Recombinant Human Serpin H1 Protein (C-6His)

Name: Recombinant Human Serpin H1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0621NP
Availability: InStock

BL-0621NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Serine Protease Inhibitor-clade H1 is produced by our Mammalian expression system and the target gene encoding Ala19-Leu418 is expressed with a 6His tag at the C-terminus.
Accession	P50454
Synonym	Serpin H1; 47 kDa Heat Shock Protein; Arsenic-Transactivated Protein 3; AsTP3; Cell Proliferation-Inducing Gene 14 Protein; Collagen-Binding Protein; Colligin; Rheumatoid Arthritis-Related Antigen RA-A47; SERPINH1; CBP1; CBP2; HSP47; SERPINH2
Gene Background	Serpin H1 is a serine proteinase inhibitors Which belongs to the serpin family. Serpin H1 is induced by heat shock. Serpin H1 localizes to the endoplasmic reticulum lumen and binds specifically to collagen. Thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. Serpin H1 may be a marker for cancer and nucleotide polymorphisms in this gene may be associated with preterm birth caused by preterm premature rupture of membranes.
Molecular Mass	45.5 KDa
Apmol Mass	51 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 1546 OMIM: 600943 KEGG: hsa:871 STRING: 9606.ENSP00000350894 UniGene: PMID: 28849239 an endoplasmic reticulum complex of resident chaperones that includes HSP47, FKBP65, and BiP regulating the activity of LH2. PMID: 28177155 These observations indicate that this system is appropriate for detecting the interaction between HSP47 and collagen, and could be applied to high-throughput screening for drugs capable of suppressing and/or curing fibrosis. PMID: 29438711 miR-29b can reduce collagen biosynthesis during skin wound healing likely via post-transcriptional inhibition of HSP47 expression. PMID: 27477081 HSP47 expression in patients with colorectal cancer and the number of HSP47-positive spindle cells in the tumor stroma were significantly higher compared with those in adjacent normal colonic mucosa, and the number of the latter cells increased with tumor progression. PMID: 27925182 The essential parts of the Golgi stress response from the perspective of the organelle autoregulation. The pathways of the mammalian Golgi stress response have been identified, specifically the HSP47 pathway. PMID: 28179603 Overexpression of LOXL2 and SERPINH1 was observed in clinical specimens of lung cancer and fibrotic lesions. Downregulation of miR-29a caused overexpression of LOXL2 and SERPINH1 in lung cancer and IPF, suggesting that these genes are involved in the pathogenesis of these two diseases. PMID: 27488440 The changes in the SERPINH1 and SERPINF1 genes in patients with osteogenesis imperfect were synonymous polymorphisms or missense changes located in non-coding regions. PMID: 27706701 Overexpression of HSP47 is associated with poor prognosis in patients with esophageal squamous cell carcinoma and this is consistent with the function of HSP47 in terms of increased cell proliferation and colony formation. PMID: 25953518 A novel homozygous variant in SERPINH1 associated with a severe, lethal presentation of osteogenesis imperfecta with hydranencephaly. PMID: 27677223 The present study demonstrates that HSP47 promotes glioma angiogenesis and highlights the importance of HSP47 as an attractive therapeutic target of GBM. PMID: 25758142 Although the chemical chaperone 4-PBA partially restores the solubility of the Hsp47 OI mutants, collagen-binding activity of Hsp47 was not improved. PMID: 26692483 Data show that the expression of heat shock protein 47 (HSP47) was increased in the peripheral blood mononuclear cells and plasma from scleroderma patients. PMID: 26091621 Mutations in the HSP47 and FKBP65 produce a moderately severe form of Osteogenesis imperfect. PMID: 25510505 In patients with schistosomiasis japonica, TGF-beta1 participates not only in the inflammatory process, but also in the fibrotic process in which Hsp47 and CTGF probably play a key role. PMID: 25111595 Hsp47 expression promotes cancer progression in part by enhancing deposition of extracellular matrix proteins. PMID: 25744716 IL-17A-induced HSP47 expression is involved in collagen I expression in intestinal subepithelial myofibroblasts, which might contribute to intestinal fibrosis in Crohn's disease. PMID: 24534724 silencing of the HSP47 gene significantly inhibited cell migration and invasion in cancer cells and the expression of HSP47 was upregulated in cancer tissues and cervical intraepithelial neoplasia, as