Recombinant Human Lysosome-Associated Membrane Glycoprotein 2 (LAMP2) Protein (His), Active

Name: Recombinant Human Lysosome-Associated Membrane Glycoprotein 2 (LAMP2) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05694P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Lysosome-Associated Membrane Glycoprotein 2 (LAMP2) Protein (His), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined by its ability to bind Human LGALS-3 in functional ELISA is less than 30 ug/ml.
Uniprotkb	P13473
Target Symbol	LAMP2
Synonyms	LAMP2; Lysosome-associated membrane glycoprotein 2; LAMP-2; Lysosome-associated membrane protein 2; CD107 antigen-like family member B; LGP-96; CD antigen CD107b
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-6His
Complete Sequence	LELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNF
Expression Range	29-375aa
Protein Length	Partial
Mol. Weight	33.94 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 20 mM PB, 150 mM NaCl, pH 7.2
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation. Plays a role in lysosomal protein degradation in response to starvation. Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes. Required for normal degradation of the contents of autophagosomes. Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens.; Modulates chaperone-mediated autophagy. Decreases presentation of endogenous antigens by MHCII. Does not play a role in the presentation of exogenous and membrane-derived antigens by MHCII.; (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. Cytoplasmic vesicle, autophagosome membrane. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane.
Protein Families	LAMP family
Database References	HGNC: 6501 OMIM: 300257 KEGG: hsa:3920 UniGene: PMID: 28729403 Results demonstrated that LAMP2 expression levels correlated with tumor histological differentiation and TNM stages. PMID: 28453465 Since effective regimens are readily available timely psychiatric evaluation is warranted in all newly diagnosed subjects with LAMP2 mutations, regardless of whether they show the typical Danon disease medical (cardiac) symptoms or not. PMID: 28627787 identified LAMP-2 as an endocytic receptor on monocyte-derived dendritic cells (MoDC) that routes cargo into unusual Ag processing pathways, which reduces surface expression of Ag-derived peptides while selectively enriching Ag within immunogenic exosome; this novel pathway has implications for the initiation of immune responses both locally and at distant sites PMID: 28607115 The results provide a new insight that LAMP-2 contributes to the ROS clearance and cell death induced by Zn(2+) treatment, which would help us to get a better understanding of Zn(2+)-induced toxicity in respiratory system. PMID: 28483530 overexpression assists neuroendocrine differentiation of prostate cancer cells induced by serum deprivation and facilitates autophagy activity PMID: 27627761 Genetic analysis identified 2 novel LAMP2 gene mutations. In Family A, a G-A transition (c.962G > A) leading to a nonsense mutation at codon 321 (p.Trp321Ter), and in Family B, a one-nucleotide insertion (c.973insC) leading to a full frame-shift (p.Pro324+24X) was detected in exon 8 of the LAMP2 gene. PMID: 27179547 intracellular Salmonella recruit the host proteins LAMP-2A and Hsc73, key components of the host protein turnover pathway known as chaperone-mediated autophagy involved in transport of cytosolic proteins to the lysosome for degradation. PMID: 27932462 3 novel nonsense mutations (p.Q240X, p.S250X, and p.G22X) were found in LAMP2 associated with early onset Danon disease with hypertrophic cardiomyopathy. LAMP2 expression was absent in both cardiac and skeletal muscle samples of the first proband and severely decreased LAMP2 expression in the skeletal muscle samples of the second proband. PMID: 27460667 Collectively, the present study shows that impaired Lamp2a expression in hepatocellular carcinoma contributes to tumor cell viability and promotes tumor growth and recurrence. PMID: 27840904 Increased expression of LAMP2 has been observed in peripheral blood mononuclear cells of coronary artery disease patients compared to the control group. PMID: 27923262 Knockdown of LAMP2A, a CMA-related protein, and TSG101, an mA-related protein, significantly but only partially decreased the punctate accumulation of GAPDH-HT in AD293 cells and primary cultured rat cortical neurons. PMID: 27377049 miR-487b-5p regulates temozolomide resistance of lung cancer cells through LAMP2-mediated autophagy. PMID: 27097129 Up-regulation of LAMP2 is associated with carcinogenesis and progression of Salivary Adenoid Cystic Carcinoma. PMID: 26350055 In our study of the EOG in Danon disease, we show for the first time to our knowledge that a LAMP2 mutation may cause a primary retinal pigment epitheliopathy. PMID: 26398689 LAMP-2C serves as a natural inhibitor of chaperone-mediated autophagy that can selectively skew MHCII presentation of cytoplasmic antigens PMID: 26856698 In the early stages of Parkinson's disease, with LAMP2A selectively reduced in association with increased alpha-synuclein, and decreased levels