Product: Crk p38 Antibody
Catalog: AF6323
Description: Rabbit polyclonal antibody to Crk p38
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Bovine, Horse, Sheep, Dog, Chicken, Xenopus
Mol.Wt.: 40kDa; 34kD(Calculated).
Uniprot: P46108
RRID: AB_2835181

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 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Crk p38 Antibody detects endogenous levels of total Crk p38.
Cite Format: Affinity Biosciences Cat# AF6323, RRID:AB_2835181.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


Adapter molecule crk; Avian sarcoma virus CT10 (v crk) oncogene homolog; CRK; CRK isoform 2; CRK isoform II; CRK_HUMAN; CRKII; FLJ38130; OTTHUMP00000115366; OTTHUMP00000198330; p38; Proto oncogene C crk; Proto-oncogene C-crk; v crk avian sarcoma virus CT10 oncogene homolog; v crk sarcoma virus CT10 oncogene homolog; v crk sarcoma virus CT10 oncogene homolog (avian);


Crk an adaptor protein with an SH2-SH3-SH3 domain structure. Recruits cytoplasmic proteins through SH2-phospho-tyrosine interaction. Phosphorylated by Abl, IGF-IR and EGFR.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P46108 As Substrate

Site PTM Type Enzyme
A2 Acetylation
S40 Phosphorylation
S41 Phosphorylation Q13153 (PAK1)
T42 Phosphorylation
S43 Phosphorylation
Y47 Phosphorylation
S74 Phosphorylation
S83 Phosphorylation
S85 Phosphorylation
S96 Phosphorylation
Y108 Phosphorylation
T111 Phosphorylation
T112 Phosphorylation
T113 Phosphorylation
S121 Phosphorylation
R122 Methylation
S125 Phosphorylation
Y136 Phosphorylation
K154 Acetylation
S175 Phosphorylation
Y190 Phosphorylation
S194 Phosphorylation
S196 Phosphorylation
S198 Phosphorylation
S208 Phosphorylation
Y221 Phosphorylation P00519 (ABL1) , P00533 (EGFR) , A0A173G4P4 (Abl fusion) , P08069 (IGF1R) , P42684 (ABL2)
S225 Phosphorylation
T228 Phosphorylation
Y239 Phosphorylation P00519 (ABL1)
Y251 Phosphorylation P00519 (ABL1)
K253 Acetylation
T254 Phosphorylation
S304 Phosphorylation

PTMs - P46108 As Enzyme

Substrate Site Source
Q05397-1 (PTK2) Y397 Uniprot

Research Backgrounds


Regulates cell adhesion, spreading and migration. Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.


Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. Isoform Crk-II is phosphorylated by KIT.

Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.

Proline isomerization at Pro-237 by PPIA acts as a switch between two conformations: an autoinhibitory conformation in the cis form, where the tandem SH3 domains interact intramolecularly, and an activated conformation in the trans form.

Subcellular Location:

Cytoplasm. Cell membrane.
Note: Translocated to the plasma membrane upon cell adhesion.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Interacts with ABL1, C3G, DOCK3, DOCK5, MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2 domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced tyrosine phosphorylation. Interacts (via SH2 domain) with several tyrosine-phosphorylated growth factor receptors such as EGFR and INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent. Interacts with EPHA3 (phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated). Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with CBLC. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases.


The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.

The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB.

Belongs to the CRK family.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > ErbB signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Bacterial > Shigellosis.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Human Diseases > Cancers: Specific types > Renal cell carcinoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Chronic myeloid leukemia.   (View pathway)

· Organismal Systems > Immune system > Chemokine signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Fc gamma R-mediated phagocytosis.   (View pathway)

· Organismal Systems > Nervous system > Neurotrophin signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Insulin signaling pathway.   (View pathway)


1). Protective effect of remdesivir against pulmonary fibrosis in mice. Frontiers in Pharmacology, 2021 (PubMed: 34512328) [IF=5.6]

Application: WB    Species: Mice    Sample: lung tissues

FIGURE 6 Remdesivir inhibits TGF-β1-induced activation of Smad and non-Smad signaling pathway in lung fibroblasts (A) Luciferase assays of CAGA-NIH3T3 cells. Cells were pretreated with Remdesivir (0–50 μM) for 30 min and then incubated with TGF-β1 (5 ng ml−1) for 24 h, then analyzed with luciferase assay. SB431542 is a TGF-β1/Smad pathway inhibitor and serves as a positive control (B) NIH-3T3 cells were co-treated with TGF-β1 (5 ng ml−1) and Remdesivir (12.5, 25, 50 μM) for 1 h. P-Smad3 and Smad3 were assessed using western blot. GAPDH was used as the internal control (C) PPF cells were co-treated with TGF-β1 (5 ng ml−1) and Remdesivir (12.5, 25, 50 μM) for 1 h. P-Smad3 and Smad3 were assessed using western blot. GAPDH was used as the internal control (D) NIH-3T3 cells were co-treated with TGF-β1 (5 ng ml−1) and Remdesivir (12.5, 25, 50 μM) for 1 h and the phosphorylation levels of P-38, JNK, ERK and Akt were analyzed by Western blot. β-tubulin was used as a loading control in grayscale analysis. Scale bar = 60 μm. Data was presented as the means ± SD, n = 3. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

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