Size: 100ul

Catalog no.: bs-12970R-A594

Price: 350 EUR

Product details

Gene ID Number


Modification Site


French translation


Tested applications




Excitation emission



1ug per 1ul



Conjugated with



Human, Mouse, Rat


Alexa conjugate 1

Recommended dilutions



Polyclonal antibody


Purified by Protein A.

Target Antigen

alpha B Crystallin Ser45


Conjugated Primary Antibodies


Alexa Fluor,ALEXA FLUOR® 594

Host Organism

Rabbit (Oryctolagus cuniculus)

Also known as

Anti-alpha B Crystallin Ser45 PAb ALEXA FLUOR 594

Long name

alpha B Crystallin (Ser45) Antibody, ALEXA FLUOR 594 Conjugated


This is a highly specific antibody against alpha B Crystallin Ser45.

Cross-reactive species details

Due to limited amount of testing and knowledge, not every possible cross-reactivity is known.


The Anti-alpha B Crystallin Ser45 is a α- or alpha protein sometimes glycoprotein present in blood.


KLH conjugated synthetic phosphopeptide derived from human alpha B Crystallin around the phosphorylation site of Ser45

Storage conditions

Store this antibody in aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Keep refrigerated at 2 to 8 degrees Celcius for up to one year.


For facs or microscopy Alexa 1 conjugate.If you buy Antibodies supplied by Bioss Primary Conjugated Antibodies. ALEXA FLUOR they should be stored frozen at - 24°C for long term storage and for short term at + 5°C.


alpha B Crystallin phospho S45; alpha B Crystallin phospho Ser45; p-alpha B Crystallin S45; p-alpha B Crystallin Ser45; AACRYA; Alpha B crystallin; Alpha crystallin B chain; Alpha crystallin B chain; AlphaB crystallin; AlphaB-crystallin; Alpha-crystallin B chain; CRYA2; CRYAB; CRYAB_HUMAN; Crystallin alpha B; Crystallin alpha polypeptide 2; CTPP 2; CTPP2; Heat shock 20 kD like protein; Heat shock protein beta 5; Heat shock protein beta-5; HSPB5; NY REN 27 antigen; Renal carcinoma antigen NY REN 27; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component.

Background of the antigen

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. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008].