描述：
CXCL12, also known as SCYB12, PBSF and SDF-1β, is an 8.3 kDa, heparinbinding member of
the CXC (or alpha-) family of chemokines. Feline CXCL12(β) is synthesized as a 93 amino acid
(aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region. The mature
molecule exhibits a typical three antiparallel β-strand chemokinelike fold. There are no
potential Nlinked glycosylation sites. N-terminal aa’s 1 8 form a receptor binding site, while
aa’s 1 and 2 (LysPro) are involved in receptor activation. The C-terminus is likely associated
with heparin binding. SDF1β circulates and undergoes proteolytic processing. CD26 will remove
the first two Nterminal amino acids, possibly creating a reducedactivity chemokine. In addition
to the βisoform, alternate splicing of the feline SDF1 gene generates an αisoform. The alpha
isoform is identical to SDF1β, but shorter by four aa’s at the C-terminus. Although αand β
isoforms show similar activity, SDF1α is differentially processed, and different cells secrete the
two isoforms. Mature feline SDF1β is 96%, 97% and 100% aa identical to rat, mouse and human SDF1β, respectively. Human (and by inference, feline) SDF1 is active on mouse cells. SDF1α
and β are reported to be a monomers at neutral pH and physiologic ionic strength. SDF1α is
also reported to form dimers in the presence of heparan sulfate. On the cell surface, this may
well facilitate SDF1 interaction with its two receptors, CXCR4 and syndecan-4. Heparan sulfate
is known to protect SDF1 from proteolysis, and CXCR4 exists constitutively as a dimer.
Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning
and cell number of neural progenitors, and promote angiogenesis. It also enhances the survival
of myeloid progenitor cells.
原厂资料：
CXCL12, also known as SCYB12, PBSF and SDF-1β, is an 8.3 kDa, heparinbinding member of
the CXC (or alpha-) family of chemokines. Feline CXCL12(β) is synthesized as a 93 amino acid
(aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region. The mature
molecule exhibits a typical three antiparallel β-strand chemokinelike fold. There are no
potential Nlinked glycosylation sites. N-terminal aa’s 1 8 form a receptor binding site, while
aa’s 1 and 2 (LysPro) are involved in receptor activation. The C-terminus is likely associated
with heparin binding. SDF1β circulates and undergoes proteolytic processing. CD26 will remove
the first two Nterminal amino acids, possibly creating a reducedactivity chemokine. In addition
to the βisoform, alternate splicing of the feline SDF1 gene generates an αisoform. The alpha
isoform is identical to SDF1β, but shorter by four aa’s at the C-terminus. Although αand β
isoforms show similar activity, SDF1α is differentially processed, and different cells secrete the
two isoforms. Mature feline SDF1β is 96%, 97% and 100% aa identical to rat, mouse and human SDF1β, respectively. Human (and by inference, feline) SDF1 is active on mouse cells. SDF1α
and β are reported to be a monomers at neutral pH and physiologic ionic strength. SDF1α is
also reported to form dimers in the presence of heparan sulfate. On the cell surface, this may
well facilitate SDF1 interaction with its two receptors, CXCR4 and syndecan-4. Heparan sulfate
is known to protect SDF1 from proteolysis, and CXCR4 exists constitutively as a dimer.
Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning
and cell number of neural progenitors, and promote angiogenesis. It also enhances the survival
of myeloid progenitor cells.
京公网安备11010802025653 版权所有：北京逸优科技有限公司
