HSP90AA1 Products By Gene Name

LRP-1 autocrine loop" that promotes cell motility. (B) Western blot shows 231-wt and two clones of 231-Hsp90 alpha -knockout (231-alpha -KO) cells (panel a). (C) Anti-Hsp90 alpha antibody blotting of secreted Hsp90 alpha in serum-free conditioned medium (CM, 10X) from 231-wt, 231-alpha -KO (panel c) or 231-LRP-1-KD (panel d) cells. (D) Western blot analysis shows the total Hsp90 alpha level in 231-wt or 231-LRP-1-KD cells under normoxia or hypoxia. (E) Western blot analysis shows the relative levels of LRP-1 in indicated cell lines. (F) CM from 231-wt, but not 231-alpha -KO, cells stimulated B16 melanoma cell migration (panels k and l vs. panel i), with human recombinant (hr) Hsp90 alpha protein (panel j) as positive control. (G) Computer-assisted quantitation of the B16 cell migration shown in panel F as Migration Index (%) (“Methods"). CM from 231-alpha -KO cells completely lost pro-motility activity (panel l). Asterisks indicate significance of the induced migration by indicated stimuli (panels j, k) versus the serum-free control (panel i). (H) The indicated cells were simultaneously compared for their motility under serum-fee conditions. Neither total alpha -KO (panels o and s) nor extracellular blockade of secreted Hsp90 alpha function by mAb1G7-D7 (panels p, t) re-produced the degree of inhibition of cell motility by LRP-1-KD (panels n and u), in reference to 231-wt cells (panels m and q). (L) Computer-assisted quantitation of the cell migration data with indicated panels. Asterisks indicate the significance of indicated cell motility over that of the LRP-1-KD cells. All experiments were repeated multiple times to reach the final conclusion. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35835845), licensed under a CC-BY license. Not internally tested by Novus Biologicals." class="big_lightbox"> LRP-1 autocrine loop" that promotes cell motility. (B) Western blot shows 231-wt and two clones of 231-Hsp90 alpha -knockout (231-alpha -KO) cells (panel a). (C) Anti-Hsp90 alpha antibody blotting of secreted Hsp90 alpha in serum-free conditioned medium (CM, 10X) from 231-wt, 231-alpha -KO (panel c) or 231-LRP-1-KD (panel d) cells. (D) Western blot analysis shows the total Hsp90 alpha level in 231-wt or 231-LRP-1-KD cells under normoxia or hypoxia. (E) Western blot analysis shows the relative levels of LRP-1 in indicated cell lines. (F) CM from 231-wt, but not 231-alpha -KO, cells stimulated B16 melanoma cell migration (panels k and l vs. panel i), with human recombinant (hr) Hsp90 alpha protein (panel j) as positive control. (G) Computer-assisted quantitation of the B16 cell migration shown in panel F as Migration Index (%) (“Methods"). CM from 231-alpha -KO cells completely lost pro-motility activity (panel l). Asterisks indicate significance of the induced migration by indicated stimuli (panels j, k) versus the serum-free control (panel i). (H) The indicated cells were simultaneously compared for their motility under serum-fee conditions. Neither total alpha -KO (panels o and s) nor extracellular blockade of secreted Hsp90 alpha function by mAb1G7-D7 (panels p, t) re-produced the degree of inhibition of cell motility by LRP-1-KD (panels n and u), in reference to 231-wt cells (panels m and q). (L) Computer-assisted quantitation of the cell migration data with indicated panels. Asterisks indicate the significance of indicated cell motility over that of the LRP-1-KD cells. All experiments were repeated multiple times to reach the final conclusion. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35835845), licensed under a CC-BY license. Not internally tested by Novus Biologicals." class="big_thumb" />

