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Proteintech anti sar1a
Anti Sar1a, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+sar1a/SAR1A+Antibody/pmc11303508-242-42-46
Average 92 stars, based on 13 article reviews

anti sar1a - by Bioz Stars, 2026-10

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Article Title: Selenoprotein K contributes to CD36 subcellular trafficking in hepatocytes by accelerating nascent COPII vesicle formation and aggravates hepatic steatosis.
Article Snippet: The following primary antibodies were used: anti-CD36 (1:2000; #NB400-144, Novus Biologicals), anti-β actin (1:3000, #20536-1-AP, Proteintech), anti-SelK (1:2000; #ab139949, Abcam), anti-Calnexin (1:2000; #2679S, Cell Signaling Technology), anti-GM130 (1:2000; #11308-1-AP, Proteintech), antiTGN46 (1:2000; #MA3-063, Invitrogen), anti-Caveolin-1 (1:2000; #16447-1-AP, Proteintech), anti-SAR1A (1:1000; #15350-1-AP, Proteintech), anti-SAR1B (1:1000; #22292-1-AP, Proteintech), anti-TFG (1:1000; #11571-1-AP, Proteintech), anti-SEC24 (1:1000; #15958-1- AP, Proteintech), anti-SEC13 (1:1000; #15397-1-AP, Proteintech), antiSEC31A (1:1000; #17913-1-AP, Proteintech), anti-SEC12 (1:1000; #10146-2-AP, Proteintech), anti-SEC23 (1:1000; # A12101, ABclonal), anti-GAPDH (1:5000; #60004-1-Ig, Proteintech).

Article Title: Small GTPase ActIvitY ANalyzing (SAIYAN) system: A method to detect GTPase activation in living cells
Article Snippet: The Sec24D antibody (RRID: N/A) was gifted by Schekman Lab. Other antibodies used in this study were as follows: anti-GAPDH (Cat# sc-32233, RRID:AB_627679; Santa Cruz Biotechnology), anti-FLAG (Cat# F1804, RRID:AB_262044; Sigma-Aldrich) or anti-FLAG (Cat# 200473, RRID:AB_10596510; Agilent), anti-HA (Cat# 11867423001, RRID:AB_390918; Roche), anti-Sar1A (Cat# 22291-1-AP, RRID:AB_2879062; Proteintech), anti-ERK1 (Cat# sc-271269, RRID:AB_10611091; Santa Cruz Biotechnology), anti-calnexin (Cat# 610523, RRID:AB_397883; BD Biosciences), anti-Sec31A (Cat# 612350, RRID:AB_399716; BD Biosciences), anti-Sec24B (Cat# 12042, RRID:AB_2797807; Cell Signaling Technology), anti-p125A (Sec23IP, Cat# 20892-1-AP, RRID:AB_10896458; Proteintech), anti-collagen I (Cat# SP1.D8, RRID:AB_528438; DSHB), anti-β-COP (Cat# G6160, RRID:AB_477023; Sigma-Aldrich), anti-ERGIC53 (Cat# sc-398893, RRID:AB_2905549; Santa Cruz Biotechnology), anti-Rab1a (Cat# 13075, RRID:AB_2665537; Cell Signaling Technology), anti-GM130 (Cat# 610823, RRID:AB_398142; BD Biosciences), and anti-PDI (Cat# ab2792, RRID:AB_303304; Abcam).

Article Title: Selenoprotein K contributes to CD36 subcellular trafficking in hepatocytes by accelerating nascent COPII vesicle formation and aggravates hepatic steatosis
Article Snippet: The following primary antibodies were used: anti-CD36 (1:2000; #NB400-144, Novus Biologicals), anti-β actin (1:3000, #20536-1-AP, Proteintech), anti-SelK (1:2000; #ab139949, Abcam), anti-Calnexin (1:2000; #2679S, Cell Signaling Technology), anti-GM130 (1:2000; #11308-1-AP, Proteintech), anti-TGN46 (1:2000; #MA3-063, Invitrogen), anti-Caveolin-1 (1:2000; #16447-1-AP, Proteintech), anti-SAR1A (1:1000; #15350-1-AP, Proteintech), anti-SAR1B (1:1000; #22292-1-AP, Proteintech), anti-TFG (1:1000; #11571-1-AP, Proteintech), anti-SEC24 (1:1000; #15958-1-AP, Proteintech), anti-SEC13 (1:1000; #15397-1-AP, Proteintech), anti-SEC31A (1:1000; #17913-1-AP, Proteintech), anti-SEC12 (1:1000; #10146-2-AP, Proteintech), anti-SEC23 (1:1000; # A12101, ABclonal), anti-GAPDH (1:5000; #60004-1-Ig, Proteintech).

