Recombinant Mouse Fos-Related Antigen 1 (FOSL1) Protein (His&Myc)

Name: Recombinant Mouse Fos-Related Antigen 1 (FOSL1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06204P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Fos-Related Antigen 1 (FOSL1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P48755
Target Symbol	FOSL1
Synonyms	FRA-1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MYRDYGEPGPSSGAGSPYGRPAQPPQAQAQTAQQQKFHLVPSIDSSSQELHWMVQPHFLGPTGYPRPLAYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEGDKKDPGGSGSTSGASSPPAPGRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCSSAHRKSSSSSGDPSSDPLGSPTLLAL
Expression Range	1-273aa
Protein Length	Full Length
Mol. Weight	37.2 kDa
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

Subcellular Location	Nucleus.
Protein Families	BZIP family, Fos subfamily
Database References	KEGG: mmu:14283 STRING: 10090.ENSMUSP00000025850 UniGene: PMID: 27286066 Upon stimulation with poly(I:C), malaria parasite-infected red blood cells (iRBCs), or vesicular stomatitis virus (VSV), FOSL1 "translocated" from the nucleus to the cytoplasm, where it inhibited the interactions between TNF receptor-associated factor 3 (TRAF3), TIR domain-containing adapter inducing IFN-beta (TRIF), and Tank-binding kinase 1 (TBK1) via impairing K63-linked polyubiquitination of TRAF3 and TRIF. PMID: 28049150 Adipose-derived stromal cells overexpressing Fra-1 effectively protect against osteoarthritis. PMID: 26361381 Overexpression of Fosl1, which encodes a component of the AP-1 transcription factor complex, in osteoblasts significantly blocked malleal capillary narrowing. PMID: 26428006 Fra-1 gene expression is activated in response lipopolysaccharide induced lung-injury in mice. PMID: 26071555 Data suggest that expression of Fra1 (fos-related antigen 1) in preadipocytes is up-regulated by arachidonic acid (AA) during late stages of adipogenesis; however, in early stage of adipogenesis, AA inhibits adipogenesis via Fra1-dependent mechanism. PMID: 25325755 Fra-1 plays a key role in promoting chronic CS-induced lung macrophagic inflammation in vivo PMID: 25489966 we demonstrate that Fra1 negatively controls plasma cell differentiation by repressing Blimp1 expression. PMID: 25288397 observations suggest that MyoD and pRb work together cooperatively at the level of the intronic enhancer of Fra-1 during terminal cell cycle arrest PMID: 25006242 findings, based on a definitive genetic mouse model provide fundamental insights into mammary duct maturation and homeostasis and reveal that Scrib loss activates a MAPK/Fra1 pathway that alters mammary progenitor activity PMID: 24852022 findings support the hypothesis that miR-19a-3p, which regulates tumor-associated macrophages(TAMs)in the breast tumor microenvironment,is able to regulate the phenotype of TAMs by targeting the Fra-1 gene and other genes in its downstream signaling pathway PMID: 23831570 modulates the expression of detoxification genes and the adaptive response of the liver to bile acids/xenobiotic overload PMID: 23703832 these results indicate that Fra-1 is a direct target of Runx2 during osteogenic differentiation of C2C12 myogenic progenitor cells. PMID: 23159633 Fra-1 mediates anti-fibrotic effects in the lung through the modulation of proinflammatory, profibrotic and fibrotic gene expression. PMID: 22911824 data suggest the involvement of an injury-induced Fra-1 transcription factor as a regulator of keratinocyte gene expression, which might act as an antagonistic player to restrict epithelial-driven angiogenic responses during normal skin flap integration. PMID: 21840727 FRA-1, induced in response to estrogen signaling via ESR1, is a key regulator of stromal differentiation and remodeling during early pregnancy. PMID: 22514284 Fra-1 (Delta/Delta) mice showed a greater resistance to LPS-induced mortality than did their Fra-1(+/+) counterparts. PMID: 21816965 Fra-1 is an important mediator of interstitial lung disease following gefitinib treatment PMID: 21460858 Fra-1tg mice spontaneously develop a progressive biliary disease. PMID: 21480331 4T1 cells stimulate de novo overexpression of Fra-1 in RAW264.7 cells, and then Fra-1 binds to the interleukin 6 (IL-6) promoter to increase production of cytokine IL-6 in murine RAW264.7 cells. PMID: 20386569 Study supports potential roles for jun D, jun B, and fra-1 in the dietary energy restriction regulation of AP-1 function in the Sencar mouse skin carcinogenesis model. PMID: 20232358 AP-1 (Fra-1/c-Jun)-mediated induction of expression of matrix metalloproteinase-2 is required for 15S-hydroxyeicosatetraenoic acid-induced angiogenesis PMID: 20353950 data suggest that the Fra-1-containing transcription factor AP-1 inhibits fracture-induced endochondral ossification and bony bridge formation presumably through suppression of inflammation-induced chondrogenesis PMID: 19558315 interactions between mouse breast tumor cells and tumor-associated macrophages remodel the tumor microenvironment, leading to the upregulation of Fra-1 PMID: 19966854 results demonstrate that the Erk cascade plays a dual role in the co-ordinated regulation of the transcription and the phosphorylation of Fra-1 by insulin. PMID: 12197835 examination of the anabolic action of Fra-1 in treatment of osteoporosis PMID: 15121008 Fra-1 is an activator of bone matrix formation. PMID: 15229648 reduced expression of thrombospondins in Fra1 Tg mice underlies craniofacial dysmorphism, independent of osteosclerosis. PMID: 16598380 Expression of transcription factor Fra-1 was significantly elevated in emphysema lungs. PMID: 17298450 FRA-1 can promote motility, invasion, and anchorage-independent growth of lung epithelial cells in vitro, but is insufficient for tumor formation PMID: 17616677 Fra-1 suppresses LPS-induced mRNA expression by binding to the AP-1-binding site PMID: 19251936 Inorganic phosphate regulates MGP expression in osteoblasts through the ERK1/2-Fra-1 pathway. PMID: 19419315

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.