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MKI67 Antibody, Mouse MAb

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Human MKI67 Antibody Product Information
Immunogen:Recombinant Human MKI67 protein (Catalog#13180-H09E)
Clone ID:01
Ig Type:Mouse IgG1
Formulation:0.2 μm filtered solution in PBS with 5% trehalose
Preparation:This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human MKI67 (rh MKI67; Catalog#13180-H09E; P46013-2; Met1-Pro120). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Human MKI67 Antibody Usage Guide
Specificity:Human MKI67
Application:WB, ICC/IF, IF

WB: 5-10 μg/mL

ICC/IF: 10-25 μg/mL

Storage:This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
Human MKI67 Antibody WB Application Image
MKI67 Antibody, Mouse MAb, Western blot
Human MKI67 Antibody IF Application Image
[Click to enlarge image]
Immunofluorescence staining of Human MKI67 in Hela cells. Cells were fixed with 4% PFA, permeabilzed with 0.3% Triton X-100 in PBS, blocked with 10% serum, and incubated with mouse anti-Human MKI67 monoclonal antibody (15 µg/ml) at 37℃ 1 hour. Then cells were stained with the Alexa Fluor® 488-conjugated Goat Anti-mouse IgG secondary antibody (green) and counterstained with DAPI (blue). Positive staining was localized to nucleus.
MKI67 Antibody, Mouse MAb, Immunohistochemistry
Other MKI67 Antibody Products
Ki67 / MKI67 Background

MKI67 contains 1 FHA domain and plays a key role in cell proliferation. During interphase, the MKI67 antigen can be exclusively detected within the cell nucleus, whereas in mitosis most of the protein is relocated to the surface of the chromosomes. MKI67 protein is present during all active phases of the cell cycle (G1, S, G2, and mitosis), but is absent from resting cells. MKI67 is an excellent marker to determine the growth fraction of a given cell population. The fraction of MKI67-positive tumor cells is often correlated with the clinical course of cancer. It is also associated with ribosomal RNA transcription. Inactivation of antigen MKI67 leads to inhibition of ribosomal RNA synthesis.

The MKI67 protein is a nuclear and nucleolar protein, which is tightly associated with somatic cell proliferation. Antibodies raised against the human MKI67 protein paved the way for the immunohistological assessment of cell proliferation, particularly useful in numerous studies on the prognostic value of cell growth in clinical samples of human neoplasms. MKI67 protein expression is an absolute requirement for progression through the cell-division cycle. Recently, MKI67 is proved be an independent prognostic factor for disease-free survival (HR 1.05-1.72) in multivariate analyses studies using samples from randomized clinical trials with secondary central analysis of the biomarker. MKI67 was not found to be predictive for long-term follow-up after chemotherapy. Nevertheless, high KI-67 was found to be associated with immediate pathological complete response in the neoadjuvant setting, with an LOE of II-B. MKI67 could be considered as a prognostic biomarker for therapeutic decision.

Human Ki67 / MKI67 References
  • Rahmanzadeh R, et al. (2007) Chromophore-assisted light inactivation of pKi-67 leads to inhibition of ribosomal RNA synthesis. Cell Prolif. 40(3):422-30.
  • Bullwinkel J, et al. (2006) Ki-67 protein is associated with ribosomal RNA transcription in quiescent and proliferating cells. J Cell Physiol. 206(3):624-35.
  • Schonk DM, et al. (1989) Assignment of the gene(s) involved in the expression of the proliferation-related Ki-67 antigen to human chromosome 10. Hum Genet. 83(3):297-9.
  • Endl E, et al., 2000, Exp Cell Res. Jun 15;257(2): 231-7.
  • Luporsi E, et al., 2012, Breast Cancer Res Treat. 132(3): 895-915.
  • Scholzen T, et al., 2000, J Cell Physiol. 182(3): 311-22.
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