demonstrated by immunostaining. PMID: 24141696 miR-29b down-regulates HSP47 and LOX expression. PMID: 24650661 HSP47 is a novel glioma-associated antigen PMID: 24623841 TRAIL induced HSF1 inactivation leads to the suppression of Hsp47-dependent collagen production in activated human hepatic stellate cells. PMID: 23587601 Correlative Hsp47 expression in fibroblasts with bFGF in inflammatory cells may contribute to stromal fibrosis and obstruction in colorectal carcinoma PMID: 23265436 NMR and mutational identification of the collagen-binding site of the chaperone Hsp47 PMID: 23049894 Hsp47 may be related to the TGF-beta1-induced transdifferentiation of human Tenon's fibroblasts to myofibroblasts. PMID: 22967132 Hsp47 recognizes the triple-helix form of procollagen in vitro and in vivo. PMID: 22235129 Overexpression of HSP47 decreased the secretion of heterotrimers containing the mutant collagen alpha5(IV) chain. PMID: 21187648 HSP47 and fascin expression may play role in the pathogenesis of invasive ductal carcinoma of the breast and prostatic adenocarcinoma because their expression is significantly higher than their normal counterpart. PMID: 20701077 We conclude that colligin 2 is expressed in all cellular components of glioma blood vessels and may serve as a general marker for active angiogenesis PMID: 19067716 down-regulated KLF4, CHGA, GPX3, SST and LIPF, together with up-regulated SERPINH1, THY1 and INHBA is an 8-gene signature for gastric cancer PMID: 20043075 Increased heat shock protein 47 expression is associated with esophageal squamous cell carcinoma. PMID: 20112500 The enhancement of HSP47 expression by TGF-beta and IL-1 beta has been confirmed in embryonic lung fibroblasts. PMID: 11994473 induced in cicatricial pemphigoid: possible role(s) in dermal fibrosis PMID: 12061838 Results indicate a novel means by which type I collagen production is regulated by the endoplasmic reticulum constituent, Hsp47. PMID: 12163502 Modulates the production of the endostatin precursor collagen XVIII in head and neck carcinomas PMID: 12174873 levels of HSP47 protein and autoantibodies to HSP47 in the sera of patients with rheumatic autoimmune diseases PMID: 12659832 gene expression profiling in epidermolysis bullosa acquisita PMID: 12824005 high levels of expression of Hsp47 and adult and oncofetal fibronectin in Dupuytren's contracture suggests that cell-mediated alterations in the extracellular environment may play an important role in the disease process PMID: 15047128 HSP47 has a role in aging and photoaging in human fibroblasts PMID: 15247019 The surface-exposed RA-A47 may induce autoantibodies and inflammatory reactions in autoimmune disease situations such as rheumatoid arthritis. PMID: 15389525 HSP47 is constitutively expressed in human hepatic stellate cells and may be a target for antifibrotic therapy. PMID: 15806139 Our results suggest the existence of different fibrotic pathways among these groups involved in the expression of HSP47 and type I procollagen. PMID: 15955241 results suggest nitric oxide has dual effects on collagen synthesis by fibroblasts: the direct stimulation of collagen synthesis due to the up-regulation of procollagen alphaI(1) mRNA, and an indirect effect through the increase of HSP47 mRNA expression PMID: 16171977 analysis of the client recognition mechanism of HSP47 PMID: 16326708 analysis of recognition of the collagen triple helix by chaperone HSP47 PMID: 16484215 A functional SNP in the promoter of the SERPINH1 gene increases risk of preterm premature rupture of membranes in African Americans. PMID: 16938879 The anti-fibrotic effect of pirfenidone may be mediated through direct inhibition of collagen type I expression and inhibition of HSP47 expression in lung fibroblasts. PMID: 18093617 HSP47-positive fibroblasts were main constituent cell of dermatofibroma. PMID: 18095990 These studies define a new haplotype in the SERPINH1 gene that modifies risk of an adverse obstetrical outcome. PMID: 18205191 During keratin preparation from cultured human tumor cell lines, Hsps might be associated with keratin expression in tumor cells PMID: 18293509 Hsp47 was exposed on surface of GPVI-activated platelets; inhibition of Hsp47 abolished platelet aggregation in response to collagen, but partially reduced aggregation in response to other agonists; propose Hsp47 may play a role in hemostasis & thrombosis PMID: 19341245

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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.