Recombinant human MCP2 protein (Active) (ab256074)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
-
Product name
Recombinant human MCP2 protein (Active)
See all MCP2 proteins and peptides -
Biological activity
Human THP-1 chemotaxis (first detectable at 100 ng/mL).
-
Purity
> 95 % SDS-PAGE. -
Endotoxin level
1.000 Eu/µg -
Expression system
Escherichia coli -
Accession
-
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
-
Species
Human -
Sequence
QPDSVSIPITCCFNVINRKIPIQRLESYTRITNIQCPKEAVIFKTKRGKE VCADPKERWVRDSMKHLDQIFQNLKP -
Predicted molecular weight
9 kDa -
Amino acids
24 to 99 -
Additional sequence information
Full-length mature C-C motif chemokine 8 chain lacking the signal peptide.
-
Preparation and Storage
-
Alternative names
- Ccl8
- CCL8_HUMAN
- HC14
see all -
Function
Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils. May play a role in neoplasia and inflammatory host responses. This protein can bind heparin. The processed form MCP-2(6-76) does not show monocyte chemotactic activity, but inhibits the chemotactic effect most predominantly of CCL7, and also of CCL2 and CCL5 and CCL8. -
Tissue specificity
Highest expression found in the small intestine and peripheral blood cells. Intermediate levels seen in the heart, placenta, lung, skeletal muscle, thymus, colon, ovary, spinal cord and pancreas. Low levels seen in the brain, liver, spleen and prostate. -
Sequence similarities
Belongs to the intercrine beta (chemokine CC) family. -
Post-translational
modificationsN-terminal processed form MCP-2(6-76) is produced by proteolytic cleavage after secretion from peripheral blood monocytes. -
Cellular localization
Secreted. - Information by UniProt
Images
-
SDS-PAGE - Recombinant human MCP2 protein (Active) (ab256074)
SDS-PAGE analysis of ab256074 (1 μg) under non-reducing (Lane 1) and reducing (Lane 2) conditions.
4-20% Tris-Glycine gel. Coomassie Blue staining.