Cat. # | Size | Price | Inventory |
---|---|---|---|
73812S | 100 µl |
REACTIVITY | All |
SENSITIVITY | Endogenous |
MW (kDa) | |
SOURCE | Rabbit |
Product Information
Application | Dilution |
---|---|
Immunohistochemistry (Paraffin) | 1:50 - 1:200 |
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
NOTE: Do not allow slides to dry at any time during this procedure.
For Citrate: Heat slides in a microwave submersed in 1X citrate unmasking solution until boiling is initiated; follow with 10 min at a sub-boiling temperature (95°-98°C). Cool slides on bench top for 30 min.
RECOMMENDED DETECTION REAGENTS |
SignalStain® Boost IHC Detection Reagent (HRP, Rabbit) #8114 | SignalStain® Boost IHC Detection Reagent (AP, Rabbit) #18653 |
---|---|---|
COMPATIBLE CHROMOGEN |
SignalStain® DAB Substrate Kit #8059 | SignalStain® Vibrant Red Alkaline Phosphatase Substrate Kit #76713 |
SignalStain® Vivid Purple Peroxidase Substrate Kit #96632 | SignalStain® Ultra Blue Alkaline Phosphatase Substrate Kit #12824 | |
SignalStain® Deep Black Peroxidase Substrate Kit #72986 | ||
SignalStain® Radiant Yellow Peroxidase Substrate Kit #69644 |
NOTE: Use of detection reagents other than those specified in this protocol may require further optimization of the primary antibody to account for the different sensitivities of the detection reagents.
posted February 2010
revised April 2020
Protocol Id: 1989
All Species Expected
Polyclonal antibodies are produced by immunizing animals with an antigen containing hydroxyproline. Antibodies are purified by affinity chromatography.
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).
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