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CRYBA4 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P53673 |
| Other Accession | NP_001877.1 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 22374 Da |
| Antigen Region | 98-127 aa |
| Gene ID | 1413 |
|---|---|
| Other Names | Beta-crystallin A4, Beta-A4 crystallin, CRYBA4 |
| Target/Specificity | This CRYBA4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 98-127 amino acids from the C-terminal region of human CRYBA4. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | CRYBA4 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | CRYBA4 |
|---|---|
| Function | Crystallins are the dominant structural components of the vertebrate eye lens. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq].
References
Zhou, G., et al. Mol. Vis. 16, 1019-1024 (2010) :
Zhang, X., et al. Mol. Vis. 15, 2911-2918 (2009) :
Billingsley, G., et al. Am. J. Hum. Genet. 79(4):702-709(2006)
Collins, J.E., et al. Genome Biol. 5 (10), R84 (2004) :
Mackay, D.S., et al. Am. J. Hum. Genet. 71(5):1216-1221(2002)
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