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Crystallin-αB Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P |
|---|---|
| Primary Accession | P02511 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 20159 Da |
| Gene ID | 1410 |
|---|---|
| Other Names | CRYAB; CRYA2; Alpha-crystallin B chain; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component |
| Dilution | IHC~~Immunohistochemistry: 1/100 - 1/300. ELISA: 1/5000. Not yet tested in other applications. |
| Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
| Storage Conditions | -20℃ |
| Name | CRYAB (HGNC:2389) |
|---|---|
| Synonyms | CRYA2, HSPB5 |
| Function | May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). |
| Cellular Location | Cytoplasm. Nucleus Secreted. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (PubMed:19464326). Localizes at the Z- bands and the intercalated disk in cardiomyocytes (PubMed:28493373) Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum- Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). |
| Tissue Location | Lens as well as other tissues (PubMed:2387586, PubMed:838078). Expressed in myocardial tissue (PubMed:28493373) |
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Provided below are standard protocols that you may find useful for product applications.
Background
May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
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