Recombinant Human LAMP1 Protein

Name: Recombinant Human LAMP1 Protein
Brand: Beta LifeScience
SKU: BLA-5253P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P11279
Synonym	CD107 antigen like family member A CD107 antigen-like family member A CD107a CD107a antigen LAMP 1 LAMP-1 LAMP1 LAMP1_HUMAN LAMPA LGP120 lgpA Lysosomal membrane glycoprotein 120KD Lysosomal Associated Membrane Protein 1 Lysosome associated membrane glycoprotein 1 Lysosome-associated membrane glycoprotein 1 Lysosome-associated membrane protein 1 OTTHUMP00000040663
Description	Recombinant Human LAMP1 Protein was expressed in HEK293. It is a Protein fragment
Source	HEK293
AA Sequence	AMFMVKNGNGTACIMANFSAAFSVNYDTKSGPKNMTFDLPSDATVVLNRS SCGKENTSDPSLVIAFGRGHTLTLNFTRNATRYSVQLMSFVYNLSDTHLF PNASSKEIKTVESITDIRADIDKKYRCVSGTQVHMNNVTVTLHDATIQAY LSNSSFSRGETRCEQDRPSPTTAPPAPPSPSPSPVPKSPSVDKYNVSGTN GTCLLASMGLQLNLTYERKDNTTVTRLLNINPNKTSASGSCGAHLVTLEL HSEGTTVLLFQFGMNASSSRFFLQGIQLNTILPDARDPAFKAANGSLRAL QATVGNSYKCNAEEHVRVTKAFSVNIFKVWVQAFKVEGGQFGSVEECLLD ENSMVDHHHHHH
Molecular Weight	39 kDa including tags
Purity	Greater than 95% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilised
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. The lyo

Target Details

Target Function	Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, autophagy, and cholesterol homeostasis. Plays also an important role in NK-cells cytotoxicity. Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule. In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content. Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.; (Microbial infection) Acts as a receptor for Lassa virus glycoprotein. Promotes also fusion of the virus with host membrane in less acidic endosomes.; (Microbial infection) Supports the FURIN-mediated cleavage of mumps virus fusion protein F by interacting with both FURIN and the unprocessed form but not the processed form of the viral protein F.
Subcellular Location	Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. Cytolytic granule membrane; Single-pass type I membrane protein.
Protein Families	LAMP family
Database References	HGNC: 6499 OMIM: 153330 KEGG: hsa:3916 STRING: 9606.ENSP00000333298 UniGene: Hs.494419

