CSF-1R Antibody (YA3685)(PBS only)

Cat. No.: HY-P83988A: Data Sheet COA
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CSF-1R Antibody (YA3685)(PBS only) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to CSF-1R.

For research use only. We do not sell to patients.

Size	Stock	Quantity
10 μL	In-stock	Estimated Time of Arrival: December 31
50 μL	In-stock	Estimated Time of Arrival: December 31
100 μL	In-stock	Estimated Time of Arrival: December 31
250 μL	Get quote

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
Documentation

Description

CSF-1R Antibody (YA3685)(PBS only) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to CSF-1R.

Host

Mouse

Clonality

Monoclonal

Molecular Weight

Predicted band size: 108 kDa;

Observed band size: 108 kDa

Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.

Species Reactivity

Human

SwissProt ID

P07333

Gene ID

1436 [NCBI]

Immunogen

Purified recombinant fragment of human CSF1R (AA: 344-497) expressed in E. Coli.

Application &
Dilution Ratio

Application	Dilution Ratio
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:200-1:1000
ICC/IF ICC/IF: Immunocytochemistry/Immunofluorescence	1:200-1:1000
ELISA ELISA: Enzyme Linked Immunosorbent Assay	1:10000

Purity	affinity purified.	Conjugation	Non-conjugated
Modification	Unmodified	Isotype	IgG2b

Appearance

Liquid

Formulation

Purified antibody in PBS only.

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Shipping

Shipping with blue ice.

Background

Function：Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. In adipocytes, inhibits lipolysis (By similarity)

Subcellular Localization：Cell membrane; Single-pass type I membrane protein; Late endosome; Lysosome

Expression：
Tissue_specificity:Both the long and short subtypes are primarily expressed in target tissues involved in insulin metabolism, including the liver, adipose tissue, and skeletal muscle, but are also expressed in peripheral nerves, kidneys, alveoli, pancreatic acini, placental vascular endothelial cells, fibroblasts, monocytes, granulocytes, erythrocytes, and skin. The short subtype is preferentially expressed in fetal cells (such as fetal fibroblasts) , muscle, liver, and kidneys. A heterozygous receptor for IGF1R is present in muscle, heart, kidneys, adipose tissue, skeletal muscle, liver cancer, fibroblasts, spleen, and placenta (at the protein level) . It is overexpressed in various tumors, including breast cancer, colon cancer, lung cancer, ovarian cancer, and thyroid cancer.

Isoforms & Post-Translational Modification：P06213 has 2 isomers: P06213-1: 156333 Da (predicted); P06213-2: 155146 Da (predicted).
After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane;Autophosphorylated on tyrosine residues in response to insulin (PubMed:14690593, PubMed:16246733, PubMed:16271887, PubMed:18278056, PubMed:18767165, PubMed:3166375, PubMed:9312016). Phosphorylation of Tyr-999 is required for binding to IRS1, SHC1 and STAT5B (PubMed:14690593, PubMed:16246733, PubMed:16271887, PubMed:18278056, PubMed:18767165, PubMed:3166375, PubMed:9312016). Dephosphorylated by PTPRE at Tyr-999, Tyr-1185, Tyr-1189 and Tyr-1190 (PubMed:14690593, PubMed:16246733, PubMed:16271887, PubMed:18278056, PubMed:18767165, PubMed:3166375, PubMed:9312016). May also be phosphorylated at Tyr-1185 and Tyr-1190 by mTORC2 (PubMed:26584640). Dephosphorylated by PTPRF and PTPN1 (PubMed:8995282). Dephosphorylated by PTPN2; down-regulates insulin-induced signaling (PubMed:10734133, PubMed:12612081). Dephosphorylation at Tyr-1189 and Tyr-1190 requires the SH2/SH3 adapter protein NCK1, probably to recruit its interaction partner PTPN1 (PubMed:21707536);S-nitrosylation at Cys-1083 by BLVRB inhibits the receptor tyrosine kinase, thereby inhibiting insulin signaling;Ubiquitinated by MARCHF1; leading to degradation thereby reducing surface INSR expression

Subunit：Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains carry the insulin-binding regions, while the beta chains carry the kinase domain.

Synonyms

FMS; CSFR; FIM2; HDLS; C-FMS; CD115; CSF-1R; M-CSF-R

Documentation

Select Batch:

Data Sheet (235 KB) SDS (251 KB)

COA (205 KB)

User Guide for Antibodies (1077 KB)