Clone:
51D6
Type of antibody:
Primary antibodies
Isotype:
mouse IgG3κ
Applications:
FC
Alternative names:
HGK2, MCK-10, RTK-6, TRK E, DDR, CAK

Specifications for CD167a (DDR1) Antibody, anti-human

Overview

Clone 51D6 recognizes the human CD167a antigen, a single-pass type I membrane protein, which is also known as discoidin domain receptor (DDR1), mammary carcinoma kinase 10 (MCK-10), or tyrosine kinase receptor E (trkE). CD167a is a tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival, and cell proliferation. It promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. CD167a also plays a role in tumor cell invasion. Three isoforms of CD167a have been reported. CD167a is expressed on epithelial cells, keratinocytes, leukocytes, monocytes, and has been reported to be overexpressed in some breast carcinomas.

Alternative names

HGK2, MCK-10, RTK-6, TRK E, DDR, CAK

Detailed product information

Technical specifications

Clone51D6
Clonalitymonoclonal
Isotypemouse IgG3κ
Hostmouse
Type of antibodyPrimary antibodies
Specieshuman
AntigenCD167a (DDR1)
Alternative names of antigenHGK2, MCK-10, RTK-6, TRK E, DDR, CAK
Molecular mass of antigen [kDa]99
Distribution of antigenepithelial cells, monocytes, keratinocytes, breast
Entrez Gene ID780
RRIDAB_2655535, AB_2655534

Resources for CD167a (DDR1) Antibody, anti-human

Certificates

Please follow this
link
to search for Certificates of Analysis (CoA) by lot number.

References for CD167a (DDR1) Antibody, anti-human

Publications

  1. Di Marco, E. et al. (1993) Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues. J. Biol. Chem. 268(32): 2490-2495
  2. Canning, P. et al. (2014) Structural mechanisms determining inhibition of the collagen receptor DDR1 by selective and multi-targeted type II kinase inhibitors. J. Mol. Biol. 426(13): 2457-2470
  3. Hohenester, E. (2014) Signalling complexes at the cell-matrix interface. Curr. Opin. Struct. Biol. 29C: 10-16

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