M8072
Anti-Mucolipin-1 antibody, Mouse monoclonal
clone MLN128, purified from hybridoma cell culture
别名:
Anti-MCOLN1, Anti-ML4, Anti-MLIV, Anti-MST080, Anti-MSTP080, Anti-Mucolipidin, Anti-TRP-ML1, Anti-TRPM-L1, Anti-TRPML1, Anti-Transient receptor potential cation channel, mucolipin subfamily, member 1
产品名称
Anti-Mucolipin-1 antibody, Mouse monoclonal, clone MLN128, purified from hybridoma cell culture
biological source
mouse
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
MLN128, monoclonal
form
buffered aqueous solution
mol wt
antigen ~110 kDa (additional bands may be observed)
species reactivity
human
packaging
antibody small pack of 25 μL
concentration
~2.0 mg/mL
technique(s)
immunocytochemistry: suitable
indirect ELISA: suitable
western blot: 4-8 μg/mL using membrane fraction of HEK-293T expressing human mucolipin-1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MCOLN1(57192)
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Application
Monoclonal Anti-Mucolipin-1 has been used in:
- enzyme linked immunosorbent assay (ELISA)
- immunoblotting
- immunocytochemistry.
Biochem/physiol Actions
Mucolipin-1 (MCOLN1) is involved in the regulation of lysosomal trafficking. It aids in the transport of Ca2+ into the cytosol from the lumen, in response to the changing levels of phosphatidylinositol-3, 5-bisphosphate. Mutations in the gene encoding MCOLN1 have been shown to be associated with mucolipidosis type IV.
Mutations in the MCOLN1 gene is implicated in Mucolipidosis type IV (MLIV) is an autosomal recessive, neurodegenerative disorder. Rather, MLIV pathophysiology has been linked to deficiency in membrane trafficking, and organelle dynamics in the late endocytic pathway. Specifically, MLIV cells have been shown to accumulate autophagosomes, due to increased de novo autophagosome formation and due to delayed fusion of autophagosomes with late endosomes/lysosomes.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Monoclonal Anti-Mucolipin-1 (mouse IgG1 isotype) is derived from the hybridoma MLN128 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a recombinant fusion protein corresponding to amino acid 1.Mucolipin-1 is also termed TRP-ML1, MLN1, ML1 mucolipidin. MLN1 shares significant sequence homology with the TRP superfamily of cation channels.
Mucolipin-1 (MCOLN1) is a member of transient receptor potential (TRP) protein family. It is a cation channel present on endosomes and lysosomes.
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存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Zhenxing Liu et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 92(4), 279-286 (2014-06-25)
Lysosomotropic amines cause serious side effects such as cytoplasmic vacuolation and cell death. TRPML1 (also known as mucolipin1), a member of the transient receptor potential (TRP) protein family, may regulate fusion/fission of vesicles along the endocytic pathway and some aspects
Posttranslational cleavage and adaptor protein complex-dependent trafficking of mucolipin-1
Miedel MT, et al.
The Journal of Biological Chemistry, 281(18), 12751-12759 (2006)
Autophagic dysfunction in mucolipidosis type IV patients
Vergarajauregui S, et al.
Human Molecular Genetics, 17(17), 2723-2737 (2008)
Helen Waller-Evans et al.
Biochemical Society transactions, 43(3), 442-446 (2015-05-27)
TRPML1 is a ubiquitously expressed cation channel found on lysosomes and late endosomes. Mutations in TRPML1 cause mucolipidosis type IV and it has been implicated in Alzheimer's disease and HIV. However, the mechanisms by which TRPML1 activity is regulated are not
Wuyang Wang et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(11), E1373-E1381 (2015-03-04)
Upon nutrient starvation, autophagy digests unwanted cellular components to generate catabolites that are required for housekeeping biosynthesis processes. A complete execution of autophagy demands an enhancement in lysosome function and biogenesis to match the increase in autophagosome formation. Here, we
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