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L0419

Sigma-Aldrich

Anti-LAMP1−Cy3™ antibody produced in rabbit

1-2 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-CD107a, Anti-LAMPA, Anti-LGP120, Anti-Lysosomal-associated membrane protein 1

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About This Item

MDL number:
MFCD01864611
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

CY3 conjugate

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human, rat

concentration

1-2 mg/mL

technique(s)

direct immunofluorescence: 1-2 μg/mL using human HeLa cells, rat NRK cells and mouse 3T3 cells

UniProt accession no.

P11279

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

human ... LAMP1(3916)
mouse ... Lamp1(16783)
rat ... Lamp1(25328)

General description

Lysosomal-associated membrane protein 1 (LAMP1), also termed LGP120, is a heavily glycosylated lysosomal membrane protein with a molecular mass of 120 kDa. It consists of a 40 kDa core polypeptide with O-linked and 18 asparagine-linked oligosaccharide side chains. LAMP1 protein contains a leader sequence, a large intralumenal region consisting of 2 homologous domains separated by a hinge region rich in proline and serine, a 24-amino acid transmembrane region, and a short cytoplasmic tail containing the lysosomal membrane targeting signal.
The gene LAMP1 (lysosomal-associated membrane protein 1) encodes a type I transmembrane protein that has a short cytoplasmic tail containing a lysosome-targeting signal of GYQTI(382)-COOH. The gene is mapped to human chromosome 13q34.

Application

Anti-LAMP1-Cy3™ antibody produced in rabbit has been used in immunofluorescence.

Biochem/physiol Actions

The gene LAMP1 (lysosomal associated membrane protein 1) encodes a membrane glycoprotein that functions as an intracellular receptor. It is found to be expressed in the cytoplasm of several types of tumor cells and may be involved in tumor invasion. Lamp1 is crucial for perforin trafficking to the lytic granules and motility of these lytic granules. Its knockdown leads to inhibition of cytotoxicity of human natural killer cells.

Physical form

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

Legal Information

Cy3 is a trademark of Cytiva

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.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Expression of the lysosomal-associated membrane protein-1 (LAMP-1) in astrocytomas
Jensen SS, et al.
International Journal of Clinical and Experimental Pathology, 6(7), 1294-1294 (2013)
Shou-Bin Tang et al.
Reproduction (Cambridge, England) (2019-03-19)
It is demonstrated that repeated superovulation has deleterious effects on mouse ovaries and cumulus cells. However, little is known about the effects of repeated superovulation on early embryos. Epigenetic reprogramming is an important event in early embryonic development, and could
Three-dimensional invasion of macrophages is mediated by cysteine cathepsins in protrusive podosomes.
Jevnikar Z, et.al.
European Journal of Immunology, 42, 3429-3441 (2012)
Zala Jevnikar et al.
European journal of immunology, 42(12), 3429-3441 (2012-09-29)
Podosomes, specialized actin-rich structures in macrophages (Mfs), degrade the extra-cellular matrix (ECM) and are involved in cell migration. On two-dimensional (2D) surfaces Mfs form spot-like podosomes at the ventral cell surface that develop into protrusive structures in a three-dimensional (3D)
C Banfi et al.
Communications biology, 4(1), 1109-1109 (2021-09-23)
The research into the pathophysiology of atherosclerosis has considerably increased our understanding of the disease complexity, but still many questions remain unanswered, both mechanistically and pharmacologically. Here, we provided evidence that the pro-oxidant enzyme Prenylcysteine Oxidase 1 (PCYOX1), in the
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