Rabbit Multiclonal HJURP antibody. Suitable for ICC/IF, WB and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human HJURP.
IgG
Rabbit
pH: 7.4
Preservative: 0.09% Sodium azide
Constituents: 99.91% PBS
Liquid
Multiclonal
ICC/IF | WB | |
---|---|---|
Human | Tested | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500 | Notes - |
Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerization and prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds Holliday junctions.
FAKTS, FLEG1, URLC9, HJURP, FAKTS, FLEG1, URLC9, Holliday junction recognition protein, 14-3-3-associated AKT substrate, Fetal liver-expressing gene 1 protein, Up-regulated in lung cancer 9
Rabbit Multiclonal HJURP antibody. Suitable for ICC/IF, WB and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human HJURP.
IgG
Rabbit
pH: 7.4
Preservative: 0.09% Sodium azide
Constituents: 99.91% PBS
Liquid
Multiclonal
RP23040269
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
Recombinant multiclonals are a mixture of recombinant antibodies co-expressed from a library of heavy and light chains.
Recombinant multiclonal antibodies offer the sensitivity of polyclonal antibodies by recognising multiple epitopes, along with consistency of a recombinant antibody.
This supplementary information is collated from multiple sources and compiled automatically.
HJURP also known as Holliday junction recognition protein plays an important mechanical role in chromatin assembly. This protein weighs approximately 82 kDa and coordinates the correct loading of CENP-A at the centromeres during S phase and early G1 phase of the cell cycle. HJURP is mostly expressed in proliferative tissues and cell lines reflecting its involvement in processes requiring accurate chromosomal segregation during cell division. Its presence ensures that centromere identity is passed onto the daughter cells.
HJURP is critical for centromere function and stability. It operates by forming a complex with centromere protein A (CENP-A) which completes the assembly and maintenance of centromere chromatin. HJURP achieves this by acting as a chaperone specifically ensuring the accurate deposition of CENP-A at the centromeres. The functionality of HJURP within this complex highlights its role in sustaining genomic integrity throughout cell division processes.
HJURP lies at the center of the centromere-specific chromatin assembly pathway. This pathway is essential for the replenishment of centromeric CENP-A thereby ensuring accurate chromosome segregation. HJURP interacts significantly with other proteins such as CALM and H4 aiding in chromatin dynamics and stability. These interactions help integrate HJURP's actions into larger cellular and genetic processes particularly those involving DNA replication and cell cycle progression.
HJURP links closely to cancerous transformations and chromosomal instability disorders. Abnormal expression or mutations of HJURP can disrupt centromere function potentially leading to aneuploidy—a condition often found in various cancers. Its association with other proteins such as HJURP's interaction with overexpressed CENP-A in these pathological states highlights its significance in maintaining cellular health. Therefore HJURP emerges as a potential biomarker for these conditions and warrants further research into therapeutic interventions.
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Western blot analysis was performed on modified whole cell extracts (30 µg lysate) of HeLa (Lane 1), T98G (Lane 2), U-87 MG (Lane 3) and U-2 OS (Lane 4). The blot was probed with ab308103 at 1:500 dilution and detected by chemiluminescence using a Goat anti-Rabbit IgG (H+L) Secondary Antibody, HRP conjugate at 1:4000 dilution. A ~83 kDa band corresponding to HJURP was observed across the cell lines tested.
All lanes: Western blot - Anti-HJURP antibody [RP23040269] (ab308103) at 1/500 dilution
Lane 1: HeLa whole cell lysate at 30 µg
Lane 2: T98G whole cell lysate at 30 µg
Lane 3: U-87 MG whole cell lysate at 30 µg
Lane 4: U-2 OS whole cell lysate at 30 µg
All lanes: HRP-conjugated Goat anti-Rabbit IgG (H+L) Secondary Antibody at 1/4000 dilution
Developed using the ECL technique.
Observed band size: 83 kDa
Knockdown of HJURP was achieved by transfecting A549 cells with HJURP specific siRNA. Western blot analysis was performed using modified whole cell extracts (1% SDS) from HJURP knockdown cells (Lane 2) and non-specific scrambled siRNA transfected cells (Lane 1). The blot was probed with ab308103 at 1:500 dilution and a Goat anti-Rabbit IgG (H+L) Secondary Antibody, HRP conjugate at 1:4000 dilution. Loss of signal upon siRNA mediated knockdown confirms that antibody is specific to HJURP.
All lanes: Western blot - Anti-HJURP antibody [RP23040269] (ab308103) at 1/500 dilution
Lane 1: non-specific scrambled siRNA transfected A549 cells
Lane 2: HJURP knockdown A549 cells
All lanes: HRP-conjugated Goat anti-Rabbit IgG (H+L) Secondary Antibody at 1/4000 dilution
Observed band size: 83 kDa
For immunofluorescence analysis, A549 cells were fixed and permeabilized for detection of endogenous HJURP using ab308103 at 1/100 dilution and labeled with a Goat anti-Rabbit IgG (H+L) Secondary Antibody, Alexa Fluor® 488 conjugate at 1/2000 dilution.
Panel a) shows representative cells that were stained for detection and localization of HJURP protein (green)
Panel b) is stained for nuclei (blue) using DAPI
Panel c) represents cytoskeletal F-actin staining using Rhodamine Phalloidin at 1/300 dilution
Panel d) is a composite image of Panels a, b and c clearly demonstrating nuclear localization of HJURP
Panel e) represents control cells with no primary antibody to assess background
The images were captured at 60X magnification
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