Recombinant Human Dedicator Of Cytokinesis Protein 8 (DOCK8) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03193P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Dedicator Of Cytokinesis Protein 8 (DOCK8) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03193P
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Product Overview

Description Recombinant Human Dedicator Of Cytokinesis Protein 8 (DOCK8) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q8NF50
Target Symbol DOCK8
Synonyms DOCK8Dedicator of cytokinesis protein 8
Species Homo sapiens (Human)
Expression System Yeast
Tag N-6His
Target Protein Sequence RNLLYVYPQRLNFVNKLASARNITIKIQFMCGEDASNAMPVIFGKSSGPEFLQEVYTAVTYHNKSPDFYEEVKIKLPAKLTVNHHLLFTFYHISCQQKQGASVETLLGYSWLPILLNERLQTGSYCLPVALEKLPPNYSMHSAEKVPLQNPPIKWAEGHKGVFNIEVQAV
Expression Range 560-729aa
Protein Length Partial
Mol. Weight 21.3kDa
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 Guanine nucleotide exchange factor (GEF) which specifically activates small GTPase CDC42 by exchanging bound GDP for free GTP. During immune responses, required for interstitial dendritic cell (DC) migration by locally activating CDC42 at the leading edge membrane of DC. Required for CD4(+) T-cell migration in response to chemokine stimulation by promoting CDC42 activation at T cell leading edge membrane. Is involved in NK cell cytotoxicity by controlling polarization of microtubule-organizing center (MTOC), and possibly regulating CCDC88B-mediated lytic granule transport to MTOC during cell killing.
Subcellular Location Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families DOCK family
Database References

