Recombinant Human Fermitin Family Homolog 2 (FERMT2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00723P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Fermitin Family Homolog 2 (FERMT2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00723P
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Product Overview

Description Recombinant Human Fermitin Family Homolog 2 (FERMT2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q96AC1
Target Symbol FERMT2
Synonyms (Kindlin-2)(Mitogen-inducible gene 2 protein)(MIG-2)(Pleckstrin homology domain-containing family C member 1)(PH domain-containing family C member 1)
Species Homo sapiens (Human)
Expression System E.coli
Tag C-6His
Target Protein Sequence MALDGIRMPDGCYADGTWELSVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLITPGSGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPITSPEILAKMFKPQALLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPEQITTDITPECLVSPRYLKKYKNKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKKEELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV
Expression Range 1-680aa
Protein Length Full Length
Mol. Weight 83.8 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

Target Function Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling.
Subcellular Location Cytoplasm. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, stress fiber. Cell junction, focal adhesion. Membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, myofibril, sarcomere, I band. Cell surface. Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with ITGB3 at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides.
Protein Families Kindlin family
Database References
Tissue Specificity Ubiquitous. Found in numerous tumor tissues.

Gene Functions References

  1. Using molecular modeling and molecular dynamics simulations, we show that Asp344, Asp352, and Thr356 in kindlin-2 and Arg243 and Arg334 in ILK kinase domain (KD) are important in kindlin-2/ILK complex formation. Mutations that disrupt these interactions abrogate kindlin-2 and ILK colocalization in HeLa cells. PMID: 29237230
  2. Results found Kindlin-2 expression upregulated in hepatocellular carcinoma (HCC) tissues and cell lines and it correlates with aggressive clinicopathological features and poor prognosis. Mechanistically, Kindlin-2 promotes HCC invasion, metastasis and epithelial-mesenchymal transition through Wnt/beta-catenin signaling. PMID: 28969700
  3. Kindlin-2 is mainly expressed in the cytoplasm and nuclei of fibroblasts in the Esophageal cancer (EC) stroma. Kindlin-2 is upregulated in ECs compared with normal esophageal tissues. Kindlin-2 is more prevalent in poorly differentiated tumors. Kindlin-2 is expressed higher in EC smoker patients than non-smoker patients. Patients with a family history of EC show lower Kindlin-2 expression. PMID: 28667517
  4. Long noncoding RNA-ATB functions as a molecular sponge for miR-200b and Kindlin-2. PMID: 28640252
  5. Kindlin-2 is up-regulated in glioma cells and acts as an oncogene. It is an independent risk factor for poor prognosis. The Kindlin-2/YB-1/beta-catenin complex promotes EGFR transcription and contributes to glioma progression. Kindlin-2 is a potential diagnostic and prognostic marker in glioma, and inhibition of Kindlin-2 may be a novel strategy for glioma treatment. PMID: 27713156
  6. the rs17125944 polymorphism in FERMT2 gene might not be association with late-onset Alzheimer's disease in northern Han Chinese population PMID: 27244899
  7. analysis of the Kindlin-2-RhoGDIalpha-Rac1 signaling axis that is critical for regulation of podocyte structure and function in vivo PMID: 28775002
  8. Study found that FERMT2 (a beta3-integrin co-activator) was significantly associated with a variation in cerebrospinal fluid Abeta peptide levels in 2886 Alzheimer's disease cases.Under-expression of FERMT2 increases Abeta peptide production by raising levels of mature APP at the cell surface and facilitating its recycling PMID: 27933404
  9. High kindlin 2 expression is associated with Breast Cancer. PMID: 28687620
  10. Data suggest that the extreme C terminus of kindlin-2 is essential for interaction with and activation of integrin alphaIIBbeta3; these studies were conducted in macrophage cell line and erythroleukemia cell line. PMID: 28652408
  11. We show a direct relationship between kindlin-1 abundance and UV-B induced apoptosis in keratinocytes, whereas kindlin-2 overexpression has no compensatory effect. PMID: 27798104
  12. The F0 domain of K2 binds actin. PMID: 27044892
  13. data indicate that kindlin-2 promotes the invasiveness of prostate cancer cells largely through NF-kappaB-dependent upregulation of MMP-9 and MMP-2 PMID: 26551397
  14. High kindlin-2 expression is associated with esophageal squamous cell carcinoma. PMID: 25605255
  15. our findings suggested that Kindlin-2 was highly expressed in hepatocellular carcinoma tissues and was closely related to clinical progression. Kindlin-2 protein could be a potential biomarker for predicting poor prognosis of HCC patients after surgery. PMID: 25618552
