Thermo Fisher Scientific Alpha B Crystallin Polyclonal Antibody
Rabbit polyclonal antibody targeting human Alpha B Crystallin for WB applications. Reacts with bovine, chicken, human, mouse, and rat. Supplied as liquid whole serum without preservative. Ideal for research on lens protein structure and stress response...
- 카탈로그번호
- 11073-100UL
- 판매단위
- pk
카탈로그
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Applications
- Western Blot (WB): Tested dilution 1:5,000–1:10,000
Product Specifications
| 항목 | 내용 |
|---|---|
| Species Reactivity | Bovine, Chicken, Human, Mouse, Rat |
| Host / Isotype | Rabbit |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | Synthetic peptide corresponding to human alpha B crystallin |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 0.5–1.0 mg/mL |
| Storage Buffer | Whole serum |
| Contains | No preservative |
| Storage Conditions | -20°C, Avoid freeze/thaw cycles |
| Shipping Conditions | Ambient (domestic); Wet ice (international) |
Target Information
Lens proteins consist almost entirely of crystallins (about 95%). Crystallins 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.
- Beta-crystallins comprise at least five different proteins.
- Gamma-crystallins are monomeric, with several identified in bovine and rat lens.
Alpha-crystallin comprises about 40% of total lens protein and also functions as a molecular chaperone, preventing protein aggregation that may lead to cataract formation.
Phosphorylation of alpha-crystallin occurs in response to cellular stress, playing a role in structural control and protein maintenance.
Alpha-B crystallin has been linked to Alexander’s disease, where it accumulates in brain cells of affected individuals.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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