Article Title: Small GTPase ActIvitY ANalyzing (SAIYAN) system: A method to detect GTPase activation in living cells.
Article Snippet: Small GTPases are essential in various cellular signaling pathways, and detecting their activation within living cells is crucial for understanding cellular processes.. The current methods for detecting GTPase activation using fluorescent proteins rely on the interaction between the GTPase and its effector.. Consequently, these methods are not applicable to factors, such as Sar1, where the effector also functions as a GTPase-activating protein.

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Loss of functional Sar1 GTPase inhibits ER NKCC2 export. ( A , B ) representative immunoblot showing the effect of overexpressing WT Sar1 or its dominant negative (DN Sar1) Sar1 H79G on NKCC2 processing. ( A ) HEK cells were transfected with NKCC2 alone or with WT Sar1 or DN Sar1. 48 h post-transfection, total cell extract from each sample was run on a parallel SDS gel and immunoblotted for total NKCC2 using Myc antibody. Middle panel, the same membrane stained with Ponceau S to illustrate the equal loading of protein extracts. Lower panel, Representative immunoblot illustrating the expression of endogenous Sar1 (control) and transfected WT Sar1 and its dominant negative in HEK cells. Sar1 proteins were detected using anti-Sar1A antibodies. ( B ) Quantitative analysis of the maturation efficiency of NKCC2 in the presence or absence of WT Sar1 or DN Sar1 in HEK cells, estimated as the ratio of the mature vs. immature form of the cotransporter. Data are expressed as percentage of control ± S.E. NKCC2 alone n = 3. NKCC2 with WT Sar1, n = 4. NKCC2 with DN Sar1, n = 4. # p < 0.0001 versus NKCC2 alone. * p < 0.0005 versus WT Sar1. ( C ) Representative immunoblot illustrating the effect of DN Sar1 in OKP cells. Lower panel, Quantitative analysis of the maturation efficiency of NKCC2 with or without WT Sar1 or DN Sar1 in OKP cells. Each point represents mean ± S.E of four independent experiments. # p < 0.02 versus NKCC2 alone. * p < 0.007 versus WT Sar1. ( C ) Comparison between the effects of mutating the 1019 DAELE 1023 motif and DN Sar1 on NKCC2 subcellular distribution. HEK cells transfected with mutated Myc-NKCC2 proteins as indicated, or with WT NKCC2 alone in the presence or absence of WT Sar1 or DN Sar1, were stained with mouse anti-Myc (Texas Red; red) and rabbit anti-calnexin (FITC; green). The yellow color indicates overlap between the Myc tag of NKCC2 protein (red) and the ER marker (green), representing co-localization of the proteins. Bars, 10 μm.

Journal: International Journal of Molecular Sciences

Article Title: Diacidic Motifs in the Carboxyl Terminus Are Required for ER Exit and Translocation to the Plasma Membrane of NKCC2

