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Merck
모든 사진(1)

Key Documents

M8072

Sigma-Aldrich

Anti-Mucolipin-1 antibody, Mouse monoclonal

clone MLN128, purified from hybridoma cell culture

동의어(들):

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 코드:
12352203
NACRES:
NA.41

생물학적 소스

mouse

결합

unconjugated

항체 형태

purified from hybridoma cell culture

항체 생산 유형

primary antibodies

클론

MLN128, monoclonal

형태

buffered aqueous solution

분자량

antigen ~110 kDa (additional bands may be observed)

종 반응성

human

포장

antibody small pack of 25 μL

농도

~2.0 mg/mL

기술

immunocytochemistry: suitable
indirect ELISA: suitable
western blot: 4-8 μg/mL using membrane fraction of HEK-293T expressing human mucolipin-1

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... MCOLN1(57192)

일반 설명

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.

애플리케이션

Monoclonal Anti-Mucolipin-1 has been used in:
  • enzyme linked immunosorbent assay (ELISA)
  • immunoblotting
  • immunocytochemistry.

생화학적/생리학적 작용

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.

물리적 형태

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

면책조항

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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문서 라이브러리 방문

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)
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
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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