Render Target: SSR
Render Timestamp: 2024-12-26T19:16:06.915Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-05-10 22:35:49.984
Product last modified at: 2024-11-27T13:15:09.149Z
Cell Signaling Technology Logo
1% for the planet logo
PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Hydroxyproline Antibody #73812

Filter:
  • IHC

    Supporting Data

    REACTIVITY All
    SENSITIVITY Endogenous
    MW (kDa)
    SOURCE Rabbit
    Application Key:
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • All-All Species Expected 

    Product Information

    Product Description

    Hydroxyproline Antibody provides a means of visualizing hydroxyproline in paraffin-embedded tissues. Using Hydroxyproline Antibody in the IHC assay, global collagen in tissue can be detected, while also providing contextual information that is lost in traditional hydroxyproline assays. Additionally, Hydroxyproline Antibody can be combined with other antibodies to enable detection of other markers of interest.

    Product Usage Information

    Application Dilution
    Immunohistochemistry (Paraffin) 1:50 - 1:200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Hydroxyproline Antibody recognizes endogenous levels of proline only when the proline is hydroxylated. The antibody does not react with non-hydroxylated proline.

    Species Reactivity:

    All Species Expected

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with an antigen containing hydroxyproline. Antibodies are purified by affinity chromatography.

    Background

    Collagens are a large family of proteins and collectively they are the most abundant protein in mammals. They are trimeric molecules comprised of three alpha polypeptide chains that form a triple helix structure that is characteristic of all collagens (1). Collagen chains have important features that allow helix to form: every third amino acid in the sequence is a glycine, and the chains are co- and post-translationally modified. Prolines are hydroxylated by collagen prolyl 4-hydroxylases. These hydroxyproline modifications are critical for the stability of the triple helix to form fibrils (2).

    While proline hydroxylation occurs on a small number of other proteins, the hydroxyproline content of tissue comes almost entirely from collagen, such that hydroxyproline quantitative biochemical assays are routinely utilized as a measurement of collagen (3).
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    SignalStain is a registered trademark of Cell Signaling Technology, Inc.
    All other trademarks are the property of their respective owners. Visit our Trademark Information page.