Recombinant Human Iba1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2481

Recombinant Human Iba1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2481
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Product Overview

Tag His
Host Species Human
Accession P55008
Synonym AIF-1, IBA1, IRT-1, IRT1
Background AIF1, also known as IBA1, is an actin-binding protein. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. It is expressed in macrophages and neutrophils. AIF1 enhances membrane ruffling and RAC activation. AIF1 enhances the actin-bundling activity of LCP1. It also enhances lymphocyte migration. AIF1 may play a role in macrophage activation and function. It binds calcium and plays a role in RAC signaling and in phagocytosis. It promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes.
Description A DNA sequence encoding the mature form of human AIF1 (P55008-1) (Met1-Pro147) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal His
AA Sequence Met1-Pro147
Molecular Weight The recombinant human AIF1 consists of 162 a.a. and predicts a molecular mass of 18.5 KDa. It migrates as an approximately 18 KDa band in SDS-PAGE under reducing conditions.
Purity >85% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 10% glycerol, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.
Subcellular Location Cytoplasm, cytoskeleton. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, phagocytic cup.
Database References
Tissue Specificity Detected in T-lymphocytes and peripheral blood mononuclear cells.

Gene Functions References

  1. Small interfering RNA (siRNA)-mediated silencing of AIF-1 expression resulted in a reduction in cell proliferation and migration in human HCC cells. PMID: 30188879
  2. It may be speculated that Iba-1 protein besides its major function (involvement in phagocytosis) can perform the role of a transcriptional factor. PMID: 30136808
  3. This study shown the AIF1 expression in Microglia and Astrocytes in stroke, Alzheimer's disease, and Lewy body dementia. PMID: 28398520
  4. involved in the immunological process underlying rheumatoid arthritis PMID: 26585362
  5. Using double labeling with Iba-1 and cd68 could determine the physiological state of microglia in brain contusion based on their morphology and immunoreactivity. PMID: 27442380
  6. The results of our study suggest that the AIF1 gene polymorphisms have no influence on long-term kidney allograft function. PMID: 26324213
  7. Data showed that AIF-1 promoted the proliferation of HepG2 cells by accelerating the activation of IGF-1R and its downstream signaling pathway, which confirms that AIF-1 plays a crucial role in the development of hepatocellular carcinoma cells. PMID: 25998745
  8. AIF-1 functions as a tumor suppressor possibly by regulating beta-catenin in gastric cancer. the level of AIF-1 expression may serve as a protective prognostic indicator for gastric cancer. PMID: 24337893
  9. AIF-1, which induced chemokines and enhanced chemotaxis of monocytes, may represent a molecular target for the therapy of immune-inflammatory disorders PMID: 24796669
  10. The results of this study suggest a lack of association between AIF-1 gene polymorphisms and response to sulphasalazine treatment in rheumatoid arthritis. PMID: 25026748
  11. The results of this study suggest that the patients with the rs2259571 CC AIF1 genotype have a poorer response to therapy with Methotrexate. PMID: 24018427
  12. We are unable to find statistically significant association between COX-2 and AIF-1 gene polymorphisms and allograft survival. PMID: 23777936
  13. The overexpressed AIF-1, the novel inflammatory polypeptide derived from macrophage lineages, is closely associated with atherogenesis via affecting the blood composition and promoting macrophage uptake and foam cell formation. PMID: 23867161
  14. AIF-1 can protect rheumatoid arthritis fibroblast-like synoviocytes from apoptosis induced by NO by upregulating the expression of p-Akt and p-BAD. PMID: 23547889
  15. daintain/AIF-1 reinforced the resistance of breast cancer cells to cisplatin by inhibition of cell apoptosis and reduction of intracellular cisplatin accumulation PMID: 23221708
  16. Serum AIF-1 concentration correlated with albuminuria and eGFR in patients with type 2 diabetes and it could be a marker of diabetic nephropathy as well as activated macrophages. PMID: 22560794
  17. Our results suggest that the AIF1 rs2259571 CC genotype is associated with the active form of RA. PMID: 22106834
  18. The serum AIF-1 concentrations were positively correlated with levels of fasting plasma glucose, hemoglobin A1c, triglycerides, and uric acid, and with waist circumference and BMI, and were inversely correlated with HDL cholesterol levels. PMID: 22225958