LRP-1 autocrine loop" that promotes cell motility. (B) Western blot shows 231-wt and two clones of 231-Hsp90 alpha -knockout (231-alpha -KO) cells (panel a). (C) Anti-Hsp90 alpha antibody blotting of secreted Hsp90 alpha in serum-free conditioned medium (CM, 10X) from 231-wt, 231-alpha -KO (panel c) or 231-LRP-1-KD (panel d) cells. (D) Western blot analysis shows the total Hsp90 alpha level in 231-wt or 231-LRP-1-KD cells under normoxia or hypoxia. (E) Western blot analysis shows the relative levels of LRP-1 in indicated cell lines. (F) CM from 231-wt, but not 231-alpha -KO, cells stimulated B16 melanoma cell migration (panels k and l vs. panel i), with human recombinant (hr) Hsp90 alpha protein (panel j) as positive control. (G) Computer-assisted quantitation of the B16 cell migration shown in panel F as Migration Index (%) (“Methods"). CM from 231-alpha -KO cells completely lost pro-motility activity (panel l). Asterisks indicate significance of the induced migration by indicated stimuli (panels j, k) versus the serum-free control (panel i). (H) The indicated cells were simultaneously compared for their motility under serum-fee conditions. Neither total alpha -KO (panels o and s) nor extracellular blockade of secreted Hsp90 alpha function by mAb1G7-D7 (panels p, t) re-produced the degree of inhibition of cell motility by LRP-1-KD (panels n and u), in reference to 231-wt cells (panels m and q). (L) Computer-assisted quantitation of the cell migration data with indicated panels. Asterisks indicate the significance of indicated cell motility over that of the LRP-1-KD cells. All experiments were repeated multiple times to reach the final conclusion. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35835845), licensed under a CC-BY license. Not internally tested by Novus Biologicals." class="big_lightbox"> LRP-1 autocrine loop" that promotes cell motility. (B) Western blot shows 231-wt and two clones of 231-Hsp90 alpha -knockout (231-alpha -KO) cells (panel a). (C) Anti-Hsp90 alpha antibody blotting of secreted Hsp90 alpha in serum-free conditioned medium (CM, 10X) from 231-wt, 231-alpha -KO (panel c) or 231-LRP-1-KD (panel d) cells. (D) Western blot analysis shows the total Hsp90 alpha level in 231-wt or 231-LRP-1-KD cells under normoxia or hypoxia. (E) Western blot analysis shows the relative levels of LRP-1 in indicated cell lines. (F) CM from 231-wt, but not 231-alpha -KO, cells stimulated B16 melanoma cell migration (panels k and l vs. panel i), with human recombinant (hr) Hsp90 alpha protein (panel j) as positive control. (G) Computer-assisted quantitation of the B16 cell migration shown in panel F as Migration Index (%) (“Methods"). CM from 231-alpha -KO cells completely lost pro-motility activity (panel l). Asterisks indicate significance of the induced migration by indicated stimuli (panels j, k) versus the serum-free control (panel i). (H) The indicated cells were simultaneously compared for their motility under serum-fee conditions. Neither total alpha -KO (panels o and s) nor extracellular blockade of secreted Hsp90 alpha function by mAb1G7-D7 (panels p, t) re-produced the degree of inhibition of cell motility by LRP-1-KD (panels n and u), in reference to 231-wt cells (panels m and q). (L) Computer-assisted quantitation of the cell migration data with indicated panels. Asterisks indicate the significance of indicated cell motility over that of the LRP-1-KD cells. All experiments were repeated multiple times to reach the final conclusion. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35835845), licensed under a CC-BY license. Not internally tested by Novus Biologicals." class="big_thumb" />

HAF007). For additional reference, recombinant human HSP90a and HSP90 beta (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 100 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_lightbox"> HAF007). For additional reference, recombinant human HSP90a and HSP90 beta (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 100 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." alt="Western blot shows lysates of Raji human Burkitt's lymphoma cell line and HeLa human cervical epithelial carcinoma cell line, CH-1 mouse B cell lymphoma cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.25 µg/mL Human/Mouse/Rat HSP90 Monoclonal Antibody (Catalog # MAB3286) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). For additional reference, recombinant human HSP90a and HSP90 beta (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 100 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_thumb" />

HAF017). For additional reference, recombinant human HSP90a and HSP90b (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 96 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_lightbox"> HAF017). For additional reference, recombinant human HSP90a and HSP90b (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 96 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." alt="Western blot shows lysates of Jurkat human acute T cell leukemia cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.5 µg/mL Human/Mouse/Rat HSP90 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3775) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). For additional reference, recombinant human HSP90a and HSP90b (5 ng/lane) were included. A specific band for HSP90 was detected at approximately 96 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_thumb" />

HAF019). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_lightbox"> HAF019). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_thumb" />