HGNC: 19191

OMIM: 243700

KEGG: hsa:81704

STRING: 9606.ENSP00000408464

UniGene: PMID: 28067314

  • A novel DOCK8 sequence insertion caused primary immunodeficiency in two siblings from a consanguineous family. PMID: 26883462
  • DOCK8 deficiency may present severe immune dysregulation with features that may overlap with those of immune dysregulation, polyendocrinopathy, enteropathy, X-linked (IPEX) and other IPEX-like disorders PMID: 29058101
  • Recent advances in the understanding of DOCK8 function are summarized, paying particular attention to an emerging role as a signaling intermediate to promote immune responses to diverse external stimuli. [Review] PMID: 28366940
  • In severe atopic eczema the dermatologist should initially suspect and document a mutation of DOCK8. PMID: 28065530
  • Our results suggest that decreased expression of DOCK8 in response to CRH might disturb the immunosuppressive function of Tregs and contribute to stress-induced aggravation of AD symptoms. PMID: 26799599
  • Sequence analysis identified two copies of missense mutation, c.4346C > T, in the coding region of the DOCK8 gene in a family with 3 patients with autosomal recessive Hyper-IgE syndrome. PMID: 27890707
  • Our results showed that DOCK8-deficient patients have a profound defect in TH17 differentiation related to decreased STAT3 phosphorylation, translocation to the nucleus, and transcriptional activity PMID: 27350570
  • The CD4+ T-cell compartment is greatly altered in the absence of DOCK8. Specifically, DOCK8-deficient patients have increased TH2 cells and defects in TH1 and TH17 cell differentiation PMID: 27554822
  • comparative study provides a long-term observation of DOCK8- and STAT3-hyper-IgE syndrome patients with regard to clinical and laboratory findings, and assesses the activation and cytokine secretion of lymphocytes after in vitro stimulation PMID: 26592211
  • mutations in Chinese patients with hyper-IgE syndrome PMID: 26659092
  • Letter/Case Report: DOCK8 homozygous mutation leading to primary immune deficiency. PMID: 26235511
  • DOCK8 deficiency is likely in patients with severe viral infections, allergies, and/or low IgM levels. PMID: 25724123
  • CD147 has a role in promoting Src-dependent activation of Rac1 signaling through STAT3/DOCK8 during the motility of hepatocellular carcinoma cells PMID: 25428919
  • DOCK8-regulated shape integrity of lymphocytes prevents cytothripsis and promotes antiviral immunity in the skin. PMID: 25422492
  • Dedicator of cytokinesis 8-deficient patients have a breakdown in peripheral B-cell tolerance and defective regulatory T cells PMID: 25218284
  • Mutations of DOCK8 in three children, two of whom developed sclerosing cholangitis, are reported. PMID: 25220305
  • Hyper-IgE syndromes and atopic dermatitis patients showed different sensitization pattern of serum IgE corresponding to the allergic disease manifestations and Th-cell subset data, suggesting a key role of DOCK8 in the development of food allergy PMID: 24898675
  • This is a case of systemic lupus erythematosus with hyper-immunoglobulin E syndrome documented as DOCK8 deficiency. PMID: 25332498
  • Biallelic mutations in the DOCK8 gene cause autosomal-recessive hyper-IgE syndrome. PMID: 24698323
  • Two novel large deletions, del1-14 exons and del8-18 exons, of DOCK8 have been identified in two siblings with the adaptive immune deficiencies. PMID: 23859592
  • DOCK8 is required for the development and survival of mature NKT cells. PMID: 23929855
  • DOCK8 deficiency results in defective antibody responses and undirected plasma cell expansion in the lymph nodes, as part of a combined immunodeficiency cured by hematopoietic stem cell transplantation. PMID: 23891736
  • Clinical features of immunodeficiency syndrome are associated with DOCK8 mutations. (Review) PMID: 23911989
  • We used this new approach to analyse exome data from 24 patients with primary immunodeficiencies. Our analysis identified two novel causative deletions in the genes GATA2 and DOCK8 PMID: 22942019
  • Dedicator of cytokinesis 8 interacts with talin and Wiskott-Aldrich syndrome protein to regulate NK cell cytotoxicity. PMID: 23455509
  • Three novel DOCK8 mutations and two large deletions are found in thirteen patients with autosomal recessive hyper-IgE syndrome in a single center experience. PMID: 22968740
  • DOCK8 deficiency results in severely impaired natural killer cell function because of an inability to form a mature lytic immunologic synapse through targeted synaptic F-actin accumulation PMID: 23380217
  • DOCK8 mediates an MyD88 signaling pathway essential for TLR9-driven B-cell proliferation aand immunoglobulin production. PMID: 22581261
  • DOCK8 encodes dedicator of cytokinesis 8. PMID: 22876580
  • DOCK8 deficiency (a newly described combined primary immunodeficiency disease) accounted for 15% of combined immune deficiency cases in the National Primary Immunodeficiency Disorders Registry in Kuwait, a country with high prevalence of consanguinity. PMID: 22534316
  • Findings help to explain why DOCK8-deficient patients are susceptible to recurrent infections and provide new insights into how T-cell memory is sustained. PMID: 21969276
  • Rates of malignancy and overall mortality in patients with DOCK8 deficiency were higher than in those with Job's syndrome PMID: 21931011
  • These findings highlight a key role for DOCK8 in the survival and function of human and mouse CD8 T cells. PMID: 22006977
  • A 2-bp deletion at codon 510 in exon 14 causing a frameshift mutation was found in 3 homozygous siblings with Job syndrome and their heterozygous first-cousin parents. PMID: 21763205
  • DOCK8 deficiency and clinical manifestations of hyper IgE syndromes (Review) PMID: 21178271
  • Mutations in DOCK8 lead to DOCK8 immunodeficiency syndrome characterized by recurrent viral infections, severe atopy, and early onset malignancy. (Review) PMID: 21178272
  • Several AR-HIES patients have recently been shown to harbour mutations in the gene for dedicator of cytokinesis 8 (DOCK8). Here, we present the long-term outcome of a girl having received a hematopoietic stem cell graft. PMID: 21058221
  • Autosomal-recessive mutations in DOCK8 are responsible for many, although not all, cases of autosomal-recessive hyper-IgE syndrome. PMID: 20004785
  • involvement of DOCK8 in processes that affect the organisation of filamentous actin. PMID: 15304341
  • rare mutations in the DOCK8 gene may contribute to some cases of autosomal dominant mental retardation PMID: 18060736
  • Under-expression of DOCK8 is associated with hepatocellular carcinoma. PMID: 19640199
  • Autosomal recessive DOCK8 deficiency is associated with a novel variant of combined immunodeficiency. PMID: 19776401
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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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