Datasheet

Biological Description

Specificity	Anti-β Crystallin A3 Rabbit Antibody [N15M18] recognizes total endogenous levels of β Crystallin A3 protein.
Background	Crystallins, the predominant proteins of the ocular lens, are crucial for maintaining the lens’s transparency and refractive properties. Although best known for their structural role in the lens, crystallins are also expressed in non-lens tissues, where they perform diverse cellular functions. Among them, β-crystallins constitute the largest fraction of human lens proteins and exist as a heterogeneous population of dimers and higher-order oligomers, with molecular weights ranging from ~50 to 200 kDa. The human lens contains α-, β-, and γ-crystallins; within this group, seven β-crystallin subtypes have been identified—four acidic (βA1, βA2, βA3, βA4) and three basic (βB1, βB2, βB3). Their distribution across size classes is influenced by protein concentration, ionic strength, and pH. The N-terminal extension of βA3-crystallin facilitates its assembly into homodimers. Interestingly, βA3- and βA1-crystallins are also expressed in astrocytes and retinal pigment epithelial (RPE) cells, where they are essential for lysosomal acidification. In RPE cells, defective acidification results in elevated lysosomal pH, which disrupts phagocytosis and autophagy, ultimately leading to the accumulation of undigested material within autophagolysosomes. A distinctive feature of βA3/A1-crystallin is that both proteins are produced from a single Cryba1 mRNA through alternative translation via leaky ribosomal scanning, generating two closely related isoforms—βA3 and βA1—from separate translation initiation sites.

Specificity

Anti-β Crystallin A3 Rabbit Antibody [N15M18] recognizes total endogenous levels of β Crystallin A3 protein.

Background

Crystallins, the predominant proteins of the ocular lens, are crucial for maintaining the lens’s transparency and refractive properties. Although best known for their structural role in the lens, crystallins are also expressed in non-lens tissues, where they perform diverse cellular functions. Among them, β-crystallins constitute the largest fraction of human lens proteins and exist as a heterogeneous population of dimers and higher-order oligomers, with molecular weights ranging from ~50 to 200 kDa. The human lens contains α-, β-, and γ-crystallins; within this group, seven β-crystallin subtypes have been identified—four acidic (βA1, βA2, βA3, βA4) and three basic (βB1, βB2, βB3). Their distribution across size classes is influenced by protein concentration, ionic strength, and pH. The N-terminal extension of βA3-crystallin facilitates its assembly into homodimers. Interestingly, βA3- and βA1-crystallins are also expressed in astrocytes and retinal pigment epithelial (RPE) cells, where they are essential for lysosomal acidification. In RPE cells, defective acidification results in elevated lysosomal pH, which disrupts phagocytosis and autophagy, ultimately leading to the accumulation of undigested material within autophagolysosomes. A distinctive feature of βA3/A1-crystallin is that both proteins are produced from a single Cryba1 mRNA through alternative translation via leaky ribosomal scanning, generating two closely related isoforms—βA3 and βA1—from separate translation initiation sites.

Usage Information

Application

WB, IF

Dilution

WB	IF
1:10000 - 1:50000	1:50- 1:100

Reactivity

Mouse, Rat, Human

Source

Rabbit

MW

25 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/18823128/
https://pubmed.ncbi.nlm.nih.gov/25461968/

Anti-β Crystallin A3 Rabbit Antibody [N15M18]

Biological Description

Usage Information

References

Application Data