Recombinant Mouse Serpin H1 (SERPINH1) Protein (His-SUMO)

Name: Recombinant Mouse Serpin H1 (SERPINH1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08631P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Serpin H1 (SERPINH1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P19324
Target Symbol	SERPINH1
Synonyms	Serpinh1; Cbp1; Hsp47; Serpin H1; 47 kDa heat shock protein; Collagen-binding protein; Colligin; Serine protease inhibitor J6
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	AEVKKPLEAAAPGTAEKLSSKATTLAERSTGLAFSLYQAMAKDQAVENILLSPLVVASSLGLVSLGGKATTASQAKAVLSAEKLRDEEVHTGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWASQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVTMMHRTGLYNYYDDEKEKLQMVEMPLAHKLSSLIILMPHHVEPLERLEKLLTKEQLKAWMGKMQKKAVAISLPKGVVEVTHDLQKHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFEWDTEGNPFDQDIYGREELRSPKLFYADHPFIFLVRDNQSGSLLFIGRLVRPKGDKMRDEL
Expression Range	18-417aa
Protein Length	Full Length of Mature Protein
Mol. Weight	60.8kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.
Subcellular Location	Endoplasmic reticulum lumen.
Protein Families	Serpin family
Database References	KEGG: mmu:12406 STRING: 10090.ENSMUSP00000091706 UniGene: PMID: 28802097 miR-29b can reduce collagen biosynthesis during skin wound healing likely via post-transcriptional inhibition of HSP47 expression. PMID: 27477081 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 Intradermal administration of siHSP47-nanoparticles effectively reduced HSP47 protein expression in skin to normal level. PMID: 26196532 2014). Data show that the expression of heat shock protein 47 (HSP47) was increased in the scleroderma mouse model. PMID: 26091621 Deletion of Hsp47 caused activated hepatic stellate cells to undergo ER stress-mediated apoptosis when autophagy was inhibited PMID: 25525267 Mouse embryonic stem cell migration and differentiation into smooth muscle cells is induced by the over-expression of HSP47. PMID: 24454956 Authors conclude that heat shock protein 47 plays an essential role in Schistosoma japonicum-induced hepatic fibrosis in mice. PMID: 24295791 miR-29b down-regulates HSP47 and LOX expression. PMID: 24650661 expression patterns of HSP70 and HSP47 in tissues following short-pulse laser irradiation PMID: 23587755 The pH sensitivity of murine heat shock protein 47 (HSP47) binding to collagen is affected by mutations in the breach histidine cluster. PMID: 23212911 These results demonstrate that Hsp47 is indispensable for well-organized cartilage and normal endochondral bone formation. PMID: 22492985 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 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 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 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 type IV collagen in dilated endoplasmic reticulum leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP PMID: 15522896 analysis of the client recognition mechanism of HSP47 PMID: 16326708 analysis of recognition of the collagen triple helix by chaperone HSP47 PMID: 16484215 Hsp47 is required for correct folding and prevention of aggregation of type I collagen in the ER. PMID: 16525016 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.