  19. Overexpression of AIF-1 stimulates migration and proliferation of human vascular smooth muscle cells, whereas IRT-1 exerts opposite effects. PMID: 22116621
  20. Our data suggest that SNPs in or near the AIF1 locus contribute to obesity risk in the Greek population. PMID: 21720444
  21. daintain/AIF-1 activates p38 MAPK signaling pathway contributing to up-regulation of TNF-alpha in MDA-MB-231 and MCF-7 cells. PMID: 21509525
  22. AIF-1 shows promise that it can be a potential biomarker for cardiac allograft rejection. PMID: 20850992
  23. data demonstrated that expression profiles of AIF-1 and TLR-2 correlated with biopsy-proven allograft rejection in both peripheral blood and local tissue, suggesting their potential as diagnostic biomarkers for early detection of allograft rejection PMID: 21168672
  24. AIF-1 can induce IL-6 secretion on mononuclear cells and fibroblast chemotaxis. AIF-1 may accordingly provide an attractive new target for antifibrotic therapy in SSc as well as Scl GVHD. PMID: 21040744
  25. findings suggest that the impact of AIF-1 on endothelial cells would stimulate angiogenesis and consequently affect the progression of infantile hemangiomas PMID: 19745784
  26. AIF-1 binds and polymerizes F actin and also regulates Rac1 activity and vascular smooth muscle migration PMID: 12714565
  27. more AIF-1 immunoreactive macrophages/microglial cells and, interestingly, neurones were observed in Creutzfeldt-Jakob disease patients PMID: 12887599
  28. AIF-1 enhances VSMC growth by autocrine production of G-CSF, and AIF-1 expression may influence VSMC-inflammatory cell communication. PMID: 15117732
  29. Genomic rearrangement of AIF1 in arteriosclerosis was studied. PMID: 15784173
  30. The ability of AIF-1 to activate vascular smooth muscle is lost by mutation in the EF-hand calcium-binding region. PMID: 15922740
  31. Overexpression of allograft inflammatory factor-1 is associated with development of coronary artery vasculopathy PMID: 16049345
  32. These data indicate that AIF-1 mediates atherogenesis-initiated signaling and activation of macrophages. PMID: 16291819
  33. The subtle regulation of allograft inflammatory factor-1 in the involution of hemangiomas will help design a new anti-angiogenic therapy for some tumors. [REVIEW] PMID: 17010532
  34. The molecular conformational change induced by Ca(2+)-binding of Iba1 is different from that found in the classical EF-hand proteins, which demonstrates that Iba1 has an unique molecular switching mechanism dependent on Ca(2+)-binding. PMID: 17011575
  35. AIF-1 is a novel molecular component of podocytes and the upregulation of AIF-1 in an anti-GBM nephritis model may mainly be a consequence of its expression in infiltrating cells. PMID: 17035944
  36. Crystals of AIF-1 were grown at 291 K using PEG-8000 as precipitant, and diffraction extends to 3.3 A resolution. PMID: 17073733
  37. association of a nonsynonymous change within the AIF-1 gene with systemic sclerosis, and linkage with TNFA alleles within 50 kb of this gene PMID: 17498268
  38. a genetic association between AIF1 and the anti-centromere antibodies-positive subset of systemic sclerosis. PMID: 17522098
  39. Using immunohistochemistry, we found that AIF-1 is expressed at low levels in normal skin, but is highly upregulated in various inflammatory skin disorders PMID: 17533487
  40. These results suggest that AIF-1 may participate in the early pathogenesis of systemic sclerosis by promoting tissue T cell infiltration and production of cytokines capable of inducing the expression of a fibrotic phenotype in normal fibroblasts. PMID: 17907195
  41. daintain/AIF-1 can promote the growth of breast tumors via activating NF-kappaB signaling, which consequently up-regulates the expression of cyclin D1. PMID: 18341653
  42. The AIF1 rs2269475 T allele is associated with increased risk of rheumatoid arthritis development. PMID: 18721278
  43. AIF-1 expression regulates endothelial cell activation, signal transduction, and vasculogenesis. PMID: 18787073
  44. AIF-1 plays a role in inflammatory nerve disease and vascular smooth muscle cell proliferation and may be a new molecular target for treatment. PMID: 18816612
  45. Genetic variants of the HLA-A, HLA-B and AIF1 loci show independent associations with type 1 diabetes in Norwegian families PMID: 18987644


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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.

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