Serpinh1 Antibody, FITC conjugated

Code CSB-PA021087LC01MO
Size US$166
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Product Details

Full Product Name
Rabbit anti-Mus musculus (Mouse) Serpinh1 Polyclonal antibody
Uniprot No.
Target Names
Serpinh1
Alternative Names
Serpinh1 antibody; Cbp1 antibody; Hsp47 antibody; Serpin H1 antibody; 47 kDa heat shock protein antibody; Collagen-binding protein antibody; Colligin antibody; Serine protease inhibitor J6 antibody
Raised in
Rabbit
Species Reactivity
Mouse
Immunogen
Recombinant Mouse Serpin H1 protein (18-417AA)
Immunogen Species
Mus musculus (Mouse)
Conjugate
FITC
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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Target Background

Function
Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.
Gene References into Functions
  1. The HSP47 might exert influence on liver fibrosis via the regulation ofendothelin receptor A (ETAR) and endothelin receptor B (ETBR). PMID: 28802097
  2. miR-29b can reduce collagen biosynthesis during skin wound healing likely via post-transcriptional inhibition of HSP47 expression. PMID: 27477081
  3. HSP47 appears after a period of certain activities to repair damaged collagen fibers, and the activity was returned to a state of equilibrium at day 30 with significantly diminished expression. Thus, the results suggest that HSP47 is actively involved in homeostasis of periodontal tissue subjected to occlusal overload PMID: 27076780
  4. Intradermal administration of siHSP47-nanoparticles effectively reduced HSP47 protein expression in skin to normal level. PMID: 26196532
  5. 2014). Data show that the expression of heat shock protein 47 (HSP47) was increased in the scleroderma mouse model. PMID: 26091621
  6. Deletion of Hsp47 caused activated hepatic stellate cells to undergo ER stress-mediated apoptosis when autophagy was inhibited PMID: 25525267
  7. Mouse embryonic stem cell migration and differentiation into smooth muscle cells is induced by the over-expression of HSP47. PMID: 24454956
  8. Authors conclude that heat shock protein 47 plays an essential role in Schistosoma japonicum-induced hepatic fibrosis in mice. PMID: 24295791
  9. miR-29b down-regulates HSP47 and LOX expression. PMID: 24650661
  10. expression patterns of HSP70 and HSP47 in tissues following short-pulse laser irradiation PMID: 23587755
  11. The pH sensitivity of murine heat shock protein 47 (HSP47) binding to collagen is affected by mutations in the breach histidine cluster. PMID: 23212911
  12. These results demonstrate that Hsp47 is indispensable for well-organized cartilage and normal endochondral bone formation. PMID: 22492985
  13. overexpression of HSP47 in keloid fibroblast cells could induce excessive collagen accumulation by enhancing collagen synthesis, which not only presents a possible mechanism of keloid formation PMID: 22295344
  14. alpha-smooth-muscle-actin-positive myofibroblast of bleomycin-induced pulmonary fibrosis cells may synthesize procollagen in the fibrotic process of bleomycin-treated lungs through upregulation of HSP47 mRNA and play an important role in fibrogenesis. PMID: 20094730
  15. HSP47 localized in alpha-smooth muscle actin-positive myofibroblasts, F4/80 negative, surfactant protein-A-positive type II pneumocytes, and F4/80-positive macrophages. Cells may play role in fibrotic process through upregulation of HSP47. PMID: 12842808
  16. Results indicate that Hsp47 is required for the molecular maturation of type IV collagen and suggest that misfolded type IV collagen causes abnormal morphology of embryoid bodies. PMID: 15282337
  17. type IV collagen in dilated endoplasmic reticulum leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP PMID: 15522896
  18. analysis of the client recognition mechanism of HSP47 PMID: 16326708
  19. analysis of recognition of the collagen triple helix by chaperone HSP47 PMID: 16484215
  20. Hsp47 is required for correct folding and prevention of aggregation of type I collagen in the ER. PMID: 16525016
  21. the HSP47-specific siRNA inhibited expression of HSP47 at the level of mRNA and protein, and furthermore, adenovirus-mediated transfer of siRNA against HSP47 inhibited the expression of type I collagen and formation of scar tissue in animal mod PMID: 18093850

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Subcellular Location
Endoplasmic reticulum lumen.
Protein Families
Serpin family
Database Links
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