Flow Cytometry (FC/FACS)
(Flow-cytometry using anti-CD3 epsilon and TRP1 antibodies. Mouse splenocytes (A), B16F10 murine melanoma cells (B), KPC3 pacreas carcinoma cells (C) and KPC3 cells transfected with the Trp1 gene (D) were fixed using 2% PFA, permeabilised using 0.5% Triton and were subject to a primary treatment of either buffer, mouse-IgG1 chimeric 2C11 or mouse-IgG1 chimeric TA99 (indicated above plots) before a secondary treatment with buffer, goat anti-mouse Ig-allophycocyanin (G-aM Ig-APC) or anti-HisTag-APC (aHis-APC) antibodies (indicated beside plots). In panel A, splenocytes were also stained with a commercially available anti-CD3 (2C11) antibody conjugated to phycoerythrin (PE); all cells (i-v) were CD3 and thus PE positive. In subpanel ‘A v’ an increase in APC fluorescence intensity (FI(APC)) indicates binding of aHis-APC to 2C11 bound to CD3 at the cell surface. Some Ig containing proteins expressed by the splenocytes may explain the increase in APC fluorescence in subpanel ‘A iii’. In panel B an increase in FI(APC) in subpanel ‘iii’ indicates that TA99 binds to heavily expressed TRP1 at B16F10 cell surfaces and is then detectable using an G-aM Ig-APC antibody. Conversely, G-aM Ig-APC did not detect 2C11 at the cell surface, whereas a subset of cells with 2C11 bound to the surface were detectable using aHis-APC. Panel C shows that TRP1 is not detectable in KPC3 carcinoma cells (‘Ci, iii, v’) as expected, and that again, aHis-APC is able to detect a small subset of CD3 expressing cells (‘C vi’). When transfected with the Trp1 gene, KPC3 cells then strongly express TRP1 and it becomes detectable (‘D iii’). A small subset of CD3 positive cells was again detectable in Trp1 transfected KPC3 cells (‘D vi’). All analyses were made using FACSCanto flow-cytometer.)
TRP-1 recombinant antibody
Anti-TRP-1, gp75 [TA99]
Flow Cytometry (FC/FACS)
(Flow-cytometry using anti-CD3 epsilon and TRP1 antibodies. Mouse splenocytes (A), B16F10 murine melanoma cells (B), KPC3 pacreas carcinoma cells (C) and KPC3 cells transfected with the Trp1 gene (D) were fixed using 2% PFA, permeabilised using 0.5% Triton and were subject to a primary treatment of either buffer, mouse-IgG1 chimeric 2C11 or mouse-IgG1 chimeric TA99 (indicated above plots) before a secondary treatment with buffer, goat anti-mouse Ig-allophycocyanin (G-aM Ig-APC) or anti-HisTag-APC (aHis-APC) antibodies (indicated beside plots). In panel A, splenocytes were also stained with a commercially available anti-CD3 (2C11) antibody conjugated to phycoerythrin (PE); all cells (i-v) were CD3 and thus PE positive. In subpanel ‘A v’ an increase in APC fluorescence intensity (FI(APC)) indicates binding of aHis-APC to 2C11 bound to CD3 at the cell surface. Some Ig containing proteins expressed by the splenocytes may explain the increase in APC fluorescence in subpanel ‘A iii’. In panel B an increase in FI(APC) in subpanel ‘iii’ indicates that TA99 binds to heavily expressed TRP1 at B16F10 cell surfaces and is then detectable using an G-aM Ig-APC antibody. Conversely, G-aM Ig-APC did not detect 2C11 at the cell surface, whereas a subset of cells with 2C11 bound to the surface were detectable using aHis-APC. Panel C shows that TRP1 is not detectable in KPC3 carcinoma cells (‘Ci, iii, v’) as expected, and that again, aHis-APC is able to detect a small subset of CD3 expressing cells (‘C vi’). When transfected with the Trp1 gene, KPC3 cells then strongly express TRP1 and it becomes detectable (‘D iii’). A small subset of CD3 positive cells was again detectable in Trp1 transfected KPC3 cells (‘D vi’). All analyses were made using FACSCanto flow-cytometer.)