doi: 10.3390/ijms232112761

Figure Lengend Snippet: Loss of functional Sar1 GTPase inhibits ER NKCC2 export. ( A , B ) representative immunoblot showing the effect of overexpressing WT Sar1 or its dominant negative (DN Sar1) Sar1 H79G on NKCC2 processing. ( A ) HEK cells were transfected with NKCC2 alone or with WT Sar1 or DN Sar1. 48 h post-transfection, total cell extract from each sample was run on a parallel SDS gel and immunoblotted for total NKCC2 using Myc antibody. Middle panel, the same membrane stained with Ponceau S to illustrate the equal loading of protein extracts. Lower panel, Representative immunoblot illustrating the expression of endogenous Sar1 (control) and transfected WT Sar1 and its dominant negative in HEK cells. Sar1 proteins were detected using anti-Sar1A antibodies. ( B ) Quantitative analysis of the maturation efficiency of NKCC2 in the presence or absence of WT Sar1 or DN Sar1 in HEK cells, estimated as the ratio of the mature vs. immature form of the cotransporter. Data are expressed as percentage of control ± S.E. NKCC2 alone n = 3. NKCC2 with WT Sar1, n = 4. NKCC2 with DN Sar1, n = 4. # p < 0.0001 versus NKCC2 alone. * p < 0.0005 versus WT Sar1. ( C ) Representative immunoblot illustrating the effect of DN Sar1 in OKP cells. Lower panel, Quantitative analysis of the maturation efficiency of NKCC2 with or without WT Sar1 or DN Sar1 in OKP cells. Each point represents mean ± S.E of four independent experiments. # p < 0.02 versus NKCC2 alone. * p < 0.007 versus WT Sar1. ( C ) Comparison between the effects of mutating the 1019 DAELE 1023 motif and DN Sar1 on NKCC2 subcellular distribution. HEK cells transfected with mutated Myc-NKCC2 proteins as indicated, or with WT NKCC2 alone in the presence or absence of WT Sar1 or DN Sar1, were stained with mouse anti-Myc (Texas Red; red) and rabbit anti-calnexin (FITC; green). The yellow color indicates overlap between the Myc tag of NKCC2 protein (red) and the ER marker (green), representing co-localization of the proteins. Bars, 10 μm.

Article Snippet: The primary antibodies used in this study were mouse anti–Myc (Takara, Clontech, Saint-Germain-en-Laye, France) and anti-Sar1A (Invitrogen).

Techniques: Functional Assay, Western Blot, Dominant Negative Mutation, Transfection, SDS-Gel, Staining, Expressing, Marker

Differential expression of Sar1a between NF and HTSF. Isolated NFs or HTSFs were cultured in 6-well plates. The cell culture supernatant was collected for PC-I ELISA (c), and cell lysates were immunoblotted with antibodies against the indicated proteins (a). (a) Immunoblots of Col-1A, α-SMA, CTGF, Sar1a, Sar1b, Sec23, Sec24, Sec13, Sec31, Sec12p, and the loading control GAPDH. (b) Fold change of Sar1a was calculated ( n = 3, ±SD); ** p < 0.01 vs NF 1. (c) NF or HTSF were cultured until near confluence, and they were then starved in serum-free DMEM for 24 h. Secreted PC-I was determined via ELISA ( n = 3, ±SD); ** p < 0.01 and *** p < 0.001 vs NF 1. (d) Cultured cells were stained with anti-Sar1a (FITC, green) and DAPI (blue), and images were obtained using a fluorescence microscope (Scale bar: 10 μm). (e) Images were captured, and the fluorescence intensity was quantitated using ImageJ software ( n = 3, ±SD); * p < 0.05 and ** p < 0.01 vs NF 1.

Journal: Open Medicine

Article Title: TGF-β1 upregulates Sar1a expression and induces procollagen-I secretion in hypertrophic scarring fibroblasts

doi: 10.1515/med-2022-0543

Figure Lengend Snippet: Differential expression of Sar1a between NF and HTSF. Isolated NFs or HTSFs were cultured in 6-well plates. The cell culture supernatant was collected for PC-I ELISA (c), and cell lysates were immunoblotted with antibodies against the indicated proteins (a). (a) Immunoblots of Col-1A, α-SMA, CTGF, Sar1a, Sar1b, Sec23, Sec24, Sec13, Sec31, Sec12p, and the loading control GAPDH. (b) Fold change of Sar1a was calculated ( n = 3, ±SD); ** p < 0.01 vs NF 1. (c) NF or HTSF were cultured until near confluence, and they were then starved in serum-free DMEM for 24 h. Secreted PC-I was determined via ELISA ( n = 3, ±SD); ** p < 0.01 and *** p < 0.001 vs NF 1. (d) Cultured cells were stained with anti-Sar1a (FITC, green) and DAPI (blue), and images were obtained using a fluorescence microscope (Scale bar: 10 μm). (e) Images were captured, and the fluorescence intensity was quantitated using ImageJ software ( n = 3, ±SD); * p < 0.05 and ** p < 0.01 vs NF 1.

Article Snippet: Antibodies against CTGF, Sar1a, Sar1b, Sec13, Sec31a (Santa Cruz, Dallas, TX, USA), Sec23a, Sec24a (Abcam, Cambridge, UK), JNK, p-JNK, ERK, p-ERK, p38, p-p38 (Cell Signaling, Danvers, MA, USA), Col-1A, and GAPDH (Millipore, Billerica, MA, USA) antibodies were obtained.

