Mouse Anti-DOCK8 Recombinant Antibody (D1487) (CBMAB-D1487-YC)

Name: Mouse Anti-DOCK8 Recombinant Antibody (D1487)
SKU: CBMAB-D1487-YC
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

D1487

Application

WB, IP, IF, ELISA, IHC-P

Immunogen

Amino acids 119-277 mapping near the N-terminus of human DOCK8.

Host Species

Mouse

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG1, κ

Clonality

Monoclonal Antibody

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
ELISA	1:100-1:1,000
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)	1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

Gelatin & PBS

Preservative

Sodium Azide

Concentration

0.2 mg/ml

Storage

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

dedicator of cytokinesis 8

Introduction

DOCK8 belongs to the DOCK180 family of guanine nucleotide exchange factors. Guanine nucleotide exchange factors interact with Rho GTPases and are components of intracellular signaling networks. Mutations in this gene result in the autosomal recessive form of the hyper-IgE syndrome.

Entrez Gene ID

81704

UniProt ID

Q8NF50

Alternative Names

Dedicator Of Cytokinesis 8; Dedicator Of Cytokinesis Protein 8; Epididymis Luminal Protein 205; 1200017A24Rik; HEL-205; MRD2; ZIR8;

Function

Guanine nucleotide exchange factor (GEF) which specifically activates small GTPase CDC42 by exchanging bound GDP for free GTP (PubMed:28028151, PubMed:22461490).

During immune responses, required for interstitial dendritic cell (DC) migration by locally activating CDC42 at the leading edge membrane of DC (By similarity).

Required for CD4+ T-cell migration in response to chemokine stimulation by promoting CDC42 activation at T cell leading edge membrane (PubMed:28028151).

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 (PubMed:25762780).

Biological Process

Cellular response to chemokine Source: UniProtKB
Dendritic cell migration Source: Ensembl
Immunological synapse formation Source: Ensembl
Memory T cell proliferation Source: MGI
Negative regulation of T cell apoptotic process Source: Ensembl
Positive regulation of establishment of T cell polarity Source: UniProtKB
Positive regulation of GTPase activity Source: UniProtKB
Positive regulation of T cell migration Source: UniProtKB
Regulation of small GTPase mediated signal transduction Source: Reactome
Small GTPase mediated signal transduction Source: InterPro

Cellular Location

Cell membrane; Lamellipodium membrane; Cytoplasm. Enriched and co-localizes with GTPase CDC42 at the immunological synapse formed during T cell/antigen presenting cell cognate interaction. Translocates from the cytoplasm to the plasma membrane in response to chemokine CXCL12/SDF-1-alpha stimulation.

Involvement in disease

Hyper-IgE recurrent infection syndrome 2, autosomal recessive (HIES2):
A rare disorder characterized by immunodeficiency, recurrent infections, eczema, increased serum IgE, eosinophilia and lack of connective tissue and skeletal involvement.
Mental retardation, autosomal dominant 2 (MRD2):
The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration disrupting DOCK8 has been found in a patient with mental retardation and ectodermal dysplasia. A balanced translocation, t(X;9) (q13.1;p24). A genomic deletion of approximately 230 kb in subtelomeric 9p has been detected in a patient with mental retardation. A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.

PTM

In response to chemokine CXCL12/SDF-1-alpha stimulation, phosphorylated by PRKCA/PKC-alpha which promotes DOCK8 dissociation from LRCH1.

Pillay, B. A., Fusaro, M., Gray, P. E., Statham, A. L., Burnett, L., Bezrodnik, L., ... & Ma, C. S. (2021). Somatic reversion of pathogenic DOCK8 variants alters lymphocyte differentiation and function to effectively cure DOCK8 deficiency. The Journal of clinical investigation, 131(3).

Eken, A., Cansever, M., Okus, F. Z., Erdem, S., Nain, E., Azizoglu, Z. B., ... & Patiroglu, T. (2020). ILC3 deficiency and generalized ILC abnormalities in DOCK8‐deficient patients. Allergy, 75(4), 921-932.

Aydin, S. E., Freeman, A. F., Al-Herz, W., Al-Mousa, H. A., Arnaout, R. K., Aydin, R. C., ... & Albert, M. H. (2019). Hematopoietic stem cell transplantation as treatment for patients with DOCK8 deficiency. The Journal of Allergy and Clinical Immunology: In Practice, 7(3), 848-855.

Kim, D., Uner, A., Saglam, A., Chadburn, A., & Crane, G. M. (2019). Peripheral eosinophilia in primary immunodeficiencies of actin dysregulation: a case series of Wiskott-Aldrich syndrome, CARMIL2 and DOCK8 deficiency and review of the literature. Annals of Diagnostic Pathology, 43, 151413.

Tirosh, O., Conlan, S., Deming, C., Lee-Lin, S. Q., Huang, X., Su, H. C., ... & Kong, H. H. (2018). Expanded skin virome in DOCK8-deficient patients. Nature medicine, 24(12), 1815-1821.

Kearney, C. J., Randall, K. L., & Oliaro, J. (2017). DOCK8 regulates signal transduction events to control immunity. Cellular & molecular immunology, 14(5), 406-411.

Biggs, C. M., Keles, S., & Chatila, T. A. (2017). DOCK8 deficiency: insights into pathophysiology, clinical features and management. Clinical Immunology, 181, 75-82.

Alroqi, F. J., Charbonnier, L. M., Keles, S., Ghandour, F., Mouawad, P., Sabouneh, R., ... & Chatila, T. A. (2017). DOCK8 deficiency presenting as an IPEX-like disorder. Journal of clinical immunology, 37(8), 811-819.

Yamamura, K., Uruno, T., Shiraishi, A., Tanaka, Y., Ushijima, M., Nakahara, T., ... & Fukui, Y. (2017). The transcription factor EPAS1 links DOCK8 deficiency to atopic skin inflammation via IL-31 induction. Nature communications, 8(1), 1-13.

Janssen, E., Kumari, S., Tohme, M., Ullas, S., Barrera, V., Tas, J. M., ... & Geha, R. S. (2017). DOCK8 enforces immunological tolerance by promoting IL-2 signaling and immune synapse formation in Tregs. JCI insight, 2(19).

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

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