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Mouse Anti-CD44 Recombinant Antibody (BU52) (CBMAB-C2437-CQ)


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Published Data
CBMAB-C2437-CQ-1
Mouse Anti-CD44 Recombinant Antibody (BU52) (CBMAB-C2437-CQ) in IF
Detection of CD44-positive CTCs using double-immunofluorescent staining (×400). CD44 was costained. ...View More
Li, M., Zhang, B., Zhang, Z., Liu, X., Qi, X., Zhao, J., ... & Luo, D. (2014). Stem cell-like circulating tumor cells indicate poor prognosis in gastric cancer. BioMed research international, 2014(1), 981261. Distributed under Open Access license CC BY 3.0, without modification.

Summary

Host Animal
Mouse
Specificity
Human
Clone
BU52
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, FC

Basic Information

Immunogen
Peripheral myeloma cells of human origin.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IF(ICC)1:20-1:100
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% 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.

Target

Full Name
CD44 Molecule (Indian Blood Group)
Introduction
The protein encoded by this gene is a cell-surface glycoprotein involved in cell-cell interactions, cell adhesion and migration. It is a receptor for hyaluronic acid (HA) and can also interact with other ligands, such as osteopontin, collagens, and matrix metalloproteinases (MMPs). This protein participates in a wide variety of cellular functions including lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis. Transcripts for this gene undergo complex alternative splicing that results in many functionally distinct isoforms, however, the full length nature of some of these variants has not been determined. Alternative splicing is the basis for the structural and functional diversity of this protein, and may be related to tumor metastasis.
Entrez Gene ID
960
UniProt ID
P16070
Alternative Names
CD44 Molecule (Indian Blood Group); Hematopoietic Cell E- And L-Selectin Ligand; GP90 Lymphocyte Homing/Adhesion Receptor; Chondroitin Sulfate Proteoglycan 8; Extracellular Matrix Receptor III; Heparan Sulfate Proteoglycan; Phagocytic Glycoprotein 1; Hyaluronate Receptor; Hermes Antigen; CD44 Antigen; ECMR-III; HUTCH-I; Epican; CDW44; MDU2; MDU3;
Function
Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment (PubMed:16541107, PubMed:19703720, PubMed:22726066).
Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection (PubMed:7528188).
Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:18757307, PubMed:23589287).
Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion (PubMed:15123640).
Biological Process
Cartilage development Source: UniProtKB
Cell adhesion Source: UniProtKB
Cell-cell adhesion Source: UniProtKB
Cell-matrix adhesion Source: UniProtKB
Cell migration Source: UniProtKB
Cellular response to fibroblast growth factor stimulus Source: UniProtKB
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: Reactome
Hyaluronan catabolic process Source: UniProtKB
Inflammatory response Source: GO_Central
Interferon-gamma-mediated signaling pathway Source: Reactome
Leukocyte migration Source: Reactome
Monocyte aggregation Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
Negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
Neutrophil degranulation Source: Reactome
Positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
Positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
Positive regulation of monocyte aggregation Source: BHF-UCL
Positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
Positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
Regulation of lamellipodium morphogenesis Source: UniProtKB
T cell activation Source: UniProtKB
Wound healing, spreading of cells Source: UniProtKB
Cellular Location
Cell membrane; Microvillus. Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli. Localizes to cholesterol-rich membrane-bound lipid raft domains.
Topology
Extracellular: 21-649
Helical: 650-670
Cytoplasmic: 671-742
PTM
Proteolytically cleaved in the extracellular matrix by specific proteinases (possibly MMPs) in several cell lines and tumors.
N-glycosylated.
O-glycosylated. O-glycosylation contains more-or-less-sulfated chondroitin sulfate glycans, whose number may affect the accessibility of specific proteinases to their cleavage site(s). It is uncertain if O-glycosylation occurs on Thr-637 or Thr-638.
Phosphorylated; activation of PKC results in the dephosphorylation of Ser-706 (constitutive phosphorylation site), and the phosphorylation of Ser-672.
More Infomation

Liang, Y., Wang, Y., Wang, L., Liang, Z., Li, D., Xu, X., ... & Niu, H. (2021). Self-crosslinkable chitosan-hyaluronic acid dialdehyde nanoparticles for CD44-targeted siRNA delivery to treat bladder cancer. Bioactive materials, 6(2), 433-446.

Al-Othman, N., Alhendi, A., Ihbaisha, M., Barahmeh, M., Alqaraleh, M., & Al-Momany, B. Z. (2020). Role of CD44 in breast cancer. Breast disease, 39(1), 1-13.

Godavarthy, P. S., Kumar, R., Herkt, S. C., Pereira, R. S., Hayduk, N., Weissenberger, E. S., ... & Krause, D. S. (2020). The vascular bone marrow niche influences outcome in chronic myeloid leukemia via the E-selectin-SCL/TAL1-CD44 axis. Haematologica, 105(1), 136.

Zhang, R., Rejeeth, C., Xu, W., Zhu, C., Liu, X., Wan, J., ... & Qian, K. (2019). Label-free electrochemical sensor for cd44 by ligand-protein interaction. Analytical chemistry, 91(11), 7078-7085.

Skandalis, S. S., Karalis, T. T., Chatzopoulos, A., & Karamanos, N. K. (2019). Hyaluronan-CD44 axis orchestrates cancer stem cell functions. Cellular signalling, 63, 109377.

Chen, C., Zhao, S., Karnad, A., & Freeman, J. W. (2018). The biology and role of CD44 in cancer progression: therapeutic implications. Journal of hematology & oncology, 11(1), 1-23.

Morath, I., Jung, C., Lévêque, R., Linfeng, C., Toillon, R. A., Warth, A., & Orian-Rousseau, V. (2018). Differential recruitment of CD44 isoforms by ErbB ligands reveals an involvement of CD44 in breast cancer. Oncogene, 37(11), 1472-1484.

Klement, J. D., Paschall, A. V., Redd, P. S., Ibrahim, M. L., Lu, C., Yang, D., ... & Liu, K. (2018). An osteopontin/CD44 immune checkpoint controls CD8+ T cell activation and tumor immune evasion. The Journal of clinical investigation, 128(12), 5549-5560.

Suleiman, M., Abdulrahman, N., Yalcin, H., & Mraiche, F. (2018). The role of CD44, hyaluronan and NHE1 in cardiac remodeling. Life sciences, 209, 197-201.

Cortes-Dericks, L., & Schmid, R. A. (2017). CD44 and its ligand hyaluronan as potential biomarkers in malignant pleural mesothelioma: evidence and perspectives. Respiratory research, 18(1), 1-12.

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

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