Flow Cytometry (FC/FACS)
(Flow-cytometry using anti-CD3 epsilon and TRP1 antibodies. Mouse splenocytes (A), B16F10 murine melanoma cells (B), KPC3 pacreas carcinoma cells (C) and KPC3 cells transfected with the Trp1 gene (D) were fixed using 2% PFA, permeabilised using 0.5% Triton and were subject to a primary treatment of either buffer, mouse-IgG1 chimeric 2C11 or mouse-IgG1 chimeric TA99 (indicated above plots) before a secondary treatment with buffer, goat anti-mouse Ig-allophycocyanin (G-aM Ig-APC) or anti-HisTag-APC (aHis-APC) antibodies (indicated beside plots). In panel A, splenocytes were also stained with a commercially available anti-CD3 (2C11) antibody conjugated to phycoerythrin (PE); all cells (i-v) were CD3 and thus PE positive. In subpanel ‘A v’ an increase in APC fluorescence intensity (FI(APC)) indicates binding of aHis-APC to 2C11 bound to CD3 at the cell surface. Some Ig containing proteins expressed by the splenocytes may explain the increase in APC fluorescence in subpanel ‘A iii’. In panel B an increase in FI(APC) in subpanel ‘iii’ indicates that TA99 binds to heavily expressed TRP1 at B16F10 cell surfaces and is then detectable using an G-aM Ig-APC antibody. Conversely, G-aM Ig-APC did not detect 2C11 at the cell surface, whereas a subset of cells with 2C11 bound to the surface were detectable using aHis-APC. Panel C shows that TRP1 is not detectable in KPC3 carcinoma cells (‘Ci, iii, v’) as expected, and that again, aHis-APC is able to detect a small subset of CD3 expressing cells (‘C vi’). When transfected with the Trp1 gene, KPC3 cells then strongly express TRP1 and it becomes detectable (‘D iii’). A small subset of CD3 positive cells was again detectable in Trp1 transfected KPC3 cells (‘D vi’). All analyses were made using FACSCanto flow-cytometer.)
Original Published Journal: Proc Natl Acad Sci U S A. 1987 Jun;84(12):4200-4.
Publication Note: Describes the isolation of TA99 from mice immunized with the pigmented melanoma cell line SK-MEL-23 and the characterisation by radioimmunolocalisation showing the tumor imaging.
NCBI and Uniprot Product Information
NCBI Description
This gene encodes a melanosomal enzyme that belongs to the tyrosinase family and plays an important role in the melanin biosynthetic pathway. Defects in this gene are the cause of rufous oculocutaneous albinism and oculocutaneous albinism type III. [provided by RefSeq, Mar 2009]
Uniprot Description
TYRP1: Oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Defects in TYRP1 are the cause of albinism oculocutaneous type 3 (OCA3); also known as Rufous oculocutaneous albinism. An autosomal recessive disorder in which the biosynthesis of melanin pigment is reduced in skin, hair, and eyes. Tyrosinase activity is normal and patients have only moderate reduction of pigment. The eyes present red reflex on transillumination of the iris, dilution of color of iris, nystagmus and strabismus. Darker-skinned individuals have bright copper-red coloration of the skin and hair. Belongs to the tyrosinase family.
Protein type: Amino Acid Metabolism - tyrosine; EC 1.14.18.-; Membrane protein, integral; Oxidoreductase
Chromosomal Location of Human Ortholog: 9p23
Cellular Component: endosome membrane; melanosome; melanosome membrane
Molecular Function: protein binding; protein heterodimerization activity; protein homodimerization activity
Biological Process: positive regulation of melanin biosynthetic process
Disease: Albinism, Oculocutaneous, Type Iii; Skin/hair/eye Pigmentation, Variation In, 11
Research Articles on TRP-1
Similar Products
Product Notes
The TRP-1 tyrp1 (Catalog #AAA488391) is a Recombinant Antibody and is intended for research purposes only. The product is available for immediate purchase. The Anti-TRP-1, gp75 [TA99] reacts with Human and may cross-react with other species as described in the data sheet. AAA Biotech's TRP-1 can be used in a range of immunoassay formats including, but not limited to, ELISA (EIA), Flow Cytometry (FC/FACS), Immunofluorescence (IF), Immunohistochemistry (IHC) Frozen, Immunoprecipitation (IP), Western Blot (WB). Researchers should empirically determine the suitability of the TRP-1 tyrp1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "TRP-1, Monoclonal Recombinant Antibody" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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