Human PlGF Antibody

Catalog #: MAB2643 Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
MAB2643-100
MAB2643-SP

PlGF in MDA‑MB‑231 human breast cancer cell line.

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Human PlGF Antibody Summary

Species Reactivity

Human

Specificity

Detects human PIGF in direct ELISAs.

Source

Monoclonal Mouse IgG_2B Clone # 1038864

Purification

Protein A or G purified from hybridoma culture supernatant

Immunogen

E. coli-derived human PlGF
Ala21-Arg149
Accession # P49763-2

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Label

Unconjugated

Applications

Recommended Concentration

Sample

Immunocytochemistry

8-25 µg/mL

Immersion fixed MDA‑MB‑231 human breast cancer cell line

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Immunocytochemistry

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PlGF in MDA‑MB‑231 human breast cancer cell line. PlGF was detected in immersion fixed MDA‑MB‑231 human breast cancer cell line (positivie staining) and K562 human chronic myelogenous leukemia cell line (negative staining) using Mouse Anti-Human PlGF Monoclonal Antibody (Catalog # MAB2643) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. Staining was performed using our protocol for Fluorescent ICC Staining of Non-adherent Cells.

Reconstitution Calculator

Preparation and Storage

Reconstitution

Reconstitute at 0.5 mg/mL in sterile PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: PlGF

Placenta Growth Factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines (1, 2). Alternative splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively (1, 2). Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus (1). Human PlGF-1 shares 56%, 55%, 74% and 95% aa identity with the comparable isoform of mouse, rat, canine, and equine PlGF, respectively. PlGF is mainly found as variably glycosylated, secreted, 55-60 kDa disulfide linked homodimers (3). Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes, and some endothelial cells (1, 4-6). Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia (7). However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia (8). PlGF binds and signals through VEGF R1/Flt-1 but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis (1, 4, 8, 9). However, PlGF (especially PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2 (3, 4). PlGF-2, but not PLGF-1, shows heparin-dependent binding of Neuropilin (Npn)-1 and Npn-2 (10, 11). PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound, bone fracture, and cardiac repair, but also contribute to inflammation in active sickle cell disease and atherosclerosis (5, 6, 8, 12-15). PlGF can also inhibit TIMP3 expression in the spleen, leading to immune triggering of hypertension (16).

References

Hauser, S. and H.A. Weich (1993) Growth Factors 9:259.
Maglione, D. et al. (1993) Oncogene 8:925.
Eriksson, A. et al. (2002) Cancer Cell 1:99.
Ribatti, D. (2008) Angiogenesis 11:215.
Oura, H. et al. (2003) Blood 101:560.
Roncal, C. et al. (2010) Cardiovasc. Res. 86:29.
Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
Carmeliet, P. et al. (2001) Nat. Med. 7:575.
Autiero, M. et al. (2003) Nat. Med. 9:936.
Migdal, M. et al. (1998) J. Biol. Chem. 273:22272.
Cheng, L. et al. (2004) J. Biol. Chem. 279:30654.
Perelman, N. et al. (2003) Blood 102:1506.
Cianfarani, F. et al. (2006) Am. J. Pathol. 169:1167.
Maes, C. et al. (2006) J. Clin. Invest. 116:1230.
Iwasaki, H. et al. (2011) PLoS One 6:e24872.
Carnevale, D. et al. (2014) Immunity 41:737.

Long Name

Placenta Growth Factor

Entrez Gene IDs

5228 (Human); 18654 (Mouse)

Alternate Names

D12S1900; PGF; PGFL; placenta growth factor; placental growth factor; placental growth factor, vascular endothelial growth factor-related protein; PlGF; PlGF-2; PLGFplacental growth factor-like; SHGC-10760