biological source
mouse
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
western blot: 1 μg/mL
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MLPH(79083)
General description
MLPH (melanophilin) belongs to the family of synaptotagmin-like proteins and is a Ras-related protein Rab27A effector. It is a component of a tripartite complex, which also includes myosin-Va and Rab27A. The protein contains a Slp homology domain (SHD) in its N-terminal and a myosin Va-binding region in its C-terminal. Also, amino acids 400-590 in the C-terminal, directly bind to actin. MLPH contains two α-helices (SHD1 and SHD2), which are conserved in nature. These two regions are intervened by two zinc finger motifs. The MLPH gene is localized to human chromosome 2q37.3.
Immunogen
MLPH (NP_077006.1, 1 a.a. ~ 600 a.a) full-length human protein.
Sequence
MGKKLDLSKLTDEEAQHVLEVVQRDFDLRRKEEERLEALKGKIKKESSKRELLSDTAHLNETHCARCLQPYQLLVNSKRQCLECGLFTCKSCGRVHPEEQGWICDPCHLARVVKIGSLEWYYEHVKARFKRFGSAKVIRSLHGRLQGGAGPELISEERSGDSDQTDEDGEPGSEAQAQAQPFGSKKKRLLSVHDFDFEGDSDDSTQPQGHSLHLSSVPEARDSPQSLTDESCSEKAAPHKAEGLEEADTGASGCHSHPEEQPTSISPSRHGALAELCPPGGSHRMALGTAAALGSNVIRNEQLPLQYLADVDTSDEESIRAHVMASHHSKRRGRASSESQIFELNKHISAVECLLTYLENTVVPPLAKGLGAGVRTEADVEEEALRRKLEELTSNVSDQETSSEEEEAKDEKAEPNRDKSVGPLPQADPEVGTAAHQTNRQEKSPQDPGDPVQYNRTTDEELSELEDRVAVTASEVQQAESEVSDIESRIAALRAAGLTVKPSGKPRRKSNLPIFLPRVAGKLGKRPEDPNADPSSEAKAMAVPYLLRRKFSNSLKSQGKDDDSFDRKSVYRGSLTQRNPNARKGMASHTFAKPVVAHQS
Sequence
MGKKLDLSKLTDEEAQHVLEVVQRDFDLRRKEEERLEALKGKIKKESSKRELLSDTAHLNETHCARCLQPYQLLVNSKRQCLECGLFTCKSCGRVHPEEQGWICDPCHLARVVKIGSLEWYYEHVKARFKRFGSAKVIRSLHGRLQGGAGPELISEERSGDSDQTDEDGEPGSEAQAQAQPFGSKKKRLLSVHDFDFEGDSDDSTQPQGHSLHLSSVPEARDSPQSLTDESCSEKAAPHKAEGLEEADTGASGCHSHPEEQPTSISPSRHGALAELCPPGGSHRMALGTAAALGSNVIRNEQLPLQYLADVDTSDEESIRAHVMASHHSKRRGRASSESQIFELNKHISAVECLLTYLENTVVPPLAKGLGAGVRTEADVEEEALRRKLEELTSNVSDQETSSEEEEAKDEKAEPNRDKSVGPLPQADPEVGTAAHQTNRQEKSPQDPGDPVQYNRTTDEELSELEDRVAVTASEVQQAESEVSDIESRIAALRAAGLTVKPSGKPRRKSNLPIFLPRVAGKLGKRPEDPNADPSSEAKAMAVPYLLRRKFSNSLKSQGKDDDSFDRKSVYRGSLTQRNPNARKGMASHTFAKPVVAHQS
Biochem/physiol Actions
MLPH (melanophilin) acts as a receptor for myosin-Va in melanocytes. It is essential for the transport of melanosomes from perinuclear region to the actin-rich periphery of melanocytes. Thus, normal melanosome distribution is dependent on this protein. MLPH acts as a linker between myosin-Va and Rab27A, and facilitates the binding of melanosomes with actin network. This protein might also be a key player in the instantaneous skin tanning in humans, when exposed to sun. Mutation in MLPH gene leads to mice with light coat color, called leaden mice. It is the outcome of aberrant melanosome transportation. Homozygous missense mutation occurring in the Slp homology domain of this protein is associated with Griscelli syndrome type III (GSIII). MLPH is under-expressed in GSIII melanocytes and such patients are characterized by silvery-gray hair and hypopigmentation of the skin.
Physical form
Solution in phosphate buffered saline, pH 7.4
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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Cellular and clinical report of new Griscelli syndrome type III cases.
Westbroek W, et al.
Pigment Cell & Melanoma Research, 25(1), 47-56 (2011)
Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin.
Fukuda M, et al.
Journal of Cell Science, 117(4), 583-591 (2004)
Thierry Passeron et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 18(9), 989-991 (2004-04-03)
Melanosomes are melanin-containing organelles that belong to a recently individualized group of lysosome-related organelles. Recently, numerous reports have dissected the molecular mechanisms that control melanosome transport, but nothing was known about the possible regulation of melanosome distribution by exogenous physiological
Mitsunori Fukuda
The Journal of biological chemistry, 277(42), 40118-40124 (2002-08-22)
The N-terminal synaptotagmin-like protein (Slp) homology domain (SHD) of the Slp and Slac2 families has recently been identified as a specific Rab27A-binding domain (Kuroda, T. S., Fukuda, M., Ariga, H., and Mikoshiba, K. (2002) J. Biol. Chem. 277, 9212-9218; Fukuda
Mitsunori Fukuda et al.
The Journal of biological chemistry, 277(45), 43096-43103 (2002-09-11)
Slac2-a (synaptotagmin-like protein (Slp) homologue lacking C2 domains-a)/melanophilin is a melanosome-associated protein that links Rab27A on melanosomes with myosin Va, an actin-based motor protein, and formation of the tripartite protein complex (Rab27A.Slac2-a.myosin Va) has been suggested to regulate melanosome transport
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