Recombinant Human Pro-Collagen II Protein

重组人Pro-Collagen II/COL2A1蛋白 | 重组人II型胶原α1链蛋白

Alpha-1 type II collagen | ANFH | AOM | cartilage collagen | Chondrocalcin | COL11A3 | COL2A1 | Collagen 2 | collagen alpha-1(II) chain | Collagen II | collagen II, alpha-1 polypeptide | collagen type 2 | collagen, type II, alpha 1 (primary osteoarthritis

rp188297-10μg

10μg

无动物源

≥90%(SDS-PAGE)

COL2A1 is the alpha-1 chain of type II collagen which is a fibrillar collagen found in cartilage and the vitreous humor of the eye. Mutations in this protein are associated with achondrogenesis, chondrodysplasia, early onset familial osteoarthritis, SED congenita, Langer-Saldino achondrogenesis, Kniest dysplasia, Stickler syndrome type I, and spondyloepimetaphyseal dysplasia Strudwick type. In addition, defects in processing chondrocalcin, a calcium binding protein that is the C-propeptide of this collagen molecule, are also associated with chondrodysplasia. There are two transcripts identified for this gene. Type II collagen is specific for cartilaginous tissues. Thus COL2A1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. The regulation of COL2A1, likely results from a balance of both positive and negative proteins. The inhibition of COL2A1 transcription following treatment of chick sternal chondrocytes with growth factors was accompanied by increased EF1 expression. Overexpression of EF1 in differentiated chondrocytes resulted in decreased expression of a reporter construct containing a collagen II promoter/enhancer insert. Post-translational: The N-telopeptide is covalently linked to the helical COL2 region of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chain. The C-telopeptide is covalently linked to an another site in the helical region of alpha 3(IX) COL2. Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.

Testing in progress

重组表达

28.2 kDa

N-His

33.3 kDa, under reducing conditions; 96.7 kDa, under non-reducing conditions.

CHO Accession #: P02458 | CHO

<1.0 EU/μg

人(Human)

1242-1487 aa

HHHHHHDQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL​

Yes

Yes