Recombinant Human Kinesin-1 Heavy Chain (KIF5B) Protein (His)

Name: Recombinant Human Kinesin-1 Heavy Chain (KIF5B) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06275P
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 Kinesin-1 Heavy Chain (KIF5B) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P33176
Target Symbol	KIF5B
Synonyms	(Conventional kinesin heavy chain)(Ubiquitous kinesin heavy chain)(UKHC)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTIQWLENELNRWRNGETVPIDEQFDKEKANLEAFTVDKDITLTNDKPATAIGVIGNFTDAERRKCEEEIAKLYKQ
Expression Range	1-431aa
Protein Length	Partial
Mol. Weight	54.9 kDa
Research Area	Cancer
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	Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes. Can induce formation of neurite-like membrane protrusions in non-neuronal cells in a ZFYVE27-dependent manner. Regulates centrosome and nuclear positioning during mitotic entry. During the G2 phase of the cell cycle in a BICD2-dependent manner, antagonizes dynein function and drives the separation of nuclei and centrosomes. Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation. Through binding with PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus ends (Probable). Involved in NK cell-mediated cytotoxicity. Drives the polarization of cytolytic granules and microtubule-organizing centers (MTOCs) toward the immune synapse between effector NK lymphocytes and target cells.
Subcellular Location	Cytoplasm, cytoskeleton. Cytolytic granule membrane. Lysosome membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families	TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin subfamily
Database References	HGNC: 6324 OMIM: 602809 KEGG: hsa:3799 STRING: 9606.ENSP00000307078 UniGene: PMID: 30015159 the discovery of kinesore, a small molecule that in vitro inhibits kinesin-1 interactions with short linear peptide motifs found in organelle-specific cargo adaptors, yet activates kinesin-1's function of controlling microtubule dynamics in cells, demonstrating that these functions are mechanistically coupled. PMID: 29229862 HIV-1 did not stimulate widespread FEZ1 phosphorylation but, instead, bound microtubule (MT) affinity-regulating kinase 2 (MARK2) to stimulate FEZ1 phosphorylation on viral cores. PMID: 28930676 Study demonstrate that the kinesin and kinase domains of KIF5B-RET act together to establish an emergent microtubule and RAB-vesicle-dependent RET-SRC-EGFR-FGFR signaling hub. Study demonstrate that drugs designed to inhibit RET alone work poorly in KIF5B-RET-transformed cells. PMID: 28877471 In particular, counteracting forces between minus-end-directed kinesin-14 and plus-end-directed kinesin-5 motors have recently been implicated in the regulation of microtubule nucleation. PMID: 28668932 The studies describing the interplay between kinesin-1 and cytoplasmic dynein in the translocation of microtubules are discussed. PMID: 28284467 Utilizing novel electron cryomicroscopy methods, the authors solved structures of microtubule-attached, dimeric kinesin bound to an ATP analog. They find that under these conditions, the kinesin dimer can attach to the microtubule with either one or two motor domains. PMID: 28504639 cargo recognition and concurrent activation of kinesin-1 proceed in hierarchical stepwise fashion driven by a dynamic network of inter- and intra-molecular interactions. PMID: 28302907 BORC and Arl8 function upstream of two structurally distinct kinesin types: kinesin-1 (KIF5B) and kinesin-3 (KIF1Bbeta and KIF1A). PMID: 27851960 KIF5B gene rearrangement plays a role in the pathogenesis of papillary thyroid cancer. PMID: 28911147 compared to those of brain, on MCF7 microtubules, kinesin-1's processivity is significantly reduced although its velocity is only slightly altered PMID: 25450690 these observations identify a previously unappreciated role for KIF5B in mediating the Nup358 dependent nuclear import of the HIV-1 viral genome during infection. PMID: 27327622 For Fat3, the Kif5-ID is regulated by alternative splicing, and the timecourse of splicing suggests that the distribution of Fat3 may switch between early and later stages of retinal development. In contrast, P75NTR binding to Kif5B is enhanced by tyrosine phosphorylation and thus has the potential to be dynamically regulated on a more rapid time scale PMID: 27788242 Data suggest that light-chain subunits/fragments of kinesin-1 inhibit the pathological aggregation of amyloid(beta). PMID: 26991731 In this work, we performed normal mode analysis with elastic network model using different conformation of kinesin to determine the effect of tail binding. PMID: 25676575 KIF5B is essential for Ostm1 intracellular dispersion. PMID: 26598607 differences between the structural kinetics of Eg5 and kinesin-1 yield insights into how these two motors adapt their enzymologies for their distinct functions PMID: 26627252 data suggest one-step screening platform for KIF5B-RET as well as EGFR, K-RAS, ALK oncogenic mutations be necessary for lung adenocarcinoma patients PMID: 26268359 Kinesin-1 is primarily front-head gated, and its neck linker length is tuned to enhance unidirectional processivity and velocity. PMID: 25902401 the front head of a kinesin dimer is gated by the backward orientation of its neck