of heat shock cognate protein 70. PMID: 25594542 This study showed that LAMP2 upregulation occurs in vitro and in vivo in neoplastic cells. PMID: 26658462 Down-regulation of LAMP2A expression could inhibit cell proliferation in multiple myeloma cells PMID: 25940285 Data show thart lysosome-associated membrane protein type 2a (LAMP-2A) forms a coiled coil helix trimer in n-dodecylphosphocholine micelle, and protein substrates interact with its cytosolic tail. PMID: 25342746 LAMP2 has a role in differentiation of primary biliary cirrhosis PMID: 24007661 Patient B harbored a frame-shift deletion mutation in exon 3 (c.396delA) leading to a truncated LAMP2 protein PMID: 24691104 down-regulation of LAMP2A could reduce the resistance of breast cancer cells to paclitaxel PMID: 24721399 LAMP2 is investigated as a marker of Epstein-Barr virus-mediated B lymphocyte transformation in lysosomal storage diseases. PMID: 24068328 Autoantibodies to hLAMP-2 that bind native glomerular but not neutrophil hLAMP-2 are found in patients with ANCA-negative pauci-immune focal necrotizing glomerulonephritis. PMID: 24203998 These data support a positive relationship between anti-LAMP-2 antibody and cutaneous vasculitis. PMID: 23704322 Decreased levels of the chaperone-mediated autophagy proteins LAMP-2A and hsc70 (CMA) in Parkinson's disease brain samples suggests compromised alpha-synuclein degradation by CMA and may underpin the Lewy body pathology. PMID: 23492776 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 expression of LAMP2A was observed in breast tumor tissues of all patients under investigation, suggesting a survival mechanism via chaperone-mediated autophagy and LAMP2A. PMID: 22874552 Studies suggest that Hsc70 and lysosome-associated protein 2A (LAMP-2A) through chaperone-mediated autophagy (CMA) play a role in the clearance of Htt and suggest a novel strategy to target the degradation of mutant huntingtin (Htt). PMID: 23071649 There is a progressive, age-related decrease of LAMP-2 gene expression in the peripheral leukocytes of healthy subjects, indicating a trend of decreasing autophagy activities with aging. PMID: 22732524 variants within LAMP-2 gene promoter may be linked to Parkinson disease. PMID: 22867958 findings indicated that patients with Danon disease caused by mutations in exon 1 - 8 manifested as a typically severe phenotype, while patients with mutations in exon 9 of the LAMP2B isoform presented with a relatively benign phenotype PMID: 22541782 A novel LAMP2 mutation (c.940delG) in Danon disease patients, which results in a putatively truncated protein. PMID: 22365987 decreased LAMP-2 gene expression and increased LC3 gene expression may contribute to the pathogenesis of sporadic Parkinson's disease PMID: 21514572 Peripheral leukocyte LAMP-2 expression is significantly inceased in coronary artery disease. PMID: 21462217 intrafamilial phenotypic variability in Danon disease is related to a novel LAMP-2 mutation PMID: 21161685 gene deficient B cells exhibit altered MHC class II presentation of exogenous antigens PMID: 20518820 Lysosome-associated membrane protein (LAMP2) cardiomyopathy is an X-linked and highly progressive myocardial storage disorder associated with diminished survival, which clinically resembles sarcomeric hypertrophic cardiomyopathy. PMID: 20920663 The LAMP2 microdeletion mechanism appears to involve 1 Alu-mediated unequal recombination and 2 chromosomal breakage points involving TA-rich repeat sequences. PMID: 20173215 Danon disease is caused by deficiency of lysosome-associated membrane protein-2 (LAMP-2). PMID: 20513107 Data show that the BCG phagosome is relatively depleted in LAMP-2, NPC1, flotillin-1, vATPase, and syntaxin 3. PMID: 19815536 This studu showed decreased LAMP2 expression in the sketal muscle in female patient with Danon disease. PMID: 14561493 The glycogen-storage cardiomyopathy produced by LAMP2 or PRKAG2 mutations resembles hypertrophic cardiomyopathy but is distinguished by electrophysiological abnormalities PMID: 15673802 role for the lysosomal Lamp-2a-hsc70 complex in promoting immunological recognition and antigen presentation PMID: 15894275 LAMP2 mutations may account for significant proportion of cases of hypertrophic cardiomyopathy children, especially when skeletal myopathy and/or Wolff-Parkinson-White syndrome is present. Danon disease may be underrecognized in pediatric cardiology. PMID: 16144992 Our report further expands the phenotype of Danon disease by describing retinopathy in 3 cases. A thorough clinical examination, including ophthalmic investigation, is needed in all cases of Danon disease. PMID: 17296900 The biopsied muscle specimen stained for LAMP2 and confirmed the diagnosis of vacuolar myopathy with dilated cardiomyopathy. PMID: 17873513 Analysis of the lysosome-associated membrane protein-2 (LAMP-2) gene detected a novel mutation, confirming a diagnosis of Danon disease. PMID: 17899313 A new intronic mutation in the LAMP2 gene in French Candian family leading to out frame skppin of exon 7 in Dannon disease. PMID: 18004770

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.