epitope corresponding to amino acids 122-421 mapping within an internal region of EMILIN-5 of human origin
Modification Notes
EMILINs (elastin microfibril interface located proteins) are extracellular matrix glycoproteins that localize to sites with proximity to elastin and microfibrils. They consist of an N-terminal cysteine rich EMI domain and a conserved C-terminal gC1q-like domain. EMILIN-1 is abundant in elastin-rich tissues such as blood vessels, skin, heart and lung. It influences placenta formation and initial organogenesis with a later role in interstitial connective tissue. EMILIN-2 is larger than EMILIN-1 and contains a unique proline-rich domain. It is likely involved in the process of elastogenesis. Multimerin-2 (also known as EMILIN-3 or EndoGlyx-1) is expressed during embryonic development. Multimerin-1 (also known as EMILIN-4) is expressed in platelets and the endothelium of blood vessels and may act as a carrier protein for platelet factor V. EMILIN-5 is encoded by the EMILIN3 gene and is sometimes referred to as EMILIN-3. It contains the N-terminal cysteine rich EMI domain but lacks the C-terminal gC1q-like domain. EMILIN-5 is expressed in human mesenchymal stem cells and plays an important role in skeletal development.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of EMILIN-5 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 122-421 mapping within an internal region of EMILIN-5 of human origin
Tissue Specificity
epitope corresponding to amino acids 122-421 mapping within an internal region of EMILIN-5 of human origin