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Anti-β Crystallin A3 Rabbit Antibody [N15M18]

Catalog No.: F3970

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:10000 - 1:50000 IF1:50- 1:100

Application
WB, IF

Reactivity
Mouse, Rat, Human

Source
Rabbit

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

Predicted MW
25 kDa

Datasheet & SDS

Biological Description

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

Clone
N15M18

Synonym(s)
CRYB1, CRYBA1, Beta-crystallin A3

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%