Techniques: Quantitative Proteomics, Isolation, Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot, Control, Staining, Fluorescence, Microscopy, Software

TGF-β1 stimulates induction of Sar1a. HTSF and Sar1a siRNA- or a control siRNA (si-con)-transfected HTSF were cultured in 6-well plates, serum-starved for 16 h, and then treated with or without 10 ng/mL TGF-β1 or TGF-β1 + 10 μM TGF-β inhibitor (LY2109761) for 24 h. The cell culture supernatant was collected for PC-I ELISA (c and f), and cell lysates were immunoblotted with antibodies against the indicated proteins (a and d). (a) Immunoblots of Col-1A, Sar1a, and the loading control GAPDH. (b) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TGF-β-i; ## p < 0.01. (c) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β; ** p < 0.01. TGF-β1 vs TGF-β1 + TGF-β-i; ## p < 0.01. (d) Immunoblots of Col-1A, Sar1a, and the loading control GAPDH. (e) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TGF-β-i; ## p < 0.01. (f) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β; ** p < 0.01. TGF-β1 vs TGF-β1 + si-Sar1a; ## p < 0.01.

Journal: Open Medicine

Article Title: TGF-β1 upregulates Sar1a expression and induces procollagen-I secretion in hypertrophic scarring fibroblasts

doi: 10.1515/med-2022-0543

Figure Lengend Snippet: TGF-β1 stimulates induction of Sar1a. HTSF and Sar1a siRNA- or a control siRNA (si-con)-transfected HTSF were cultured in 6-well plates, serum-starved for 16 h, and then treated with or without 10 ng/mL TGF-β1 or TGF-β1 + 10 μM TGF-β inhibitor (LY2109761) for 24 h. The cell culture supernatant was collected for PC-I ELISA (c and f), and cell lysates were immunoblotted with antibodies against the indicated proteins (a and d). (a) Immunoblots of Col-1A, Sar1a, and the loading control GAPDH. (b) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TGF-β-i; ## p < 0.01. (c) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β; ** p < 0.01. TGF-β1 vs TGF-β1 + TGF-β-i; ## p < 0.01. (d) Immunoblots of Col-1A, Sar1a, and the loading control GAPDH. (e) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TGF-β-i; ## p < 0.01. (f) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β; ** p < 0.01. TGF-β1 vs TGF-β1 + si-Sar1a; ## p < 0.01.

Techniques: Control, Transfection, Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot

TAK1 is involved in TGF-β1-induced Sar1a expression. HTSF cultured in 6-well plates were serum-starved for 16 h, and they were then treated with or without 10 ng/mL TGF-β1, TGF-β1 + 10 μM SIS3, or TGF-β1 + 10 μM TAK1 inhibitor (EDHS-206) for 24 h. The cell culture supernatant was collected for PC-I ELISA (c and f), and cell lysates were immunoblotted with antibodies against the indicated proteins (a and d). (a) Immunoblots of Col-1A, Sar1a, phosphor-Smad3, Smad3, and GAPDH. (b) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1, ** p < 0.01. TGF-β1 vs TGF-β1 + Smad3-I; ## p < 0.01. (c) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + Smad3-I; ## p < 0.01. (d) Immunoblots of Col-1A, Sar1a, phosphor-TAK1, TAK1, and GAPDH as the loading control. (e) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TAK1-I; ## p < 0.01. (f) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TAK1-i; ## p < 0.01.

Journal: Open Medicine

Article Title: TGF-β1 upregulates Sar1a expression and induces procollagen-I secretion in hypertrophic scarring fibroblasts

doi: 10.1515/med-2022-0543

Figure Lengend Snippet: TAK1 is involved in TGF-β1-induced Sar1a expression. HTSF cultured in 6-well plates were serum-starved for 16 h, and they were then treated with or without 10 ng/mL TGF-β1, TGF-β1 + 10 μM SIS3, or TGF-β1 + 10 μM TAK1 inhibitor (EDHS-206) for 24 h. The cell culture supernatant was collected for PC-I ELISA (c and f), and cell lysates were immunoblotted with antibodies against the indicated proteins (a and d). (a) Immunoblots of Col-1A, Sar1a, phosphor-Smad3, Smad3, and GAPDH. (b) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1, ** p < 0.01. TGF-β1 vs TGF-β1 + Smad3-I; ## p < 0.01. (c) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + Smad3-I; ## p < 0.01. (d) Immunoblots of Col-1A, Sar1a, phosphor-TAK1, TAK1, and GAPDH as the loading control. (e) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TAK1-I; ## p < 0.01. (f) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + TAK1-i; ## p < 0.01.