  16. findings suggest that Src, Kindlin-2 and Migfilin together constitute a positive feedback loop that controls Src activity and regulates integrin-mediated cellular func PMID: 26037143
  17. Data indicate that Kindlin-2 mRNA levels in adult is highly expressed in mesoderm-derived organs. PMID: 24907935
  18. A major ILK binding site in the kindlin-2 FERM domain for regulating cell adhesion has been mapped. PMID: 25160619
  19. the first evidence that interaction between the integrin beta1 cytoplasmic tail and kindlin-2, a member of a family of adapters implicated in human disease pathogenesis, is mainly governed by the beta1 C-terminal carboxylate moiety PMID: 24599960
  20. Kindlin-2 was highly expressed in the peritumoral stroma of pancreatic ductal adenocarcinomas. Stromal kindlin-2 expression was related to nodal metastasis (P = 0.03). PMID: 23508013
  21. Kindlin-2 mediates activation of TGF-beta/Smad signaling and renal fibrosis. PMID: 23723426
  22. Kindlin-2 might promote the invasion of gastric cancer cells through enhancing proliferation and adhesion by the phosphorylation of integrin beta1 and beta3. PMID: 23857544
  23. Kindlin 2 plays a novel role in epigenetic repression of miR-200 family, a mechanism that promotes breast cancer invasion. PMID: 23483548
  24. Kindlin-1 and Kindlin-2 have opposite roles in lung cancers PMID: 23209705
  25. the novel focal adhesion gene kindlin-2 may play an important role in promoting the invasion of gastric cancer cells mediated by tumor-associated macrophages through regulating interleukin expression. PMID: 23151599
  26. A novel regulatory loop has been described between GLI1 and Kindlin-2 that determines cancer cell viability. PMID: 23337877
  27. Kindlin-2 regulates breast cancer progression by inducing genome instability. PMID: 23211537
  28. Low expression of kindlin-2 correlated with a favorable prognosis for acute myeloid leukemia. PMID: 22391155
  29. Kindlin 2 forms a tripartite complex with beta-catenin and TCF4. PMID: 22699938
  30. Kindlin-2 and talin head do not interact with one another but can bind simultaneously to the integrin beta(3) tail without enhancing or inhibiting the interaction of the other binding partner. PMID: 22648415
  31. Kindlin-2 was up-regulated both at RNA (P = .027) and protein levels (P = .014) in gastric cancer tissues and may play an important role in the development and prognosis of gastric cancer. PMID: 22056622
  32. Results define a specific PIP3 recognition mode for the kindlin PH domain and shed light upon a mechanism as to how the PH domain mediates membrane engagement of kindlin-2 to promote integrin activation. PMID: 22030399
  33. a membrane-binding function of the ubiquitin-like domain of kindlin-2, which is likely common for all kindlins, promotes localization to the plasma membrane and controls integrin activation PMID: 22078565
  34. Functional characterization of human Kindlin-2 core promoter identifies a key role of SP1 in Kindlin-2 transcriptional regulation. PMID: 21922223
  35. secondary structures predicted from amino-acid sequence alignment of kindlin PH domains indicated that our crystallized kindlin-2 PH domain has an additional C-terminal helix (alpha-2) which is highly conserved in all three kindlin-family proteins PMID: 21636915
  36. Kindlin-2 is expressed in a small subset of high-grade invasive bladder cancers and may have a role in tumor progression PMID: 21624607
  37. Kindlin-2 regulates podocyte adhesion and fibronectin deposition through interactions with phosphoinositides and integrinb1 and b3. PMID: 21325030
  38. The phenotype of kindlin-1-deficient cells can be modulated by regulating kindlin-2 gene expression and vice versa. PMID: 21356350
  39. physiological role for kindlin-2 in skin fibroblasts under normal steady-state conditions and during tissue regeneration PMID: 20861856
  40. Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation. PMID: 20702409
  41. our study suggests that heightened expression of Kindlin-2 might contribute to tumor progression in MM. PMID: 20127858
  42. cellular functions and possible clinical relevance of kindlin-2 [REVIEW] PMID: 19854292
  43. Mig-2 expression is transcriptionally elevated in leiomyomas and could be involved in its hormone-mediated growth of leiomyomas of the uterus. PMID: 14745725
  44. Results identify kindlin-2 as a novel regulator of integrin beta3 activation; it functions as a coactivator. PMID: 18458155
  45. Loss-of-function mutations in KIND1 result in marked variability in kindlin-1 immunolabeling in Kindler syndrome skin, which is mirrored by similar changes in kindlin-2 and migfilin immunoreactivity. PMID: 18528435

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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.

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