Recombinant Mouse Serpin H1 (Serpinh1)

Code CSB-YP021087MO
MSDS
Size $306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
Serpinh1
Uniprot No.
Research Area
Others
Alternative Names
Serpinh1; Cbp1; Hsp47; Serpin H1; 47 kDa heat shock protein; Collagen-binding protein; Colligin; Serine protease inhibitor J6
Species
Mus musculus (Mouse)
Source
Yeast
Expression Region
18-417aa
Target Protein Sequence
AEVKKPLEAAAPGTAEKLSSKATTLAERSTGLAFSLYQAMAKDQAVENILLSPLVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEVHTGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWASQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVTMMHRTGLYNYYDDEKEKLQMVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKAWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDTEGNPFDQDIYGREELRSPKLFYADHPFIFLVRDNQSGSLLFIGRLVRPKGDKMRDEL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
46.8kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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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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