Techniques: Expressing, Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot, Control

JNK and p38 are involved in TGF-β1-induced Sar1a expression. HTSF were cultured in 6-well plates, serum-starved for 16 h, and then treated with or without 10 ng/mL TGF-β1, TGF-β1 + 10 μM JNK inhibitor (SP600125), 50 μM ERK inhibitor (PD98059), or TGF-β1 + 10 μM p38 inhibitor (SB203580) for 24 h. The cell culture supernatant was collected for PC-I ELISA (c, f, and i), and cell lysates were immunoblotted with antibodies against the indicated proteins (a, d, and g). (a) Immunoblots of Col-1A, Sar1a, phosphor-JNK, JNK, and GAPDH as the loading control. (b) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + JNK-i; ## p < 0.01. (c) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + JNK-i; ## p < 0.01. (d) Immunoblots of Col-1A, Sar1a, phosphor-ERK, ERK, and GAPDH as the loading control. (e) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + ERK-I; # p < 0.05. (f) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. (g) Immunoblots of Col-1A, Sar1a, phosphor-p38, p38, and GAPDH as the loading control. (h) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + p38-I; ## p < 0.01. (i) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + p38-i; ## p < 0.01.

Journal: Open Medicine

Article Title: TGF-β1 upregulates Sar1a expression and induces procollagen-I secretion in hypertrophic scarring fibroblasts

doi: 10.1515/med-2022-0543

Figure Lengend Snippet: JNK and p38 are involved in TGF-β1-induced Sar1a expression. HTSF were cultured in 6-well plates, serum-starved for 16 h, and then treated with or without 10 ng/mL TGF-β1, TGF-β1 + 10 μM JNK inhibitor (SP600125), 50 μM ERK inhibitor (PD98059), or TGF-β1 + 10 μM p38 inhibitor (SB203580) for 24 h. The cell culture supernatant was collected for PC-I ELISA (c, f, and i), and cell lysates were immunoblotted with antibodies against the indicated proteins (a, d, and g). (a) Immunoblots of Col-1A, Sar1a, phosphor-JNK, JNK, and GAPDH as the loading control. (b) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + JNK-i; ## p < 0.01. (c) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + JNK-i; ## p < 0.01. (d) Immunoblots of Col-1A, Sar1a, phosphor-ERK, ERK, and GAPDH as the loading control. (e) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + ERK-I; # p < 0.05. (f) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. (g) Immunoblots of Col-1A, Sar1a, phosphor-p38, p38, and GAPDH as the loading control. (h) Fold change of Col-1A or Sar1a was calculated ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + p38-I; ## p < 0.01. (i) Secreted PC-I was determined via ELISA ( n = 3, ±SD). None vs TGF-β1; ** p < 0.01. TGF-β1 vs TGF-β1 + p38-i; ## p < 0.01.

Techniques: Expressing, Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot, Control

Journal: iScience

Article Title: Secretory defects in pediatric osteosarcoma result from downregulation of selective COPII coatomer proteins

doi: 10.1016/j.isci.2022.104100

Figure Lengend Snippet:

Article Snippet: Primary antibodies used were rabbit anti-GRP170 , rabbit anti-human BiP, kindly provided by Ineke Braakman (Utrecht University, Utrecht, Netherlands), rabbit anti-CHOP , mouse anti-HSC70 (Santa Cruz), mouse anti-SAR1A (Santa Cruz), rabbit anti-SEC24D (Cell Signaling), mouse anti-GAPDH (Millipore), rabbit anti-TIMP1 (Cell Signaling), and rabbit anti-vimentin (Abcam).

Techniques: Derivative Assay, Recombinant, Reverse Transcription, SYBR Green Assay, Labeling, Protease Inhibitor, Western Blot, Electron Microscopy, Sensitive Assay, Cloning, Proliferation Assay, Invasion Assay, RNA Sequencing, Software

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