Human BRAK Recombinant Protein LyophilizedIHUBRAKRLY5UG
Human BRAK Recombinant Protein Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in with a purity of Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per and#956;g (1EU/and#956;g)..
- Species: Human
- Target: CXCL14
Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per and#956;g (1EU/and#956;g).
- Source: E. coli
- Storage Conditions: The lyophilized BRAK recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted BRAK is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing BRAK recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 alpha and beta. Recombinant human BRAK is a 9.4 kDa protein containing 77 amino acid residues.
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This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.
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