Alpha 1 type I collagen; Alpha 2 type I collagen; alpha 2 type I procollagen; alpha 2(I) procollagen; alpha 2(I)-collagen; Alpha-1 type I collagen; alpha1(I) procollagen; CO1A1_HUMAN; COL1A1; COL1A2; collagen alpha 1 chain type I; Collagen alpha-1(I) chain; collagen alpha-1(I) chain preproprotein; Collagen I alpha 1 polypeptide; Collagen I alpha 2 polypeptide; collagen of skin, tendon and bone, alpha-1 chain; collagen of skin, tendon and bone, alpha-2 chain; Collagen type I alpha 1; Collagen type I alpha 2; EDSC; OI1; OI2; OI3; OI4; pro-alpha-1 collagen type 1; type I proalpha 1; type I procollagen alpha 1 chain; Type I procollagen;
WB 1:500-1:1000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat, Bovine
Pig(100%), Zebrafish(89%), Horse(100%), Dog(100%), Chicken(89%)
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Collagen I Antibody detects endogenous levels of total Collagen I.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
A synthesized peptide derived from human Collagen I, corresponding to a region within N-terminal amino acids.
Observed Mol.Wt.: 130-150 kDa.
Predicted Mol.Wt.: 139kDa.
Secreted > extracellular space > extracellular matrix.
Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
This gene encodes one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in this gene are associated with osteogenesis imperfecta, Ehlers-Danlos syndrome, idiopathic osteoporosis, and atypical Marfan syndrome. Symptoms associated with mutations in this gene, however, tend to be less severe than mutations in the gene for alpha-1 type I collagen since alpha-2 is less abundant.
10 20 30 40 50
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR
60 70 80 90 100
DVWKPEPCRI CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE
110 120 130 140 150
SPTDQETTGV EGPKGDTGPR GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP
160 170 180 190 200
GPPGLGGNFA PQLSYGYDEK STGGISVPGP MGPSGPRGLP GPPGAPGPQG
210 220 230 240 250
FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR PGERGPPGPQ
260 270 280 290 300
GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ
310 320 330 340 350
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG
360 370 380 390 400
AKGEAGPQGP RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN
410 420 430 440 450
GAPGIAGAPG FPGARGPSGP QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE
460 470 480 490 500
PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL PGPPGERGGP GSRGFPGADG
510 520 530 540 550
VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL TGSPGSPGPD
560 570 580 590 600
GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV
610 620 630 640 650
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG
660 670 680 690 700
PPGEAGKPGE QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN
710 720 730 740 750
GAPGNDGAKG DAGAPGAPGS QGAPGLQGMP GERGAAGLPG PKGDRGDAGP
760 770 780 790 800
KGADGSPGKD GVRGLTGPIG PPGPAGAPGD KGESGPSGPA GPTGARGAPG
810 820 830 840 850
DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP PGPAGPAGPP
860 870 880 890 900
GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP
910 920 930 940 950
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG
960 970 980 990 1000
PQGIAGQRGV VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM
1010 1020 1030 1040 1050
GPPGLAGPPG ESGREGAPGA EGSPGRDGSP GAKGDRGETG PAGPPGAPGA
1060 1070 1080 1090 1100
PGAPGPVGPA GKSGDRGETG PAGPTGPVGP VGARGPAGPQ GPRGDKGETG
1110 1120 1130 1140 1150
EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP RGPPGSAGAP
1160 1170 1180 1190 1200
GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF
1210 1220 1230 1240 1250
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG
1260 1270 1280 1290 1300
SRKNPARTCR DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV
1310 1320 1330 1340 1350
YPTQPSVAQK NWYISKNPKD KRHVWFGESM TDGFQFEYGG QGSDPADVAI
1360 1370 1380 1390 1400
QLTFLRLMST EASQNITYHC KNSVAYMDQQ TGNLKKALLL QGSNEIEIRA
1410 1420 1430 1440 1450
EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII DVAPLDVGAP
Type I collagen is a member of group I collagen (fibrillar forming collagen).
Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are 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.
Extracellular region or secreted;
Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2 (PubMed:14749390). Interacts with MFAP4 in a Ca (2+)-dependent manner (By similarity).
The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).Belongs to the fibrillar collagen family.
· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.(View pathway)
· Environmental Information Processing > Signaling molecules and interaction > ECM-receptor interaction.(View pathway)
· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.(View pathway)
· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.
· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.
· Organismal Systems > Immune system > Platelet activation.(View pathway)
· Organismal Systems > Endocrine system > Relaxin signaling pathway.
· Organismal Systems > Digestive system > Protein digestion and absorption.
Application: WB Species:human; Sample:Not available
Figure 6. PnAg regulates gp130/Jak/Stat3 signaling pathway (A) and (B) NIH-3T3 and HaCat Cells were treated with PnAg at different concentrations and cell viability was tested using MTT analysis. (C) Wound healing assay reflected the effect of PnAg on cell migration. (D) Binding mode of PnAg in the active pocket of gp130. (E) and (F) MMPs activity and expression levels of Stat3, VEGF, TGFB-1, and TGFB1 detected using zymographic and Western blot assays. (G) Diagram of the proposed function of PnAg in wound inflammation and re-epithelialization controls.
Application: IHC Species:human; Sample:Not available
Figure 2. PnAg promotes wound healing in SD rats. (A) Photographs of rat skin full-thickness excision wounds on different post-excision days. (B) Change in wound areas of SD rats after treatment; (C) and (D) Expression levels of collagen I, NF-κB, TGF-ß, MMP-2, and MMP-9 in tissues on day 7 and 17 detected by immunohistochemistry. (E) Histogram of protein expression levels in these tissues. (F) and (G) Histomorphological changes in wound tissues stained by Masson trichrome and HE on day 17.
Application: WB Species:bovine; Sample:Not available
Fig. 3. S. aureus upregulates the protein expression of p-ERK1/2 to regulate Collagen I and a-SMA expression in BMFBs. Analysis of p-ERK1/2 protein expression in BMFBs after stimulation with 5 ng/ml TGF-b1 for 0 h, 6 h, 12 h, 24 h, 36 h, 48 h and 72 h (A). BMFBs were pretreated with PD98059 2 h before the indicated treatments with 5 ng/ ml TGF-b1. b-actin was used as a loading control for each condition (B). The data shown represent one of three independent experiments.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.