Recombinant Human Tyrosine-Protein Kinase Fer (FER) Protein (His)

Name: Recombinant Human Tyrosine-Protein Kinase Fer (FER) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07408P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Tyrosine-Protein Kinase Fer (FER) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P16591
Target Symbol	FER
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VILGELLGKGNFGEVYKGTLKDKTSVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVSGGDFLTFLRRKKDELKLKQLVKFSLDAAAGMLYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQHCPEDISKIMMKCWDYKPENRPKFSELQKELTI
Expression Range	563-816aa
Protein Length	Partial
Mol. Weight	33.0 kDa
Research Area	Cell Biology
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	Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus.
Subcellular Location	Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell junction. Membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Note=Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily
Database References	HGNC: 3655 OMIM: 176942 KEGG: hsa:2241 STRING: 9606.ENSP00000281092 UniGene: PMID: 29038547 We propose a model for the regulation of Fer based on an intramolecular interaction and the curvature-dependent membrane binding mediated by its intrinsically disordered region. PMID: 29208465 Many human tumor types and cancer cell lines express the MAN2A1-FER fusion, which increases proliferation and invasiveness of cancer cell lines and has liver oncogenic activity in mice. PMID: 28245430 Fer serves as a crucial mediator and amplifier of Src-induced tumor progression. PMID: 25867068 FER encodes a cytosolic non-receptor tyrosine kinase that influences neutrophil chemotaxis and endothelial permeability. PMID: 25533491 Fer contributes to aberrant androgen receptor signaling via pSTAT3 cross-talk during castrate-resistant prostate cancer progression. PMID: 23906537 Detection of PJA2-FER fusion mRNA is correlated with poor postoperative survival periods in non-small cell lung cancer. PMID: 23931849 data show that Fer kinase is elevated in non-small cell lung cancer tumors and is important for cellular invasion and metastasis PMID: 23699534 FER kinase promotes breast cancer metastasis by regulating alpha6- and beta1-integrin-dependent cell adhesion and anoikis resistance. PMID: 23873028 Fer expression correlates with renal cell carcinoma cell proliferation both in vitro and in vivo, and with tumor progression and survival PMID: 23445469 Fer, a non-receptor-type tyrosine kinase, plays a critical role in synthesis of the laminin-binding glycans on alpha-DG. PMID: 22238358 Transcription of the ferT gene in CC cells was found to be driven by an intronic promoter residing in intron 10 of the fer gene and to be regulated by the Brother of the Regulator of Imprinted Sites (BORIS) transcription factor. PMID: 22223638 The A allele of SNP rs10447248 in the FER locus was nominally associated with lower MMW (P = 0.016) but was not associated with LMW (P > 0.05) adiponectin levels PMID: 21700879 Overexpression of FER from a cDNA confers quinacrine resistance to several different types of cancer cell lines. PMID: 21518868 tyrosine phosphorylation of RhoGDIalpha by Fer as a mechanism to regulate binding of RhoGDIalpha to Rac PMID: 21122136 FER plays a role in the invasion and metastasis of hepatocellular carcinoma cells. PMID: 19835603 Closing in on the biological functions of Fps/Fes and Fer. A review. PMID: 11994747 Fps/Fes and Fer are expressed in human and mouse platelets, and are activated following stimulation with collagen and collagen-related peptide (CRP), suggesting a role in GPVI receptor signaling PMID: 12871378 Fer is a regulator of cell-cycle progression in malignant cells and a potential target for cancer intervention. PMID: 16732323 FerT coexist in the acroplaxome with phosphorylated cortactin, a regulator of F-actin dynamics[Fer testis ] PMID: 18985748 Fer tyrosine kinase level correlates with the development of prostate cancer and aggressiveness of prostate cancer cell lines PMID: 19147545 Results suggest that Fer may allow a bypass of focal adhesion kinase-related cell anchorage dependency for intracellular signal transduction in hepatocytes. PMID: 19339212 Overexpression of Fer enhanced lamellipodia formation and cell migration in a manner dependent on PLD activity and the PA-FX interaction. PMID: 19738202

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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.