|Application ||WB, IHC-P, IF, FC, E|
|Calculated MW||60393 Da|
|Antigen Region||486-513 aa|
|Other Names||Tyrosinase, LB24-AB, Monophenol monooxygenase, SK29-AB, Tumor rejection antigen AB, TYR|
|Target/Specificity||This Tyrosinase antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 486-513 amino acids from the C-terminal region of human Tyrosinase.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Tyrosinase Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone.|
|Cellular Location||Melanosome membrane; Single-pass type I membrane protein|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
TYR catalyzes the first 2 steps, and at least 1 subsequent step, in the conversion of tyrosine to melanin. The protein has both tyrosine hydroxylase and dopa oxidase catalytic activities, and requires copper for function. Mutations in this protein result in oculocutaneous albinism, and nonpathologic polymorphisms result in skin pigmentation variation.
Ostankovitch,M. J. Immunol. 182 (8), 4830-4835 (2009)
Chintamaneni,C.D. Proc. Natl. Acad. Sci. U.S.A. 88 (12), 5272-5276 (1991)
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