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SAB1400695

Sigma-Aldrich

Anti-MLPH antibody produced in mouse

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-FLJ12145, Anti-MELPH, Anti-MGC2771, Anti-SLAC2-A, Anti-Slac-2a, Anti-exophilin-3, Anti-l(1)-3Rk, Anti-l1Rk3, Anti-ln

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

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

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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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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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)
Cellular and clinical report of new Griscelli syndrome type III cases.
Westbroek W, et al.
Pigment Cell & Melanoma Research, 25(1), 47-56 (2011)
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 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
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

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