Analytical Data
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Gene name
CRTAP
- Application
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Alternative Names
CRTAP；CASP;Cartilage-associated Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75718
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Expression Region
27-401aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSQYERYSF RSFPRDELMP LESAYRHALD KYSGEHWAES VGYLEISLRL HRLLRDSEAF CHRNCSAAPQ PEPAAGLASY PELRLFGGLL RRAHCLKRCK QGLPAFRQSQ PSREVLADFQ RREPYKFLQF AYFKANNLPK AIAAAHTFLL KHPDDEMMKR NMAYYKSLPG AEDYIKDLET KSYESLFIRA VRAYNGENWR TSITDMELAL PDFFKAFYEC LAACEGSREI KDFKDFYLSI ADHYVEVLEC KIQCEENLTP VIGGYPVEKF VATMYHYLQF AYYKLNDLKN AAPCAVSYLL FDQNDKVMQQ NLVYYQYHRD TWGLSDEHFQ PRPEAVQFFN VTTLQKELYD FAKENIMDDD EGEVVEYVDD LLELEETS
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Molecular Weight
46 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CRTAP (Cartilage Associated Protein) is a critical protein involved in collagen maturation and stability, particularly in cartilage and bone tissues. Its significance has garnered attention due to its association with osteogenesis imperfecta (OI), a genetic disorder characterized by fragile bones, which often results from mutations in genes responsible for collagen processing. Research into CRTAP's structure and function has revealed its role in the endoplasmic reticulum, where it acts as a chaperone during collagen synthesis. The reconstitution of CRTAP as a recombinant protein has been a focal point for scientists aiming to understand its specific interactions within the collagen assembly pathway. This involves examining its role in modifying the folding and stability of collagen molecules, as well as its potential therapeutic applications in treating connective tissue disorders. Furthermore, studying recombinant CRTAP offers insights into the molecular mechanisms underlying cartilage and bone development, paving the way for innovative strategies in regenerative medicine and the treatment of collagen-related diseases. The research surrounding recombinant CRTAP not only enhances our understanding of collagen biology but also provides a platform for the development of novel therapeutic interventions aimed at alleviating the symptoms of conditions such as OI and other collagenopathies. Through these efforts, scientists hope to improve clinical outcomes and quality of life for affected individuals by targeting the underlying molecular defects in collagen metabolism. Overall, the investigation of CRTAP as a recombinant protein represents a significant advancement in the field of molecular biology and genetic medicine, highlighting the intricate relationship between protein function, genetic disorders, and potential therapeutic innovations.
