Name: Recombinant Human Tyrosine-protein kinase HCK(HCK)
Brand: CUSABIO
SKU: 010211HU

Product Details

Purity	>85% (SDS-PAGE)
Target Names	HCK
Uniprot No.	P08631
Alternative Names	Bmk; Hck 1; Hck; HCK_HUMAN; Hemopoietic cell kinase; JTK9; p59-HCK/p60-HCK; p59Hck; p59HCK/p60HCK; p61Hck; Tyrosine protein kinase HCK; Tyrosine-protein kinase HCK
Species	Homo sapiens (Human)
Expression Region	2-526
Target Protein Sequence	GGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ KGDQMVVLEE SGEWWKARSL ATRKEGYIPS NYVARVDSLE TEEWFFKGIS RKDAERQLLA PGNMLGSFMI RDSETTKGSY SLSVRDYDPR QGDTVKHYKI RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP CMSSKPQKPW EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG SKQPLPKLID FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF GLARVIEDNE YTAREGAKFP IKWTAPEAIN FGSFTIKSDV WSFGILLMEI VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE NCPEELYNIM MRCWKNRPEE RPTFEYIQSV LDDFYTATES QYQQQP
Protein Length	Full Length of Mature Protein
Tag Info	The following tags are available. N-terminal His-tagged Tag-Free The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form	Lyophilized powder Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization	Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution	We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs	Protein FAQs
Storage Condition	Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life	The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time	Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time. Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet	Please contact us to get it.

