Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) (AA 1-213) antibody

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Antigen
Synonyms Vhlh, HRCA1, RCA1, VHL1, pVHL
Epitope
AA 1-213
(9), (8), (7), (4), (4), (3), (3), (2), (2), (2), (1), (1)
Reactivity
Human
(80), (42), (40), (15), (12)
Host
Mouse
(58), (22), (7)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(4), (4), (3), (3), (3), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (Formalin-fixed Sections) (IHC (f)), Immunoprecipitation (IP)
(60), (32), (22), (14), (10), (5), (4), (3), (3), (1), (1)
Pubmed 7 references available
Quantity 0.1 mg
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Catalog No. ABIN967508
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Immunogen Human VHL Recombinant Protein
Clone Ig32
Isotype IgG1
Cross-Reactivity Mouse (Murine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
3. Please refer to us for technical protocols.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name VHL
Background The von Hippel-Lindau (VHL) protein is a tumor suppressor that is highly conserved from Drosophila to mammals. VHL protein normally associates with the transcription factor Elongin. Transcription factors typically act in one of three transcriptional stages, initiation, elongation or termination. Elongin functions by increasing the rate of elongation, the rate at which RNA subunits are added to make an RNA transcript longer. Elongin is made up of three subunits, A, B, and C, and each subunit contributes to the function of the whole protein. VHL binds to Elongin B and C subunits, and appears to prevent Elongin A from associating with the B and C subunits, thereby inhibiting the transcriptional activity of Elongin. The ability of VHL to block Elongin function may play a role in normal cell growth regulation. Mutated VHL sequences lose their ability to bind to Elongin subunits B and C, suggesting that the tumor suppression function of VHL may be linked to its ability to bind to Elongin. Likewise, the introduction of wild-type VHL suppresses growth in tumor cell lines lacking normal expression of VHL genes, further supporting a role for VHL in negative growth regulation. The calculated molecular weight of VHL is 24 kDa. However, different migrating species ranging from 21-30 kDa have been observed using antibodies to VHL, and may result from a variety of factors including alternatively spliced VHL mRNAs and protein degradation. This antibody has been reported to recognize both human and mouse VHL.
Synonyms: von Hippel-Lindau protein, RCA1, HRCA1
Molecular Weight 21-30 kDa
Research Area Hormones, Cytokines
Application Notes Western Blot:
Clone Ig32 is not recommended for Western blot application. It has been shown to recognize a non-specific band above VHL protein. However, RNAi studies have demostrated that clone Ig32 recognizes a fainter band below this dominant band. Also, labs have reported using the 786-O renal cell adenocarcinoma cell line (ATCC CRL-1932, VHL null), siRNA or VHL overexpression to show that clone Ig32 recognizes the VHL protein specifically. Therefore, we recommend using clone Ig32 in over-expressing systems or under native (non-denaturing) conditions such as IHC staining or immunoprecipitation (IP) applications.

Immunohistochemistry:
The Ig32 antibody is useful for immunohistochemical staining. Following Retrievagen A pretreatment, purified Ig32 antibody should be used at 2.5 µg/ml to 5 µg/ml and titrated for optimal indirect immunohistochemical staining. Tissues can be visualized via a three-step staining procedure in combination with Biotin Goat anti-Mouse Ig secondary antibody and Streptravidin-HRP together with the DAB Substrate Kit. More conveniently, a Anti-Mouse Ig HRP Detection Kit that contains the biotinylated secondary antibody, antibody diluent, streptavidin-HRP and DAB substrate can be used for staining.
IP:
The purified Ig32 antibody has been reported to be useful to immunoprecipitate native human VHL. Please note that this application is not routinely tested. Investigators are advised to determine optimal concentrations for individual applications.
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/ml
Buffer Aqueous buffered solution.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Supplier Images
anti-Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) (AA 1-213) antibody VHL Immunohistochemical staining on human renal cell carcinoma. Formalin fixed paraffin embedded human renal cell carcinoma was pretreated with BD Retrervagen A and then stained with either Purified Mouse IgG1, kappa isotype control (Clone MOPC-21, First Panel) or Purified Mouse anti-VHL (Second Panel).
anti-Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) (AA 1-213) antibody (2) Stained with purified Mouse anti-VHL.
anti-Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) (AA 1-213) antibody (3) anti-Von Hippel-Lindau Tumor Suppressor, E3 Ubiquitin Protein Ligase (VHL) (AA 1-213) antibody (Image 3)
Product cited in: Iliopoulos, Kibel, Gray et al.: "Tumour suppression by the human von Hippel-Lindau gene product." in: Nature medicine, Vol. 1, Issue 8, pp. 822-6, 1995 (PubMed).

Chen, Kishida, Duh et al.: "Suppression of growth of renal carcinoma cells by the von Hippel-Lindau tumor suppressor gene." in: Cancer research, Vol. 55, Issue 21, pp. 4804-7, 1995 (PubMed).

Kibel, Iliopoulos, DeCaprio et al.: "Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C." in: Science (New York, N.Y.), Vol. 269, Issue 5229, pp. 1444-6, 1995 (PubMed).

Iliopoulos, Ohh, Kaelin: "pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 20, pp. 11661-6, 1998 (PubMed).

Baba, Hirai, Kawakami et al.: "Tumor suppressor protein VHL is induced at high cell density and mediates contact inhibition of cell growth." in: Oncogene, Vol. 20, Issue 22, pp. 2727-36, 2001 (PubMed).

Qi, Gervais, Li et al.: "Molecular cloning and characterization of the von Hippel-Lindau-like protein." in: Molecular cancer research : MCR, Vol. 2, Issue 1, pp. 43-52, 2004 (PubMed).

Hsu, Adereth, Kose et al.: "Endocytic function of von Hippel-Lindau tumor suppressor protein regulates surface localization of fibroblast growth factor receptor 1 and cell motility." in: The Journal of biological chemistry, Vol. 281, Issue 17, pp. 12069-80, 2006 (PubMed).

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