antibody

Anti-Alpha A Crystallin Monoclonal Antibody

MBS190603

0.1 mg

260 USD

monoclonal

mouse

nonconjugated

1H3.B8

human, mouse, rat, cow

western blot, ELISA

Antibody

Anti-Alpha A Crystallin Monoclonal Antibody

Alpha A Crystallin

alpha-A-crystallin; Alpha-crystallin A chain; alpha-crystallin A chain; OTTHUMP00000109430; crystallin, alpha-1; heat shock protein beta-4; human alphaA-crystallin (CRYA1); crystallin, alpha A; Heat shock protein beta-4

CRYAA; CRYAA; CRYA1; HSPB4; CRYA1; HSPB4

CRYAA_HUMAN

Monoclonal

IgG1

1H3.B8

Mouse

Human, mouse, rat, bovine

Alpha A Crystallin. This antibody recognizes human, mouse, rat, and bovine alpha A crystallin. Other species have not been tested. It does not cross-react with alpha B crystallin, beta-L crystallin, beta- H crystallin, gamma crystallin, Hsp25, Hsp27, or Hsp47.

100ug Protein G-purified antibody in PBS, pH 7.4.

This antibody is stable for at least one (1) year at -20 degree C. Avoid repeated freezing and thawing.

ELISA; Immunoblot

Immunoblotting: use at 0.5-1ug/ml. A band of ~20 kDa is detected. ELISA. User should determine optimal concentrations for their application. Positive control: Purified alpha A crystallin.

Antigen: Native alpha crystallin. Preservative: None.

Dilution Instructions: Dilute in PBS or medium which is identical to that used in the assay system.

Alpha crystallins are water-soluble lens proteins of the vertebrate eye that are related to the small heat shock protein family. Lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are further divided into acidic (Alpha A) and basic (Alpha B) groups. In the lens, alpha crystallin maintains proper refractive index, however it can also function as a molecular chaperone that binds to denatured proteins, keeping them in solution and maintaining the translucency of the lens. In response to cellular stress, alpha crystallin is phosphorlyated and may serve a structural control function and play a role in protein maintenance. Both alpha A and alpha B crystallin prevent apoptosis by inhibiting caspases.

181081

P02489

19,909 Da

Protein Processing In Endoplasmic Reticulum Pathway 167325!!Protein Processing In Endoplasmic Reticulum Pathway 167190

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. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC). [provided by RefSeq]

Function: May contribute to the transparency and refractive index of the lens. Subcellular location: Cytoplasm. Nucleus. Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Ref.16. Post-translational modification: O-glycosylated; contains N-acetylglucosamine side chains. Ref.9Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15. Involvement in disease: Defects in CRYAA are a cause of cataract autosomal dominant (ADC) [. MIM:604219]. Cataract is an opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Cataract is the most common treatable cause of visual disability in childhood. Ref.17 Ref.18 Ref.19 Ref.22. Sequence similarities: Belongs to the small heat shock protein (HSP20) family. Mass spectrometry: Molecular mass is 19950 Da from positions 1 - 173. Determined by ESI. Ref.10Molecular mass is 19863 Da from positions 1 - 172. Determined by ESI. Ref.10Molecular mass is 20029 Da from positions 1 - 173. Determined by ESI. With 1 phosphate group. Ref.10Molecular mass is 19951 Da from positions 1 - 173. Determined by ESI. Ref.13Molecular mass is 19864 Da from positions 1 - 172. Determined by ESI. Ref.13Molecular mass is 19947 Da from positions 1 - 173. Determined by ESI. Ref.14Molecular mass is 19851 Da from positions 1 - 172. Determined by ESI. Ref.14

0.1 mg

260 USD