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
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About This Item
UNSPSC代码:
12352203
NACRES:
NA.41
推荐产品
生物来源
mouse
质量水平
偶联物
unconjugated
抗体形式
purified from hybridoma cell culture
抗体产品类型
primary antibodies
克隆
MLN128, monoclonal
表单
buffered aqueous solution
分子量
antigen ~110 kDa (additional bands may be observed)
种属反应性
human
包装
antibody small pack of 25 μL
浓度
~2.0 mg/mL
技术
immunocytochemistry: suitable
indirect ELISA: suitable
western blot: 4-8 μg/mL using membrane fraction of HEK-293T expressing human mucolipin-1
UniProt登记号
运输
dry ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... MCOLN1(57192)
一般描述
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.
应用
Monoclonal Anti-Mucolipin-1 has been used in:
- enzyme linked immunosorbent assay (ELISA)
- immunoblotting
- immunocytochemistry.
生化/生理作用
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.
外形
0.01M 磷酸缓冲盐溶液，pH 7.4，含 15mM 叠氮化钠。
免责声明
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.
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产品编号
说明
价格
储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Autophagic dysfunction in mucolipidosis type IV patients
Vergarajauregui S, et al.
Human Molecular Genetics, 17(17), 2723-2737 (2008)
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)
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
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
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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