Alexa Fluor 647-Labeled Human HLA-A*11:01&B2M&MATN2 (KTLTSVFQK) Monomer Protein
Catalog No: MATN2-HP002
- Species
- Human
- Expression System
- HEK293
- Tag
- His, Avi
Product overview
Recombinant Alexa Fluor 647-Labeled Human HLA-A*11:01&B2M&MATN2 (KTLTSVFQK) Monomer Protein is expressed from HEK293 with His tag and Avi tag at the C-terminus. It contains Gly25-Thr305 (HLA-A*11:01), Ile21-Met119 (B2M) and KTLTSVFQK peptide (accession: AAV53343.1(HLA-A*11:01) & P61769(B2M) &KTLTSVFQK).
Product Details
- Molecular Aliases
- MATN2; UNQ193/PRO219; Matrilin-2
- Protein Length
- Gly25-Thr305
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 50.50 kDa. Due to glycosylation, the protein migrates to 55-65 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE
- Buffer / Formulation
- Supplied as 0.22 μm filtered solution in PBS (pH 7.4).
- State
- Liquid
- Storage Conditions
- Valid for 6 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Data Display
Alexa Fluor 647-Labeled Human HLA-A*11:01&B2M&MATN2 (KTLTSVFQK) Monomer on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
Background
The matrilins represent a new family of oligomeric proteins that are assumed to act as adapter molecules connecting other proteins and proteoglycans in the extracellular matrix. Matrilin-2, the largest member of the family, is a widely distributed, oligomeric extracellular matrix protein. It incorporates into loose and dense connective tissue and forms a filamentous network by binding to a variety of different extracellular matrix proteins.
References
- (1) Szabó E, Lódi C, Korpos E, Batmunkh E, Rottenberger Z, Deák F, Kiss I, Tokés AM, Lotz G, László V, Kiss A, Schaff Z, Nagy P. Expression of matrilin-2 in oval cells during rat liver regeneration. Matrix Biol. 2007 Sep;26(7):554-60. doi: 10.1016/j.matbio.2007.04.007. Epub 2007 Apr 21. PMID: 17513098. (2) Wang Z, Luo J, Iwamoto S, Chen Q. Matrilin-2 is proteolytically cleaved by ADAMTS-4 and ADAMTS-5. Molecules. 2014 Jun 23;19(6):8472-87. doi: 10.3390/molecules19068472. PMID: 24959676; PMCID: PMC6271824.
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