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AB323062

Recombinant Human LAMP2 Protein Standard

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Recombinant Human LAMP2 Protein Standard is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for sELISA, SDS-PAGE.

View Alternative Names

CD107b, Lysosome-associated membrane glycoprotein 2, LAMP-2, Lysosome-associated membrane protein 2, CD107 antigen-like family member B, LGP-96, LAMP2

2 Images
Sandwich ELISA - Recombinant Human LAMP2 Protein Standard (AB323062)
  • sELISA

Supplier Data

Sandwich ELISA - Recombinant Human LAMP2 Protein Standard (AB323062)

Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.

SDS-PAGE - Recombinant Human LAMP2 Protein Standard (AB323062)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human LAMP2 Protein Standard (AB323062)

SDS-PAGE analysis of ab323062 under reducing conditions for 2ug protein.

Key facts

Purity

>80% SDS-PAGE

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE, sELISA

applications

Biologically active

No

Accession

P13473

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.3 - 7.5 Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

Sequence info

[{"sequence":null,"proteinLength":"Fragment","predictedMolecularWeight":"38 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P13473","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

General info

Function

Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed : 11082038, PubMed : 18644871, PubMed : 24880125, PubMed : 27628032, PubMed : 36586411, PubMed : 37390818, PubMed : 8662539). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed : 37390818). 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 (PubMed : 11082038, PubMed : 18644871, PubMed : 24880125, PubMed : 27628032, PubMed : 36586411, PubMed : 8662539). Functions by binding target proteins, such as GAPDH, GPX4, NLRP3 and MLLT11, and targeting them for lysosomal degradation (PubMed : 11082038, PubMed : 18644871, PubMed : 24880125, PubMed : 36586411, PubMed : 8662539). In the chaperone-mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70, which recognize and bind substrate proteins and mediate their recruitment to lysosomes, where target proteins bind LAMP2 (PubMed : 36586411). Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed : 27628032). 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 (PubMed : 27628032). Required for normal degradation of the contents of autophagosomes (PubMed : 27628032). Required for efficient MHC class II-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 MHC II subunits (PubMed : 15894275, PubMed : 20518820). Is not required for efficient MHC class II-mediated presentation of endogenous antigens (PubMed : 20518820).. Isoform LAMP-2C. 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.

Sequence similarities

Belongs to the LAMP family.

Post-translational modifications

O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans.

Subcellular localisation

Endosome membrane

Product protocols

Target data

Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed : 11082038, PubMed : 18644871, PubMed : 24880125, PubMed : 27628032, PubMed : 36586411, PubMed : 37390818, PubMed : 8662539). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed : 37390818). 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 (PubMed : 11082038, PubMed : 18644871, PubMed : 24880125, PubMed : 27628032, PubMed : 36586411, PubMed : 8662539). Functions by binding target proteins, such as GAPDH, GPX4, NLRP3 and MLLT11, and targeting them for lysosomal degradation (PubMed : 11082038, PubMed : 18644871, PubMed : 24880125, PubMed : 36586411, PubMed : 8662539). In the chaperone-mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70, which recognize and bind substrate proteins and mediate their recruitment to lysosomes, where target proteins bind LAMP2 (PubMed : 36586411). Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed : 27628032). 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 (PubMed : 27628032). Required for normal degradation of the contents of autophagosomes (PubMed : 27628032). Required for efficient MHC class II-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 MHC II subunits (PubMed : 15894275, PubMed : 20518820). Is not required for efficient MHC class II-mediated presentation of endogenous antigens (PubMed : 20518820).. Isoform LAMP-2C. 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.
See full target information LAMP2

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