Mouse anti tyrosinase

Manufactured by Santa Cruz Biotechnology

Sourced in United Kingdom

Mouse anti-tyrosinase is a primary antibody that specifically recognizes the tyrosinase protein. Tyrosinase is a key enzyme involved in the production of melanin pigments. This antibody can be used to detect and study the expression and localization of tyrosinase in various biological samples.

Automatically generated - may contain errors

Lab products found in correlation

Ne per nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (2 mentions) Anti hla abc apc, by Thermo Fisher Scientific (1 mentions) Anti cd54 pe, by Beckman Coulter (1 mentions) Anti pd l1 pe, by BioLegend (1 mentions) Anti mitf, by Santa Cruz Biotechnology (1 mentions) Anti hmb 45, by Agilent Technologies (1 mentions) Anti hla dr pecy7, by Beckman Coulter (1 mentions) Anti pd l2, by BioLegend (1 mentions) Anti cd3, by BD (1 mentions) Proliferating cell nuclear antigen (pcna), by Santa Cruz Biotechnology (1 mentions) Cleaved caspase 3, by Santa Cruz Biotechnology (1 mentions) Goat anti lamin b, by Santa Cruz Biotechnology (1 mentions) Imagequant las 4000 mini, by GE Healthcare (1 mentions) Supersignal west pico chemiluminescent substrate kit, by Thermo Fisher Scientific (1 mentions) Anti goat igg conjugated to horseradish peroxidase, by Santa Cruz Biotechnology (1 mentions) Mouse anti β actin, by Santa Cruz Biotechnology (1 mentions)

3 protocols using mouse anti tyrosinase

Murine Monoclonal Antibodies for Immunodetection

Check if the same lab product or an alternative is used in the 5 most similar protocols

The following murine mAbs were used for IHC: W6/32 to detect HLA class I antigens (Dianova); bbm.1 to stain for β2m (kindly provided by G. Moldenhauer, German Cancer Research Center, Heidelberg, Germany); anti–HMB-45 (Dako) to detect melanoma cells; anti-CD3 (BD Pharmingen) to stain for T cells.
For flow cytometry, the mouse mAbs were as follows: anti–HLA-ABC-APC (eBiosciences), anti–CD54-PE and anti–HLA-DR-PECy7 (Beckmann Coulter), anti–PD-L1-PE and anti–PD-L2 (Biolegend), anti–B7-H3 (R&D Systems), anti–B7-H4 (eBiosciences); L243 was used for detection of HLA-DR molecules (17 (link)) and HC10 for labelling of β₂m-free HLA heavy chains (18 (link), 19 (link)).
The following antibodies were used for Western blot analysis: mouse anti–Melan-A/MART-1 (Zytomed), mouse anti-Tyrosinase and anti-MITF (Santa Cruz Biotechnology), rabbit anti-DCT/TRP2 (kindly provided by V. Hearing, National Cancer Institute, NIH, Bethesda); mouse anti-STAT1, rabbit anti-phospho(p)STAT1, rabbit anti-JAK1, rabbit anti-GAPDH (Cell Signaling Technology); rabbit anti-IRF1 and mouse anti-β2m (Santa Cruz Biotechnology); rabbit anti-β2m (Sigma); mouse anti-TAP1 (NOB-1) and mouse anti-tapasin (TO-3; ref. 20 (link)); mouse mAb HC10 (18 (link), 19 (link)).

Sucker A., Zhao F., Real B., Heeke C., Bielefeld N., Maβen S., Horn S., Moll I., Maltaner R., Horn P.A., Schilling B., Sabbatino F., Lennerz V., Kloor M., Ferrone S., Schadendorf D., Falk C.S., Griewank K, & Paschen A. (2014). Genetic Evolution of T-cell Resistance in the Course of Melanoma Progression. Clinical cancer research : an official journal of the American Association for Cancer Research, 20(24), 6593-6604.

+ Open protocol

+ Expand

Quantitative Analysis of Apoptosis Markers

Check if the same lab product or an alternative is used in the 5 most similar protocols

PBS, 1MT, GA, G + M, and GM (1MT: 7 μg/ml, GA: 200 μg/ml) were added, and the mixture was incubated for 48 h. Cell lysates were collected for Western blot. After electrophoresis, the separated proteins were transferred onto a polyvinylidene difluoride membrane; the membrane was incubated in diluted primary antibody at 4°C overnight, including 1:200 mouse anti-tyrosinase (Santa Cruz Biotechnology, CA), PCNA (1:1000; catalog no.13110), and cleaved caspase-3 (1: 500; catalog no.13110). After incubation with the second antibody HRP-conjugated affinity Goat anti-rabbit/mouse IgG (H + L), the results were detected by enhanced chemiluminescence Western blotting kit. A chemiluminescence imaging system was used to quantify the intensity of the strip.

Liu H., Gao H., Chen C., Jia W., Xu D, & Jiang G. (2022). IDO Inhibitor and Gallic Acid Cross-Linked Small Molecule Drug Synergistic Treatment of Melanoma. Frontiers in Oncology, 12, 904229.

+ Open protocol

+ Expand

Protein Expression Analysis in Cultured Cells

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cultured cells were collected, rinsed, and subjected to NE-PER^® Nuclear and Cytoplasmic Extraction Reagents (Thermo Fisher Scientific) as previously described [32 (link),33 (link)]. After protein quantification by Bradford assay, proteins were separated by 12% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred onto a polyvinylidene fluoride (PVDF) membrane. Primary antibodies used in this study were as follows: rabbit anti-microphthalmia-associated transcription factor (MITF; Abcam, Cambridge, UK), goat anti-lamin B, mouse anti-tyrosinase (TYR), mouse anti-tyrosinase-related protein 1 (TYRP1), mouse anti-TYRP2, and mouse anti-β-actin (Santa Cruz Biotechnology, Inc., Dallas, TX, USA). Secondary antibodies used were anti-mouse, anti-rabbit, or anti-goat IgG conjugated to horseradish peroxidase (Santa Cruz Biotechnology, Inc.). Protein bands were visualized using the SuperSignal^® West Pico Chemiluminescent Substrate kit (Thermo Fisher Scientific) and ImageQuant LAS 4000 mini (GE Healthcare Life Sciences, Little Chalfont, UK). Digital images were analyzed for densitometry using Image Studio^TM Lite software (LI-COR Corp., Lincoln, NE, USA).

Oh J., Kim J., Jang J.H., Lee S., Park C.M., Kim W.K, & Kim J.S. (2018). Novel (1E,3E,5E)-1,6-bis(Substituted phenyl)hexa-1,3,5-triene Analogs Inhibit Melanogenesis in B16F10 Cells and Zebrafish. International Journal of Molecular Sciences, 19(4), 1067.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!