorylated states of alpha-crystallin respond to cellular stress and may serve structural control and protein maintenance roles. Alpha-B crystallin has been linked to Alexander’s disease, where it accumulates in brain cells.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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