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Target Background

Function	Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS.
Gene References into Functions	HIV infection induced Hck activation.Myeloid cells require Hck for ADAM17 activation and secretion PMID: 29331674 Lysophosphatidylcholines prime polymorphonuclear neutrophil through Hck-dependent activation of PKCdelta, which stimulates PKCgamma, resulting in translocation of phosphorylated p47(phox). PMID: 27531930 HCK represents a novel target for therapeutic development in MYD88-mutated Waldenstrom macroglobulinemia and activated-B cell diffuse large B-cell lymphoma, and possibly other diseases driven by mutated MYD88. PMID: 27143257 High HCK levels correlate with reduced survival of colorectal cancer patients and is associated with activated macrophages gene signature. PMID: 28399411 three-dimensional (3D) QSAR pharmacophore models were generated for Hck based on experimentally known inhibitors. A best pharmacophore model, Hypo1, was developed with high correlation coefficient (0.975), Low RMS deviation (0.60) and large cost difference (49.31), containing three ring aromatic and one hydrophobic aliphatic feature PMID: 27485399 Interaction with the Src homology (SH3-SH2) region of the Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment. PMID: 25122770 Interaction between Nef and Hck is important for Nef-dependent modulation of viral infectivity. PMID: 24051604 The SRC family tyrosine kinase HCK and the ETS family transcription factors SPIB and EHF regulate transcytosis across a human follicle-associated epithelium model. PMID: 23439650 This particular binding mode enables Hck SH3 to sense a specific non-canonical residue situated in the SH3 RT-loop of the kinase. PMID: 22641034 the activation of Hck, Lyn and c-Src by Nef is highly conserved among all major clades of HIV-1 PMID: 22393415 There were significant differences in the genotype and allele distribution of -627 G/T polymorphism in Hck gene between cases and controls. PMID: 22185326 Hck activation at the Golgi apparatus causes the HIV-1 Nef-induced c-Fms proto-oncogene N-glycosylation defect. PMID: 21567396 Loss of HCK is associated with acute promyelocytic leukemia. PMID: 21993313 we show that Hck, has a pre-eminent role in LPS/TLR4-induced TNF and IL-6 production. PMID: 22021612 Hck acts as a key regulator controlling gene expression in alternatively activated monocytes/macrophages. PMID: 21878628 Data show that the structures and relative orientations of the SH2 and SH3 domains down-regulated Hck. PMID: 20810664 Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X. PMID: 20670214 BSS-SAXS reconstruction is used to reveal the structural organization of Hck in solution and the different shifts in the equilibrium population of assembly states upon the binding of different signaling peptides PMID: 20798061 Taken together, PKR and Hck were critical for DON-induced ribosomal recruitment of p38, its subsequent phosphorylation, and, ultimately, p38-driven proinflammatory cytokine expression. PMID: 20181660 Nef participates in HIV-1-induced multinucleated giant cells formation via a p61Hck- and lysosomal enzyme-dependent pathway PMID: 20488787 SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo PMID: 11976726 The interaction of the Bcr-Abl tyrosine kinase with this protein is mediated by multiple binding domains. PMID: 12592324 These results suggest that CSF-induced and HIV-1-mediated regulation of Hck and C/EBPbeta represent the heterogeneous susceptibility of tissue macrophages to HIV-1 infection. PMID: 12900520 SRC kinases LYN & HCK let engaged b2 integrins form focal-adhesion-like structures needed for stable shear-resistant PMN adhesion. SRC-dependent outside-in signalling is needed for integrin adhesiveness triggered by a classical chemoattractant like IL-8. PMID: 14969582 Gab2 docking proteins in IL-6-induced proliferation and survival of multiple myeloma cells. PMID: 15010462 In humans, the cytoplasmic domain of ADAM15v2 strongly interacts with Lck and Hck and regulates leukocyte function. PMID: 15263807 HIV-1 Nef interferes with M-CSF receptor signaling through Hck activation and thereby inhibits M-CSF functions in monocytes/macrophages. PMID: 15626739 data support the existence of multiple active conformations of Src family member Hck kinase that may generate unique downstream signals PMID: 16210316 The free energy surface shows that the N-terminal end of HCK acts as a reversible two-state conformational switch coupling the catalytic domain to the regulatory modules. PMID: 16271895 Data suggest that the insertion/deletion polymorphism could be a functional polymorphism of the Hck gene, may contribute to COPD pathogenesis and modify COPD-related phenotypes. PMID: 17024369 The structure of the HckSH3:PD1 complex reveals novel features of SH3 ligand binding and yields new insights into the structural basics of SH3-ligand interactions. PMID: 17141806 p73 is identified as a novel substrate and interacting partner of Hck and it regulates p73 through mechanisms that are dependent on either catalytic activity or protein interaction domains. PMID: 17535448 hematopoietic cell kinase (hct) phosphorylates fems-like tyrosine kinase 3(FLT3) in the JM region and inhibits its maturation PMID: 17668209 Nef perturbs the intracellular maturation and the trafficking of nascent Fms, through a unique mechanism that required both the activation of Hck and the aberrant spatial regulation of the active Hck PMID: 17893228 Hck has a nonredundant function as a key downstream signaling partner for Bcr-Abl and may represent a potential drug target in CML PMID: 18794796 HCK and BIN1 plays critical roles in AHI-1-mediated leukemic transformation of cutaneous T-Cell Lymphoma. PMID: 19211505 This finding establishes an intriguing link between the pathogenesis of Nef and a newly emerging concept that the Golgi-localized Src kinases regulate the Golgi function. PMID: 19585521 Alternate use of a non-AUG (CUG), and an in-frame, downstream AUG translation initiation codon, results in the production of 2 isoforms in mouse and human. PMID: 1875927 Alternate use of a non-AUG (CUG), and an in-frame, downstream AUG translation initiation codon, results in the production of two isoforms with different subcellular localization. PMID: 10967098 A dominant negative form of Hck, in an interaction that is SH3 domain dependent, blocks HIV-1 Nef induced MHC class I downregulation. PMID: 11500821 Show More Hide All
Involvement in disease	Aberrant activation of HCK by HIV-1 protein Nef enhances HIV-1 replication and contributes to HIV-1 pathogenicity.; DISEASE: Note=Aberrant activation of HCK, e.g. by the BCR-ABL fusion protein, promotes cancer cell proliferation.
Subcellular Location	[Isoform 1]: Lysosome. Membrane; Lipid-anchor. Cell projection, podosome membrane; Lipid-anchor. Cytoplasm, cytosol. Note=Associated with specialized secretory lysosomes called azurophil granules. At least half of this isoform is found in the cytoplasm, some of this fraction is myristoylated.; [Isoform 2]: Cell membrane; Lipid-anchor. Membrane, caveola; Lipid-anchor. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Golgi apparatus. Cytoplasmic vesicle. Lysosome. Nucleus. Note=20% of this isoform is associated with caveolae. Localization at the cell membrane and at caveolae requires palmitoylation at Cys-3. Colocalizes with the actin cytoskeleton at focal adhesions.; Cytoplasmic vesicle, secretory vesicle. Cytoplasm, cytosol.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
Tissue Specificity	Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil.
Database Links	HGNC: 4840 OMIM: 142370 KEGG: hsa:3055 STRING: 9606.ENSP00000365012 UniGene: Hs.655210

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Recombinant Human Tyrosine-protein kinase HCK(HCK)

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Target Background

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