Gene Functions References

LIN28A inhibits lysosomeassociated membrane glycoprotein 1 protein expression in embryonic stem and bladder cancer cells. PMID: 29749495
A novel data on LAMP-1 overexpression in high grade glioma are presented suggesting involvement of this gene and protein in cell adhesion and tumor progression. PMID: 29920782
LAMP1 is involved in the TNM stages and histological differentiation of the esophageal squamous cell carcinoma PMID: 28687162
LAMP1 has a role in fratricide amongst T cell receptor transgenic CD8+ T cells directed against tumor-associated antigens PMID: 27447745
Impaired autophagic pathways were further shown by analyzing late autophagic vesicles; immunostaining with lysosome-associated membrane protein 1 (LAMP-1) antibody revealed enlarged and annular LAMP-1-positive organelles in AMD retinal pigment epithelium (RPE)as opposed to smaller discrete puncta observed in normal RPE PMID: 28055007
The authors show here that human LAMP1 and LAMP2 bind cholesterol in a manner that buries the cholesterol 3beta-hydroxyl group; they also bind tightly to NPC1 and NPC2 proteins that export cholesterol from lysosomes. PMID: 27664420
downregulation of FUT1, which leads to the perinuclear localization of LAMP-1 and 2, is correlated with increased rate of autophagic flux by decreasing mTOR signaling and increasing autolysosome formation. PMID: 27560716
the assembly modes of LAMP-1 and LAMP-2 are different, which may underlie their distinct functions PMID: 27663661
Overexpression of LAMP1 was observed in prostate cancer (PCa) and castration-resistant prostate cancer clinical specimens. Moreover, downstream pathways were identified using si-LAMP1-transfected cells. The discovery of tumor-suppressive miR320a-mediated pathways may provide important insights into the potential mechanisms of PCa metastasis. PMID: 27212625
The data implied that high LAMP1 expression is associated with unfavourable prognosis in laryngeal squamous cell carcinoma patients, and LAMP1 may be identified as a novel prognostic biomarker PMID: 27788920
The data support a viral entry mechanism dependent on binding to the lysosome-resident receptor LAMP1 and further dissociation of the membrane-distal GP1 subunits. PMID: 26849049
A unique triad of histidines of Lassa Virus GP1 forms a binding site for host LAMP1. PMID: 25972533
The LAMP-1 had preferential localization in the high density secondary lysosomes where endogenous human LAMP-1 was enriched. In contrast, a major portion of I382L was located in a low density fraction. PMID: 24695761
Downregulation of miR-184 was consistent with significantly lower levels of LAMP-1 PMID: 25251993
Synergistic defects of different molecules in the cytotoxic pathway lead to clinical familial hemophagocytic lymphohistiocytosis. PMID: 24916509
Caveolin-1 associated adenovirus entry into human corneal cells. PMID: 24147000
study has shown that Lassa virus entry requires a pH-regulated engagement of alpha-DG and LAMP1 both of which need to be glycosylated PMID: 24970085
in TB pleurisy regulatory T lymphocytes effectively inhibit CD107a expression PMID: 24134738
LAMP-1 and LAMP-2 could be used as additional markers with which to assess enzyme replacement therapy effectiveness in Fabry disease. PMID: 24334114
LAMP-1/GFAP showed pronounced co-expression and LAMP-1/CD133 was co-expressed as well in astrocytomas suggesting that tumor cells including the proposed tumor stem cells contain lysosomes. PMID: 23826410
CD107a/LAMP-1 has a role in the protection of NK cells from degranulation-associated suicide PMID: 23847195
Data indicate that monoclonal antibodies specific to CD107a (LAMP-1) or CD107b (LAMP-2) enhanced LPS-induced IL-8 secretion of THP-1 cells. PMID: 23603048
LAMP1 is required for efficient perforin delivery to lytic granules and NK-cell cytotoxicity. PMID: 23632890
Simultaneous expression of LAMP1 and EGFR correlates with the ovarian neoplasm grading. PMID: 23172893
LAMP proteins retain TAPL on the limiting membrane of endosomes and prevent its sorting to intraluminal vesicles. PMID: 22641697
Data indicate that lysosomally targeted cameleon Ca2+ probe LAMP1-YCaM accurately and sensitively responds to both global and lysosome-specific Ca2+ signals. PMID: 23098255
Report expression of NKG2D and CD107 in CD8(+) effector memory lymphocytes in Churg-Strauss syndrome. PMID: 22640649
nucleolin and LAMP-1 have a role in promoting infection of human monocytes by Francisella tularensis PMID: 21152024
Human full-length amelogenin increases the proliferation of mesenchymal stem cells by interaction with LAMP1 through the MAPK-ERK signaling pathway. PMID: 20967466
Immunohistochemistry studies showed EGBs to exhibit pronounced reactivity to antibodies against lysosome-associated membrane proteins (LAMP)-1 and LAMP-2, and the lysosomal enzyme cathepsin D. PMID: 20926008
review of structure, function, cell and tissue distribution, intracellular trafficking PMID: 12144129
This study identifies two cDNA clones that code for heart extracellular matrix protein, hLAMP-1. Immunohistochemical studies indicate that the myocardial layer of the heart produces hLAMP-1. PMID: 15052658
Using human leukemia and lymphoma cell lines, we observed a close correlation between CD107a surface expression and target cell lysis, indicating that NK cell cytotoxicity can be assessed by this method. PMID: 15744340
Data identify CD13, CD107a, and CD164 as novel basophil-activation antigens. PMID: 15916720
Novel evidence for differential expression of HBGA and LAMPs in proliferative and involutive phases of immunohistochemistry is presented. PMID: 16570122
expression in keratinocytes cultured at different cell densities in order to induce differentiation PMID: 16710742
Enhanced expression of lysosome-associated membrane protein-1 in melanoma may promote invasion by influencing both adhesion to extracellular matrix and perhaps also binding to endothelial cells. PMID: 16718270
CD107a surface expression has a role in Munc13-4 defect in familial hemophagocytic lymphohistiocytosis PMID: 16778144
LAMP-1 and DC-LAMP antigen chimeras follow different trafficking pathways, induce distinct modulatory immune responses, and are able to present cryptic epitopes. PMID: 16887987
LAMP-1 and LAMP-2 may have roles in accidental involution of the thymic gland PMID: 17048695
Data show that cells lacking either LAMP-1 or LAMP-2 alone formed phagosomes that gradually acquired microbicidal activity and curtailed bacterial growth, but LAMP-1 and LAMP-2 double-deficient cells failed to kill engulfed Neisseria gonorrhoeae. PMID: 17506821
CD107a expression may be a sensitive marker for the cytotoxic activity determination PMID: 18835598
Despite its abundance, LAMP-1 is not essential, but LAMP-2 may be partially important for the Salmonella-containing vacuolar membrane. PMID: 18958159
the activation-induced degranulation of Fas ligand has distinct requirements and involves different mechanisms than those of the granule markers CD63 and CD107a/Lamp-1 PMID: 19079288
Most Hassal's corpuscules in thymoma were negative for LAMPs, but positive in normal thymus. Both lymphocytes and epithelial cells in pathological thymus showed higher intensity for LAMP-2 compared with LAMP-1. PMID: 19343823
Data show that The cell surface expression levels of (ICAM)-2 and -3 on the apoptotic cells were markedly lower, while those of calnexin, calreticulin, and (LAMP)-1 and -2 were significantly higher compared to non-apoptotic cells. PMID: 19524015

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