HCC-1, a member of the C-C, or β chemokine class, is a 8.7 kDa, non-glycosylated polypeptide of 74 amino acids. Mature HCC-1 is produced by cleavage of a 19 amino acid signal peptide from the precursor HCC-1 (93 amino acids).
HCC-1, a member of the C-C, or β chemokine class, is a 8.7 kDa, non-glycosylated polypeptide of 74 amino acids. Mature HCC-1 is produced by cleavage of a 19 amino acid signal peptide from the precursor HCC-1 (93 amino acids). HCC-1 is expressed constitutively in normal tissues and is present in high concentrations in human plasma. It shows approximately 46% amino acid identity with MIP-1α and MIP-1β, and 29-37% sequence identity with other C-C chemokines.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing 0.5 mg bovine serum albumin.
Analysis Note
The biological activity is measured by its ability to chemoattract cultured human monocytes or BaF/3 hCCR1 transfected cells.
European journal of medical research, 1(5), 223-236 (1996-02-22)
The structural determination of circulating human peptides is essential to determine their correct posttranslationally processed form. Human hemofiltrate from patients with end stage renal disease is accessible in large quantities and is used as a source for the preparation of
The nuclear matrix is the non-chromatin skeleton of the nucleus. This structure contributes to the shape of the nucleus and regulates various nuclear functions. In this study, nuclear matrix proteins of human normal liver, a liver cancer cell line, HepG2
The Journal of experimental medicine, 183(1), 295-299 (1996-01-01)
A novel CC chemokine, HCC-1, was isolated from the hemofiltrate of patients with chronic renal failure. HCC-1 has a relative molecular mass of 8,673 and consists of 74 amino acids including four cysteines linked to disulfide bonds. HCC-1 cDNA was
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