Recombinant human SDF1 alpha protein (Animal Free) (ab217453)
Key features and details
- Expression system: Escherichia coli
- Purity: > 98% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE, HPLC
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Product name
Recombinant human SDF1 alpha protein (Animal Free)
See all SDF1 alpha proteins and peptides -
Biological activity
Determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentation of 20-80 ng/ml.
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Purity
> 98 % SDS-PAGE.
> 98 % by HPLC. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
Yes -
Nature
Recombinant -
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Species
Human -
Sequence
KPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVC IDPKLKWIQEYLEKALNK -
Predicted molecular weight
8 kDa -
Amino acids
22 to 89 -
Additional sequence information
This product is for the mature full length protein. The signal peptide is not included.
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Preparation and Storage
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Alternative names
- C-X-C motif chemokine 12
- Chemokine (C-X-C motif) ligand 12
- cxcl12
see all -
Function
Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the Lyn kinase. Stimulates migration of monocytes through its receptor, CXCR4, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through Lyn kinase. -
Sequence similarities
Belongs to the intercrine alpha (chemokine CxC) family. -
Post-translational
modificationsProcessed forms SDF-1-beta(3-72) and SDF-1-alpha(3-67) are produced after secretion by proteolytic cleavage of isoforms Beta and Alpha, respectively. The N-terminal processing is probably achieved by DPP4. Isoform Alpha is first cleaved at the C-terminus to yield a SDF-1-alpha(1-67) intermediate before being processsed at the N-terminus. The C-terminal processing of isoform Alpha is reduced by binding to heparin and, probably, cell surface proteoglycans. -
Cellular localization
Secreted. - Information by UniProt