Work with LifeSpan to design a custom immunohistochemistry to address your specific biological question. Outsource the entire localization process without having to
worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting
immunostaining in relation to complex human pathologies.
TCR Screening Services
Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding.
Our non-GLP TCR services are designed on the FDA recommendation outlined in their "Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use".
Rabbit Polyclonal (IgG) to Human CRYAA / Alpha A Crystallin
Human, Mouse, Rat, Zebrafish
IHC, Immunofluorescence, Western blot
Mouse Monoclonal [clone C9F2] (IgG1) to Human CRYAA / Alpha A Crystallin
Western blot, ELISA
Human CRYAA / Alpha A Crystallin
Human (tested or 100% immunogen sequence identity)
IgG1 Monoclonal [C9F2]
Protein G purified
Western blot (1:500 - 1:2000)
Specificity and Use
Recombinant human kappa-Crystallin A protein Isotype Mouse IgG1, heavy chains and kappa light chains.
The antibody has been tested by ELISA and by Western blot analysis to assure specificity and reactivity. Since application vary, however, each investigation should titrate the reagent to obtain optimal results. Recommended dilution range for Western blot analysis: 1:500-1:2000. Recommended starting dilution: 1:1000.
PBS, pH 7.4, 0.1% sodium azide
Long term: -20°C; Short term: +4°C; Avoid freeze-thaw cycles.
CRYAA Antibody, Alpha-crystallin A chain Antibody, Crystallin, alpha A Antibody, CRYA1 Antibody, Crystallin, alpha-1 Antibody, Heat shock protein beta-4 Antibody, HSPB4 Antibody
Mammalian lens crystallins are divided into alpha, beta, and gamma families. 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 (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.
Rat eye extracts were resolved by electrophoresis, transferred to PVDF membrane and probed with anti-crystallin a?(1:1000). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a DAP detection system. Arrow indicates crystalline a?(~20 kD). This antibody is not shown cross-activity.