linker until the rear head releases from the microtubule PMID: 25818289 Myo1c significantly increases the frequency of kinesin-1-driven microtubule-based runs that begin at actin/microtubule intersections. The actin-binding protein tropomyosin 2 abolishes Myo1c-specific effects on both run initiation and run termination. PMID: 25660542 A novel role of KIF5B was shown in the spatial regulation of Cdo-BNIP-2-p38MAPK signaling and discloses a previously unappreciated linkage between the intracellular transporting system and myogenesis regulation. PMID: 25378581 This study has provided a comprehensive structural and dynamic picture of kinesin's major ATPase states. PMID: 25537000 nesprin-dependent recruitment of kinesin-1 to the nuclear envelope through the interaction of a conserved LEWD motif with kinesin light chain might be a general mechanism for cell-type-specific nuclear positioning during development. PMID: 25516977 Authors find that pharmacological or small interfering RNA (siRNA)-mediated inhibition of cytoplasmic dynein or the kinesin 1 heavy chain KIF5B delays HIV-1 uncoating. PMID: 25231297 Our data suggest that KIF5B-RET promotes the cell growth and tumorigenicity of non-small cell lung cancers through multilevel activation of STAT3 signaling, providing possible strategies for the treatment of KIF5B-RET positive lung cancers. PMID: 25047660 Kinesin-1 transports c-MYC for proteasomal degradation in the cytoplasm. PMID: 24821626 Anti-oncogenic miR-203 had a pivotal role in melanoma through reducing melanosome transport and promoting melanogenesis by targeting kif5b and through negative regulation of the CREB1/MITF/Rab27a pathway. PMID: 23884313 when cargo is transported by both dynein and phosphorylated kinesin, a common occurrence in the cell, there may be a bias that favors motion toward the minus-end of microtubules. PMID: 24072715 Patients without KIF5B-RET fusions had a better prognosis than those with KIF5B-RET fusions (median survival, 52.6 months vs 21.0 months). PMID: 23378251 Study found the secretion of calu-1/2-EGFP required microtubule integrity, and that calu-1/2-EGFP-containing vesicles were transported by the motor proteins Kif5b and cytoplasmic dynein. PMID: 22514732 Nesca directly binds KIF5B, kinesin light-chain and syntaxin-1 PMID: 22404429 Expression of exogenous KIF5B-RET, induced morphological transformation and anchorage-independent growth of NIH3T3 fibroblasts PMID: 22327624 Data indicate that mutant KIF5B kinesin-1 binds ATP similarly in the presence of either metal ion, but its ATP hydrolysis activity is greatly diminished in the presence of Mg(2+). PMID: 22198464 Arl8 and SKIP are required for lysosomes to distribute away from the microtubule-organizing center. We identify two kinesin light chain binding motifs in SKIP that are required for lysosomes to accumulate kinesin-1 and redistribute to the cell periphery. PMID: 22172677 Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection. PMID: 21925109 findings show a bipartite tryptophan-based motif in vaccinia virus A36 is required for kinesin-1-dependent transport of the virus; bioinformatic analysis reveals that related bipartite tryptophan-based motifs are present in over 450 human proteins PMID: 21915095 The conventional kinesin-microtubule binding free energy is dominated by van der Waals interactions and electrostatic interactions. PMID: 21910419 The discovery of the novel KIF5B-ALK variant further consolidated the role of aberrant anaplastic lymphoma kinase signaling in lung carcinogenesis. PMID: 21656749 the interaction between the kinesin-1 head and its regulatory tail domain PMID: 19348763 a kinesin-1 tail fragment associates with microtubules with submicromolar affinity and binding is largely electrostatic PMID: 20071331 This indicates that kinesin-1 facilitates the transport of SNAP-25 containing vesicles as a prerequisite to SNAP-25 driven membrane fusion events. PMID: 19913510 Na,K-ATPase traffic toward the plasma membrane in alveolar epithelial cells is driven by kinesin-1, where KLC2 is the isoform regulating this process. PMID: 19773350 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis PMID: 12191989 With residues 814-963 of human ubiquitous kinesin heavy chain (uKHC) used as bait, a synaptosome-associated protein of 25 kDa (SNAP25) has been identified as a kinesin-binding protein in a human brain cDNA library. PMID: 12475239 Results identify the ribosome receptor, p180, as a binding partner of the kinesin heavy chain isoform KIF5B. PMID: 15184079 CRMP-2 transports the Sra-1/WAVE1 complex to axons in a kinesin-1-dependent manner and thereby regulates axon outgrowth and formation PMID: 16260607 Demonstrates the utility of screening for PDGFRA kinase domain overexpression in patients with IHES and has identified KIF5B as a third PDGFRA fusion partner in chronic myeloproliferative disorders. PMID: 16498388 binding of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function PMID: 17887960 We demonstrate that KIF5B mediates post-Golgi transport of an apical protein in epithelial cells, but only after polarity has developed. PMID: 17925227

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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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